Original Article
Safety and Efficacy of Recombinant Human α-Galactosidase A Replacement Therapy in Fabry's Disease
N Engl J Med 2001; 345:9-16July 5, 2001
- Abstract
Background
Fabry's disease, lysosomal α-galactosidase A deficiency, results from the progressive accumulation of globotriaosylceramide and related glycosphingolipids. Affected patients have microvascular disease of the kidneys, heart, and brain.
Methods
We evaluated the safety and effectiveness of recombinant α-galactosidase A in a multicenter, randomized, placebo-controlled, double-blind study of 58 patients who were treated every 2 weeks for 20 weeks. Thereafter, all patients received recombinant α-galactosidase A in an open-label extension study. The primary efficacy end point was the percentage of patients in whom renal microvascular endothelial deposits of globotriaosylceramide were cleared (reduced to normal or near-normal levels). We also evaluated the histologic clearance of microvascular endothelial deposits of globotriaosylceramide in the endomyocardium and skin, as well as changes in the level of pain and the quality of life.
Results
In the double-blind study, 20 of the 29 patients in the recombinant α-galactosidase A group (69 percent) had no microvascular endothelial deposits of globotriaosylceramide after 20 weeks, as compared with none of the 29 patients in the placebo group (P<0.001). Patients in the recombinant α-galactosidase A group also had decreased microvascular endothelial deposits of globotriaosylceramide in the skin (P<0.001) and heart (P<0.001). Plasma levels of globotriaosylceramide were directly correlated with clearance of the microvascular deposits. After six months of open-label therapy, all patients in the former placebo group and 98 percent of patients in the former recombinant α-galactosidase A group who had biopsies had clearance of microvascular endothelial deposits of globotriaosylceramide. Mild-to-moderate infusion reactions (i.e., rigors and fever) were more common in the recombinant α-galactosidase A group than in the placebo group.
Conclusions
Recombinant α-galactosidase A replacement therapy cleared microvascular endothelial deposits of globotriaosylceramide from the kidneys, heart, and skin in patients with Fabry's disease, reversing the pathogenesis of the chief clinical manifestations of this disease.
Media in This Article
Figure 2
Median Plasma Concentrations of Globotriaosylceramide in the Recombinant α-Galactosidase A Group and the Placebo Group in the Double-Blind Study and the Open-Label Study.Figure 1
Change in Levels of Pain from Base Line to Week 20 of the Double-Blind Study in the Recombinant α-Galactosidase A Group (Panel A) and the Placebo Group (Panel B).Article Activity
- Article
Fabry's disease is an X-linked inborn error of glycosphingolipid catabolism due to deficient lysosomal α-galactosidase A activity.1 In patients with the classic form of the disease, progressive accumulation of globotriaosylceramide and related glycosphingolipids in vascular endothelial lysosomes of the kidneys, heart, skin, and brain leads to the main disease manifestations. The clinical onset is in childhood and is characterized by severe acroparesthesias, angiokeratoma, corneal and lenticular opacities, and hypohidrosis. Over time, microvascular disease of the kidneys, heart, and brain progresses, leading to early death.1 Treatment is limited to symptomatic management of pain and the end-stage complications of renal failure, cardiac disease, and strokes.
Early trials demonstrated the feasibility of enzyme replacement to correct the metabolic defect in Fabry's disease.2-4 A phase 1 trial demonstrated reductions of globotriaosylceramide in the liver and in urinary sediment with a single dose of recombinant α-galactosidase A.5 A phase 1 and 2 open-label dose-escalation study of replacement therapy with recombinant α-galactosidase A in 15 male patients with classic Fabry's disease demonstrated that repeated administration (a total of five infusions) was safe and effective in clearing plasma globotriaosylceramide and microvascular endothelial deposits of globotriaosylceramide from target tissues.6 Plasma and tissue clearance of globotriaosylceramide was observed for all dose regimens, and the effect was most pronounced at higher doses. Therefore, we evaluated the safety and efficacy of recombinant α-galactosidase A replacement therapy in Fabry's disease in a multicenter, randomized, double-blind, placebo-controlled trial and subsequent open-label study.
Methods
Patients
Eligible patients had an enzymatically confirmed diagnosis of classic Fabry's disease, had a level of activity of α-galactosidase A of less than 1.5 nmol per hour per milliliter in plasma or less than 4 nmol per hour per milligram in leukocytes,7 and were at least 16 years old. Patients were excluded if their serum creatinine concentration exceeded 2.2 mg per deciliter (194.5 μmol per liter), if they were undergoing dialysis, or if they had undergone kidney transplantation.
Clinical and Biochemical Assessments
Evaluations including a medical history taking, routine chemical analyses, and hematologic indexes were obtained and a physical examination was performed at base line and before each infusion. Echocardiograms were obtained and plasma and 24-hour urinary sediments were collected at base line, after week 20 of the double-blind study, and after six months of open-label treatment. Glomerular filtration rates were measured in terms of inulin clearance at base line and after six months of the extension study. Concentrations of globotriaosylceramide in plasma, tissue, and urinary sediment8 were determined by a quantitative enzyme-linked immunosorbent assay (ELISA).9 Before each infusion, the presence or absence of antibody against recombinant α-galactosidase A was assessed by ELISA, and the results were confirmed by a radioimmunoprecipitation assay.10
Study Protocol
Enrollment in the double-blind study began on March 22, 1999, and ended on December 3, 1999. The open-label study began on October 26, 1999. Patients were randomly assigned to receive recombinant α-galactosidase A (agalsidase beta; Fabrazyme, Genzyme, Cambridge, Mass.) at a dose of 1 mg per kilogram of body weight or placebo (phosphate-buffered mannitol). Both agents were administered intravenously at a rate of 0.25 mg per minute every other week for 20 weeks (for a total of 11 infusions). Before each infusion patients were pretreated with 1000 mg of acetaminophen and 25 to 50 mg of hydroxyzine. Ibuprofen, prednisone, or both were also used in a few patients for infusion-related reactions. After the double-blind trial, all patients received recombinant α-galactosidase A in an open-label fashion at a dose of 1 mg per kilogram every other week, but the infusion rates were increased as tolerated, reducing the length of the infusion. The institutional review boards at all sites approved the double-blind and open-label protocols, and all patients gave written informed consent.
Tissue Assessments
Kidney specimens were obtained by ultrasound-guided biopsy, heart specimens were obtained through an endomyocardial catheter with the use of a bioptome, and 3-mm skin specimens were obtained by punch biopsy at base line, after infusion 11 (week 20), and after six months of the open-label study. Tissue sections (1 μm) were stained with methylene blue–azure II. Each of the three types of biopsy specimen was assessed for microvascular endothelial deposits of globotriaosylceramide by a different group of three pathologists. None of the nine pathologists were aware of the patients' treatment assignments or the times at which the specimens were obtained.
Specimens with no microvascular endothelial deposits of globotriaosylceramide or only trace amounts (normal or nearly normal) were given a score of 0; specimens in which the majority of vessels had evidence of a single endothelial inclusion were given a score of 1; specimens that contained multiple vessels with multiple sites of single or multiple inclusions were given a score of 2; and specimens that had large accumulations of inclusions with some clusters at the juxtanuclear region and around cytoplasmic borders and bulging of the vessel lumens were given a score of 3. Renal-biopsy specimens that were initially given a score of 0 or 1 were reevaluated by the three renal pathologists with the use of a slightly modified scoring system. In this system, specimens with no inclusions were given a score of 0; those with one small granule (approximately 0.2 μm) were designated as having trace evidence; those with multiple discrete granules were given a score of 1; those with single or multiple aggregates of granules were given a score of 2; and those with aggregates of granules within the endothelium that caused the distortion of the luminal endothelial cell surface were given a score of 3.
Evaluation of Efficacy
An average of 233 capillaries in each renal-biopsy specimen were assessed by each renal pathologist. The primary efficacy end point of the double-blind study required more than 50 percent of the renal interstitial capillaries in each specimen to have a score of 0, less than 5 percent to have a score of 1 or greater, and the remainder to be designated as having trace evidence of microvascular endothelial deposits of globotriaosylceramide after week 20. For each biopsy specimen, a majority score was determined from the three pathologists' scores.
Secondary end points were also assessed at base line and after the week-20 infusion and consisted of the composite score for microvascular endothelial deposits of globotriaosylceramide in the heart, kidney, and skin specimens (scores were calculated per organ and summed for all organs) and the change from base line in the concentrations of globotriaosylceramide in urinary sediment and kidney specimens and the level of pain, as assessed by the short form of the McGill Pain Questionnaire.11 Scores on this questionnaire can range from 0 to 45, with higher scores indicating severe pain intensity.
Statistical Analysis
We used chi-square tests to analyze the proportion of patients in the recombinant α-galactosidase A group and the placebo group with a renal-biopsy score of 0 after week 20 of the double-blind study and after six months of the open-label study. We used two-sample, two-tailed tests for all analyses. A P value of 0.05 or less was considered to indicate statistical significance. Changes in the concentrations of globotriaosylceramide in urinary sediment and kidney specimens on ELISA were ranked individually, and the rank-sum score for each patient was obtained. We used a two-sample Wilcoxon rank-sum test to assess the change from base line to the end of the double-blind study (after week 20). We used t-tests to compare the mean change in the level of pain from base line to the end of the double-blind study (after week 20) for each treatment group. The Genzyme Biostatistics group held the data and analyzed the data, with the help of consulting academic biostatisticians.
We used the 36-item Medical Outcomes Study Short-Form General Health Survey (SF-36)12 to evaluate the patients' quality of life. This multi-item scale measures eight health-related aspects: physical function, social function, physical role, emotional role, mental health, energy, pain, and general health perception. Scores on each aspect can range from 0 (worst) to 100 (best). The results were evaluated according to established guidelines,12 and we used a Wilcoxon signed-rank test to compare the mean change in scores from base line in each group. We used an analysis of variance to compare the differences between groups in the changes in the mean glomerular filtration rate from base line to six months of the open-label study.
Results
Characteristics of the Patients
The base-line characteristics of the 58 patients assigned to the two treatment groups were similar (Table 1Table 1
Base-Line Characteristics of the Patients.).Double-Blind Study
Renal Capillary Endothelial Clearance of Globotriaosylceramide
The primary efficacy end point was the percentage of patients in each group who were free of microvascular endothelial deposits of globotriaosylceramide in renal-biopsy specimens (i.e., who had a score of 0) after 20 weeks of treatment (11 infusions) in the double-blind study. The end point was reached by 20 of the 29 patients in the recombinant α-galactosidase A group (69 percent), as compared with none of the 29 patients in the placebo group (P<0.001; odds ratio, 0.0). Eight of the remaining nine patients in the recombinant α-galactosidase A group had a score of 1 (the scores of six of these patients had improved, and the scores of two had not changed). The ninth patient had a missing biopsy specimen and so was assigned a score of 3. An analysis of sensitivity, in which a maximum of 1 percent of the capillaries could be given a score of 1 or greater, as opposed to the original requirement of less than or equal to 5 percent, did not change the outcome (P<0.005). These results for the three renal pathologists were uniform.
Secondary End Points
The individual scores for the kidney-, heart-, and skin-biopsy specimens as well as the composite scores for all three types of specimens were compared at base line and after the week-20 infusion (Table 2Table 2
Mean Changes in Individual and Composite Scores for Microvascular Endothelial Deposits of Globotriaosylceramide in Kidney-, Heart-, and Skin-Biopsy Specimens from Base Line to after the Week-20 Infusion.). Although both groups had similar base-line scores for each type of specimen (P=0.53), the patients in the recombinant α-galactosidase A group had significantly lower scores for each type of specimen after the week-20 infusion than did the patients in the placebo group (P<0.001 for all three comparisons). In addition, the median percent changes in the kidney and urinary concentrations of globotriaosylceramide differed between the patients in the recombinant α-galactosidase A group and the patients in the placebo group (23.3 percent decrease vs. 42.8 percent increase and 34.1 percent decrease vs. 6.2 percent decrease, respectively). The rank-sum scores for kidney and urinary-sediment concentrations of globotriaosylceramide had decreased significantly in the recombinant α-galactosidase A group, but not in the placebo group (median change, 32.5 percent decrease vs. 48.0 percent decrease; P=0.003).Although both groups had low scores on all five scales of the short form of the McGill Pain Questionnaire at base line, statistically significant decreases in the scores were observed at week 20 in both treatment groups (Figure 1Figure 1
Change in Levels of Pain from Base Line to Week 20 of the Double-Blind Study in the Recombinant α-Galactosidase A Group (Panel A) and the Placebo Group (Panel B).). There was no significant difference between groups after week 20 in any pain assessment (P>0.05 for all comparisons), possibly because of a placebo effect.Clearance of Globotriaosylceramide in Plasma
Figure 2Figure 2
Median Plasma Concentrations of Globotriaosylceramide in the Recombinant α-Galactosidase A Group and the Placebo Group in the Double-Blind Study and the Open-Label Study. shows clearance of globotriaosylceramide from plasma by week 14 of treatment with recombinant α-galactosidase A; in contrast, the plasma concentrations in the placebo group did not change significantly during the double-blind study (P<0.001 for the comparison between the groups). Plasma concentrations of globotriaosylceramide were undetectable (<1.2 ng per microliter) after week 20 in all 20 patients who had no microvascular endothelial deposits of globotriaosylceramide in renal-biopsy specimens after week 20 of treatment. Five of eight patients in the recombinant α-galactosidase A group who had a renal score of 1 after week 20 had undetectable plasma concentrations of globotriaosylceramide after week 20, and three had concentrations ranging from 12 to 94 percent (mean, 35.3 percent) of their base line values. The patient who had been assigned a score of 3 because of a missing biopsy specimen at week 20 had a plasma globotriaosylceramide concentration of 3.9 ng per microliter.Quality of Life
Patients in the recombinant α-galactosidase A group had significant improvements in two components of the SF-36 (physical role and emotional role), whereas patients in the placebo group had significant improvements in the physical role and body-pain components of the SF-36.
Open-Label Extension Study
All 58 patients enrolled in the open-label study. After six months of treatment with recombinant α-galactosidase A, 98 percent of patients in whom a biopsy was performed at this time (42 of 43) had a score of 0 on histologic analysis of microvascular endothelial deposits of globotriaosylceramide in kidney specimens, 96 percent (45 of 47) had such results for skin specimens, and 75 percent (24 of 32) had such results for heart specimens (Table 3Table 3
Number of Patients with a Score of 0 on Histologic Analysis of Microvascular Capillary Endothelial Deposits of Globotriaosylceramide in Biopsy Specimens after 20 Weeks of Double-Blind Treatment and 6 Months of Open-Label Treatment with Recombinant α-Galactosidase A.). The results were similar when the analysis included only the patients who crossed over from placebo to recombinant α-galactosidase A: 100 percent, 96 percent, and 67 percent, respectively. In 95 percent of the patients who had had a biopsy during the open-label study and who received recombinant α-galactosidase A during the double-blind study, the renal scores were maintained or further decreased after six months of open-label treatment. In addition, renal function, as measured by the glomerular filtration rate, did not change substantially from base line in either group after week 20 of the double-blind study (P=0.19) or after six months of open-label treatment (P=0.81).Safety
No significant changes from base line in the echocardiograms, electrocardiograms, or other safety assessments in either group were observed after week 20 of the double-blind study or after six months of the open-label study. The infusions were generally well tolerated. Rigors and fever were the only treatment-related adverse events that occurred significantly more frequently in the recombinant α-galactosidase A group than in the placebo group during the double-blind study (P=0.004) (Table 4Table 4
Adverse Events That Occurred in at Least 10 Percent of Patients in the Recombinant α-Galactosidase A Group during the Double-Blind Study.). Although not considered to be related to recombinant α-galactosidase A therapy, skeletal pain was the only other adverse event that occurred more frequently among enzyme-treated patients during the double-blind study (P=0.02). Transient mild-to-moderate infusion-associated reactions occurred in 59 percent of patients (34 of 58) during double-blind or open-label treatment. Reducing the infusion rate, administering preventive medications, or both measures controlled these reactions. A single patient had a positive skin test to recombinant α-galactosidase A after his eighth infusion during the open-label study, and treatment was discontinued.IgG seroconversion occurred in 51 of the 58 patients who received recombinant α-galactosidase A (88 percent) during the study. Seroconversion did not affect the primary or secondary efficacy end points. For example, the distribution of the scores for renal specimens (0 vs. not 0) did not differ significantly between patients who did seroconvert and those who did not. In addition, 8 of 29 patients in the original recombinant α-galactosidase A group who had renal scores of 1 after week 20 had a reduction in their scores to 0 during the open-label study. IgG titers had decreased in 15 of 26 patients in the recombinant α-galactosidase A group (58 percent) who seroconverted during the double-blind study when the titers were assessed after 12 months of treatment. In addition, one IgG-positive patient with a low titer became seronegative during this period. These observations serve to reduce concern about potential reactions associated with seroconversion.
Discussion
During the past decade the safety and effectiveness of enzyme-replacement therapy have been demonstrated in patients with type 1 Gaucher's disease.13,14 In patients with this lysosomal storage disease, the infusion of human placental or recombinant acid β-glucosidase metabolized the accumulated substrate, reversed the disease-related abnormalities, and markedly improved the quality of life.13,14 We report the results of a randomized, double-blind, placebo-controlled trial and the first six months of an open-label extension study that demonstrate the safety and effectiveness of enzyme replacement in a second lysosomal disorder, Fabry's disease.
In patients with classic Fabry's disease, the chief debilitating manifestations result primarily from the progressive accumulation of microvascular endothelial deposits of globotriaosylceramide, leading to ischemia and infarction, particularly in the kidneys, heart, and brain.1 In contrast, patients with the cardiac variant of the disease have residual α-galactosidase A activity (<10 percent of normal levels) and do not have vascular endothelial accumulation of glycosphingolipid.1,15,16 In these patients, left ventricular hypertrophy and mild proteinuria typically develop late in life, the life span is normal, and the classic manifestations of the disease, including angiokeratoma, acroparesthesias, hypohidrosis, and renal failure, are absent.1 Thus, the reversal of the underlying vascular endothelial abnormalities in patients with classic Fabry's disease should be therapeutic.
We found that 11 infusions of recombinant α-galactosidase A at a dose of 1 mg per kilogram over a 20-week period safely and effectively cleared the abnormalities in the capillary endothelium of the kidneys, heart, and skin of patients with classic Fabry's disease. The primary efficacy end point of our study directly addressed a fundamental cause of the most common and devastating feature of classic Fabry's disease: renal failure. After 20 weeks of treatment, complete or almost complete clearance of the accumulated renal microvascular endothelial deposits of globotriaosylceramide was achieved in 69 percent of the patients in the recombinant α-galactosidase A group, as compared with none of the patients in the placebo group (P<0.001). In addition, the concentration of globotriaosylceramide was significantly reduced in the urinary sediment of patients in the recombinant α-galactosidase A group, providing indirect evidence of the clearance of glycosphingolipids in renal tubules. Similar results were achieved with respect to the clearance of microvascular endothelial deposits of globotriaosylceramide from the heart (P<0.001) and skin (P<0.001).
The open-label extension study confirmed the results of the double-blind study and demonstrated that clearance was maintained or that microvascular endothelial deposits of globotriaosylceramide were further reduced in all three types of specimens assessed in patients who were treated with recombinant α-galactosidase A for about one year. Notably, the percentage of patients with clearance of the microvascular endothelial deposits of globotriaosylceramide in the endomyocardium increased from 67 percent after 20 weeks to 82 percent after 6 months of open-label treatment, indicating that the clearance of globotriaosylceramide may be tissue specific, depending on the dose and duration of treatment, the level of enzyme uptake, and the degree of substrate accumulation. Taken together, the results of the double-blind and open-label studies confirm that recombinant α-galactosidase A replacement therapy cleared the accumulated microvascular endothelial deposits of globotriaosylceramide and reversed the chief underlying abnormality in Fabry's disease. On the basis of the results of the preclinical,17 phase 1 and 2 dose-escalation,6 and double-blind studies, the plasma globotriaosylceramide level may be correlated with the accumulation of this glycosphingolipid in tissue and may provide a noninvasive indicator of systemic substrate clearance, analogous to serum glucose levels in patients with diabetes.
Most patients with the classic form of the disease have episodic acroparesthesias that are debilitating and markedly impair their quality of life. Patients in a phase 1 and 2 open-label study reported decreased severity of pain related to Fabry's disease.6 In our double-blind study, the severity of pain and the quality of life, as assessed by standardized instruments, were significantly improved in both groups, making it impossible to differentiate treatment-related effects from a placebo effect. For ethical reasons, patients who had been dependent on prophylactic drugs, analgesics, or both for years continued to take such medications during the study, a factor that may have minimized base-line scores and subsequent differences between groups. Studies are needed to determine the long-term effects of treatment with recombinant α-galactosidase A, perhaps with the use of instruments specifically designed to assess pain related to Fabry's disease and quality-of-life issues.
In general, the infusions were well tolerated, and all 58 patients completed the double-blind trial and entered the open-label study. The possibility of infusion-related reactions was anticipated, since patients with classic Fabry's disease have no detectable α-galactosidase A activity, protein, or both.1 Therefore, we purposely kept the infusion rates slow to maintain blinding, and we administered prophylactic medications to all patients to minimize any infusion-related reactions. During the open-label study, we increased the infusion rates, and in the case of many patients, the infusion lasted two hours. In 88 percent of patients, IgG antibodies against recombinant α-galactosidase A developed; however, seroconversion did not affect primary or secondary efficacy results, nor did the antibodies have a neutralizing effect, as occurs in patients with hemophilia A in whom inhibitors develop.18,19 After approximately one year of treatment with recombinant α-galactosidase A, IgG titers had decreased in 58 percent of patients with seroconversion and became undetectable in one patient. On the basis of previous experience with long-term enzyme-replacement therapy,10,20 such findings suggest that immunologic tolerance may develop in these patients.
In conclusion, we found that a dose of 1 mg of recombinant α-galactosidase A per kilogram every other week for about six months to one year safely and effectively reversed the accumulation of microvascular endothelial deposits of globotriaosylceramide in the kidneys, heart, and skin. Continued treatment may be required to reduce the deposition of glycosphingolipids in other types of cells, to which less enzyme is delivered,17 particularly renal tubular epithelial cells, podocytes, and cardiomyocytes. Further experience will determine effective regimens for initial reversal and subsequent control of the accumulated glycosphingolipids in the capillary endothelium and other types of cells.
Supported in part by a Merit Award from the National Institutes of Health (5 R37 DK34045), by grants from the National Institutes of Health (5 M01 RR00071 and 5 M01 RR00425, to the General Clinical Research Centers at the Mount Sinai School of Medicine and Cedars–Sinai Medical Center, and 5 P30 HD28822, to the Mount Sinai Child Health Research Center), and by a grant from Genzyme Corporation.
Dr. Desnick has received grant support from and serves as a consultant to Genzyme.
We are indebted to the patients who participated in the study and to the outstanding nursing staffs of the General Clinical Research Centers at all the investigational sites.
Source Information
From the Mount Sinai School of Medicine, New York (C.M.E., R.J.D.); Hôpital Edouard Herriot, Lyons, France (N.G.); Cedars–Sinai Burns and Allen Research Institute, UCLA School of Medicine, Los Angeles (W.R.W.); Hôpital Européen Georges Pompidou, Paris (D.P.G.); University College London Hospitals, London (P.L.); Hope Hospital, Salford, Manchester, United Kingdom (S.W.); Beth Israel Deaconess Medical Center, Boston (L.C.); and Academisch Medisch Centrum, Amsterdam (G.E.L.).
Address reprint requests to Dr. Desnick at the Department of Human Genetics, Box 1498, Mount Sinai School of Medicine, Fifth Ave. at 100th St., New York, NY 10029, or at rjd.fabry@mssm.edu.
Appendix
In addition to the authors, the following members of the International Collaborative Fabry Disease Study Group participated in the study: Investigators — M. Banikazemi, J. Ibraham, and A.P. Cheng (New York); L.J. Raffel (Los Angeles); P. Cochat (Lyons, France); M. Azizi and X. Jeunemaitre (Paris); A. Vellodi (London); J.E. Wraith (Manchester, United Kingdom); C.J. Chaves, K.B. Kanis, I. Linfante, and R. Llinas (Boston); D.K. Bosman, H.S.A. Heymans, C.E.M. Hollak, and F.A. Wijburg (Amsterdam); Expert pathologists — Kidney: R.B. Colvin (Boston); S. Dikman (New York), and H. Rennke (Boston); Heart: H.T. Aretz (Boston), J. Fallon (New York), and R. Mitchell (Boston); Skin: H.R. Beyers and S. Granler (Boston) and R. Phelps (New York); and General Pathology: R.E. Gordon (New York); Specialty consultants — S. Brodie, S.A. Gass, M. Goldman, D. Mehta, and J. Winston (New York); R. Bouvier, B.P. Denis, L. Dubourg, A. Fouilhoux, A. Hadj-Aïssa, M. Laville, I. Maire, B. Ranchin, and M.T. Vanier (Lyons, France); A. Hickey, J. Jordan, S. Jordan, S.S. Khan, and E. Maguen (Los Angeles); C. Amrein, B. Diebold, J.N. Fiessinger, M. Froissart, J.P. Grunfeld, J. Julien, L.H. Noel, C. Orssaud, and L. Poenaru (Paris); M.H. Griffiths, D. Holdright, N. Phelps-Brown, S. Sporton, R. Woolfson, V.C. Worthington, and E.P. Young (London); M. Bhushan, A. Cooper, E. O'Riordan, R. Radford, S.G. Ray, and R.S. Reeve (Manchester, United Kingdom); F.G. Berson, M.S. Kruskall, and W.J. Manning (Boston); W.J.W. Bos, D.K. Bosman, F.J.W. ten Kate, R.T. Krediet, K.I. Lie, J.J. Piek, L.J.J.M. Prick, and J.H.S. Smitt (Amsterdam); Study coordinators and nurses — M. Nunn, A. Nieto, R.A. Denchy, and A. Kowalski (New York); J. Exantus, M.T. Dupret, S. Garnier, and S. Walbilic (Lyons, France); A.G. Verne and B. Williams (Los Angeles); M.C. Bernard and V. Remones (Paris); J. Morrison, D.G. Burke, L.G. Fulford, M. Jackson, R. Lobo, S. Sporton, and V.C. Worthington (London); B.M. Kenny (Manchester, United Kingdom); L. Baron (Boston); A. Vyth (Amsterdam); Genzyme personnel — R. Moscicki, T. Braakman, M. Goldberg, M. O'Callaghan, R. Cintron, S. Richards, P.K. Tandon, M.A. Fitzpatrick, M. Yelmene, and M. Nichols.
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Citing Articles
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Gustavo Saposnik, Sylvain Lanthier, Muhammad Mamdani, Kevin E. Thorpe, Magda Melo, Karen Pope, Daniel Selchen, David F. Moore, , . (2012) Fabry's disease: A prospective multicenter cohort study in young adults with cryptogenic stroke. International Journal of Stroken/a-n/a
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Elfrida R Benjamin, Richie Khanna, Adriane Schilling, John J Flanagan, Lee J Pellegrino, Nastry Brignol, Yi Lun, Darlene Guillen, Brian E Ranes, Michelle Frascella, Rebecca Soska, Jessie Feng, Leo Dungan, Brandy Young, David J Lockhart, Kenneth J Valenzano. (2012) Co-administration With the Pharmacological Chaperone AT1001 Increases Recombinant Human α-Galactosidase A Tissue Uptake and Improves Substrate Reduction in Fabry Mice. Molecular Therapy
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Satoshi ISHII. (2012) Pharmacological chaperone therapy for Fabry disease. Proceedings of the Japan Academy, Series B 88:1, 18-30
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Miguel Ángel Barba Romero, Alberto Rivera Gallego, Guillem Pintos Morell. (2012) Comparación de los pacientes de un registro español de enfermedad de Fabry en dos periodos de tiempo. Medicina Clínica
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Thomas P Mechtler, Susanne Stary, Thomas F Metz, Víctor R De Jesús, Susanne Greber-Platzer, Arnold Pollak, Kurt R Herkner, Berthold Streubel, David C Kasper. (2012) Neonatal screening for lysosomal storage disorders: feasibility and incidence from a nationwide study in Austria. The Lancet 379:9813, 335-341
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Caterina Porto, Antonio Pisani, Margherita Rosa, Emma Acampora, Valeria Avolio, Maria Rosaria Tuzzi, Bianca Visciano, Cristina Gagliardo, Serena Materazzi, Giancarlo Marca, Generoso Andria, Giancarlo Parenti. (2011) Synergy between the pharmacological chaperone 1-deoxygalactonojirimycin and the human recombinant alpha-galactosidase A in cultured fibroblasts from patients with Fabry disease. Journal of Inherited Metabolic Disease
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Max J. Hilz, Julia Koehn, Edwin H. Kolodny, Miroslaw Brys, Sebastian Moeller, Brigitte Stemper. (2011) Metronomic breathing shows altered parasympathetic baroreflex function in untreated Fabry patients and baroreflex improvement after enzyme replacement therapy. Journal of Hypertension 29:12, 2387-2394
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Robin H. Lachmann. (2011) Enzyme replacement therapy for lysosomal storage diseases. Current Opinion in Pediatrics 23:6, 588-593
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Abigail I. Guce, Nathaniel E. Clark, Jerome J. Rogich, Scott C. Garman. (2011) The Molecular Basis of Pharmacological Chaperoning in Human α-Galactosidase. Chemistry & Biology 18:12, 1521-1526
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William R. Wilcox, Gabor E. Linthorst, Dominique P. Germain, Ulla Feldt-Rasmussen, Stephen Waldek, Susan M. Richards, Dana Beitner-Johnson, Marta Cizmarik, Alex Cole, Wytske Kingma, David G. Warnock. (2011) Anti-α-galactosidase A antibody response to agalsidase beta treatment: Data from the Fabry registry. Molecular Genetics and Metabolism
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Ulla Feldt-Rasmussen, Robert Dobrovolny, Irina Nazarenko, Martin Ballegaard, Lis Hasholt, Åse K. Rasmussen, Erik I. Christensen, Soren S. Sorensen, Flemming Wibrand, Robert J. Desnick. (2011) Diagnostic dilemma: A young woman with Fabry disease symptoms, no family history, and a “sequencing cryptic” α-galactosidase a large deletion. Molecular Genetics and Metabolism 104:3, 314-318
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A. M. From, J. J. Maleszewski, C. S. Rihal. (2011) Current Status of Endomyocardial Biopsy. Mayo Clinic Proceedings 86:11, 1095-1102
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Miguel Viana-Baptista. (2011) Stroke and Fabry disease. Journal of Neurology
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Patrick B. Deegan. (2011) Fabry disease, enzyme replacement therapy and the significance of antibody responses. Journal of Inherited Metabolic Disease
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Keiko Toyooka. (2011) Fabry disease. Current Opinion in Neurology 24:5, 463-468
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Tim A. Kanters, Marloes L. C. Hagemans, Nadine A. M. E. Beek, Frans F. H. Rutten, Ans T. Ploeg, Leona Hakkaart. (2011) Burden of illness of Pompe disease in patients only receiving supportive care. Journal of Inherited Metabolic Disease 34:5, 1045-1052
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Folmer Fredslund, Maher Abou Hachem, René Jonsgaard Larsen, Pernille Gerd Sørensen, Pedro M. Coutinho, Leila Lo Leggio, Birte Svensson. (2011) Crystal Structure of α-Galactosidase from Lactobacillus acidophilus NCFM: Insight into Tetramer Formation and Substrate Binding. Journal of Molecular Biology 412:3, 466-480
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Maurizio Pieroni. (2011) Echocardiographic Assessment of Fabry Cardiomyopathy: Early Diagnosis and Follow-Up. Journal of the American Society of Echocardiography 24:9, 1033-1036
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Charles Masson. (2011) Maladie de Fabry : une maladie du métabolisme par déficit d’une enzyme lysosomale (alpha-galactosidase), de transmission héréditaire liée au chromosome X accessible au traitement enzymatique de substitution. Revue du Rhumatisme Monographies 78:4, 262-266
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J. Zamorano, V. Serra, L. Perez de Isla, G. Feltes, A. Calli, F. J. Barbado, J. Torras, S. Hernandez, J. Herrera, J. A. Herrero, G. Pintos. (2011) Usefulness of tissue Doppler on early detection of cardiac disease in Fabry patients and potential role of enzyme replacement therapy (ERT) for avoiding progression of disease. European Journal of Echocardiography 12:9, 671-677
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Melissa D. Lambourne, Murray A. Potter. (2011) Murine β-galactosidase stability is not dependent on temperature or protective protein/cathepsin A. Molecular Genetics and Metabolism
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Eri Oda, Toju Tanaka, Ohsuke Migita, Motomichi Kosuga, Masaru Fukushi, Toshika Okumiya, Makiko Osawa, Torayuki Okuyama. (2011) Newborn screening for Pompe disease in Japan. Molecular Genetics and Metabolism
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Shinya Nishizawa, Tomoko Osamura, Norikazu Takechi, Shigehiro Kusuoka, Keizo Furukawa. (2011) Mid-ventricular obstruction occurred in hypertrophic left ventricle of heterozygous Fabry's disease—Favorable effects of cibenzoline: A case report. Journal of Cardiology Cases
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Marieke Biegstraaten, Andreas Binder, Rainer Maag, Carla E.M. Hollak, Ralf Baron, Ivo N. van Schaik. (2011) The relation between small nerve fibre function, age, disease severity and pain in Fabry disease. European Journal of Pain 15:8, 822-829
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C. O'Mahony, C. Coats, M. Cardona, A. Garcia, M. Calcagnino, E. Murphy, R. Lachmann, A. Mehta, D. Hughes, P. M. Elliott. (2011) Incidence and predictors of anti-bradycardia pacing in patients with Anderson-Fabry disease. Europace
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M.-Á. Barba-Romero, A. Rivera-Gallego, G. Pintos-Morell, . (2011) Fabry disease in Spain: description of Spanish patients and a comparison with other European countries using data from the Fabry Outcome Survey (FOS). International Journal of Clinical Practice 65:8, 903-910
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D. G. Warnock, A. Ortiz, M. Mauer, G. E. Linthorst, J. P. Oliveira, A. L. Serra, L. Marodi, R. Mignani, B. Vujkovac, D. Beitner-Johnson, R. Lemay, J. A. Cole, E. Svarstad, S. Waldek, D. P. Germain, C. Wanner, . (2011) Renal outcomes of agalsidase beta treatment for Fabry disease: role of proteinuria and timing of treatment initiation. Nephrology Dialysis Transplantation
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Marina I. Giannotti, Olga Esteban, Mireia Oliva, María F. García-Parajo, Fausto Sanz. (2011) pH-Responsive Polysaccharide-Based Polyelectrolyte Complexes As Nanocarriers for Lysosomal Delivery of Therapeutic Proteins. Biomacromolecules 12:7, 2524-2533
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G. Messalli, M. Imbriaco, G. Avitabile, R. Russo, D. Iodice, L. Spinelli, S. Dellegrottaglie, F. Cademartiri, M. Salvatore, A. Pisani. (2011) Role of cardiac MRI in evaluating patients with Anderson-Fabry disease: assessing cardiac effects of long-term enzyme replacement therapy. La radiologia medica
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Julian F. Guest, Daniela Concolino, Raffaele Di Vito, Claudio Feliciani, Rossella Parini, Anna Zampetti. (2011) Modelling the resource implications of managing adults with Fabry disease in Italy. European Journal of Clinical Investigation 41:7, 710-718
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Abelardo García de Lorenzo. (2011) Consenso para el estudio y tratamiento de la enfermedad de Fabry. Fundación GETER. Medicina Clínica 137:4, 178-183
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Robert Dobrovolny, Irina Nazarenko, Jungmin Kim, Dana Doheny, Robert J. Desnick. (2011) Detection of large gene rearrangements in X-linked genes by dosage analysis: identification of novel α-galactosidase A (GLA) deletions causing Fabry disease. Human Mutation 32:6, 688-695
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Barbara K. Burton, David A.H. Whiteman. (2011) Incidence and timing of infusion-related reactions in patients with mucopolysaccharidosis type II (Hunter syndrome) on idursulfase therapy in the real-world setting: A perspective from the Hunter Outcome Survey (HOS). Molecular Genetics and Metabolism 103:2, 113-120
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Johannes M. F. G. Aerts, Wouter W. Kallemeijn, Wouter Wegdam, Maria Joao Ferraz, Marielle J. Breemen, Nick Dekker, Gertjan Kramer, Ben J. Poorthuis, Johanna E. M. Groener, Josanne Cox-Brinkman, Saskia M. Rombach, Carla E. M. Hollak, Gabor E. Linthorst, Martin D. Witte, Henrik Gold, Gijs A. Marel, Herman S. Overkleeft, Rolf G. Boot. (2011) Biomarkers in the diagnosis of lysosomal storage disorders: proteins, lipids, and inhibodies. Journal of Inherited Metabolic Disease 34:3, 605-619
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Kazuhiko Matsuoka, Tomomi Tamura, Daisuke Tsuji, Yukie Dohzono, Keisuke Kitakaze, Kazuki Ohno, Seiji Saito, Hitoshi Sakuraba, Kohji Itoh. (2011) Therapeutic Potential of Intracerebroventricular Replacement of Modified Human β-Hexosaminidase B for GM2 Gangliosidosis. Molecular Therapy 19:6, 1017-1024
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O Lidove, P Kaminsky, E Hachulla, V Leguy-Seguin, C Lavigne, I Marie, F Maillot, C Serratrice, A Masseau, P Chérin, J Cabane, E Noel, . (2011) Fabry disease ‘The New Great Imposter’: results of the French Observatoire in Internal Medicine Departments (FIMeD). Clinical Geneticsno-no
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Raymond Y. Wang, Olaf A. Bodamer, Michael S. Watson, William R. Wilcox. (2011) Lysosomal storage diseases: Diagnostic confirmation and management of presymptomatic individuals. Genetics in Medicine 13:5, 457-484
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M. Tchan, D. Sillence. (2011) Fabry disease and Factor V Leiden: a potent vascular risk combination. Internal Medicine Journal 41:5, 422-426
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Takayuki Yokoi, Hiroshi Kobayashi, Yohta Shimada, Yoshikatsu Eto, Nobuyuki Ishige, Teruo Kitagawa, Makoto Otsu, Hiromitsu Nakauchi, Hiroyuki Ida, Toya Ohashi. (2011) Minimum requirement of donor cells to reduce the glycolipid storage following bone marrow transplantation in a murine model of Fabry disease. The Journal of Gene Medicine 13:5, 262-268
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Carmen Valbuena, João Paulo Oliveira, Fátima Carneiro, Sandra Relvas, Mariana Ganhão, M. Clara Sá-Miranda, Lorena G. Rodrigues. (2011) Kidney histologic alterations in α-Galactosidase-deficient mice. Virchows Archiv 458:4, 477-486
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Daisuke Tsuji, Hiromi Akeboshi, Kazuhiko Matsuoka, Hiroko Yasuoka, Eri Miyasaki, Yoshiko Kasahara, Ikuo Kawashima, Yasunori Chiba, Yoshifumi Jigami, Takao Taki, Hitoshi Sakuraba, Kohji Itoh. (2011) Highly phosphomannosylated enzyme replacement therapy for GM2 gangliosidosis. Annals of Neurology 69:4, 691-701
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Rolando Cimaz, Severine Guillaume, Max J. Hilz, Gerd Horneff, Bernhard Manger, J. Carter Thorne, Anette Torvin Møller, Nico M. Wulffraat, Johannes Roth. (2011) Awareness of Fabry disease among rheumatologists—current status and perspectives. Clinical Rheumatology 30:4, 467-475
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Andreas Gal, Derralynn A. Hughes, Bryan Winchester. (2011) Toward a consensus in the laboratory diagnostics of Fabry disease - recommendations of a European expert group. Journal of Inherited Metabolic Disease 34:2, 509-514
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Gustavo Cabrera, Juan Politei. (2011) Interrupción de la terapia de reemplazo enzimático en la enfermedad de Fabry: mala evolución a propósito de un caso. Neurología Argentina 3:2, 113-116
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Frank Weidemann, Markus Niemann, David G. Warnock, Georg Ertl, Christoph Wanner. (2011) The Fabry Cardiomyopathy: Models for the Cardiologist. Annual Review of Medicine 62:1, 59-67
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Kimitoshi Nakamura, Kiyoko Hattori, Fumio Endo. (2011) Newborn screening for lysosomal storage disorders. American Journal of Medical Genetics Part C: Seminars in Medical Genetics 157:1, 63-71
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Takahiro Tsukimura, Yasunori Chiba, Kazuki Ohno, Seiji Saito, Youichi Tajima, Hitoshi Sakuraba. (2011) Molecular mechanism for stabilization of a mutant α-galactosidase A involving M51I amino acid substitution by imino sugars. Molecular Genetics and Metabolism
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Joseph Muenzer, Michael Beck, Roberto Giugliani, Yasuyuki Suzuki, Anna Tylki-Szymanska, Vassili Valayannopoulos, Ashok Vellodi, James E. Wraith. (2011) Idursulfase treatment of Hunter syndrome in children younger than 6 years: Results from the Hunter Outcome Survey. Genetics in Medicine 13:2, 102-109
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Alessandro P Burlina, Katherine B Sims, Juan M Politei, Gary J Bennett, Ralf Baron, Claudia Sommer, Anette Møller, Max J Hilz. (2011) Early diagnosis of peripheral nervous system involvement in Fabry disease and treatment of neuropathic pain: the report of an expert panel. BMC Neurology 11:1, 61
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Elice Carneiro Batista, Luiz Roberto Carvalho, Dulce Elena Casarini, Adriana Karaoglanovic Carmona, Edson Lucas Santos, Elton Dias Silva, Robson Augusto Santos, Clovis Ryuichi Nakaie, Maria Verônica Munoz Rojas, Suzana Macedo Oliveira, Michael Bader, Vânia D’Almeida, Ana Maria Martins, Kely Picoly Souza, João Bosco Pesquero. (2011) ACE activity is modulated by the enzyme α-galactosidase A. Journal of Molecular Medicine 89:1, 65-74
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Thomas E. Lloyd, Vinay Chaudhry. 2011. Treatment and Management of Hereditary Neuropathies. , 191-213.
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Carla EM Hollak, Johannes MFG Aerts, Ségolène Aymé, Jeremy Manuel. (2011) Limitations of drug registries to evaluate orphan medicinal products for the treatment of lysosomal storage disorders. Orphanet Journal of Rare Diseases 6:1, 16
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U. Feldt-Rasmussen. (2011) Fabry Disease and Early Stroke. Stroke Research and Treatment 2011, 1-7
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Yin-Hsiu Chien, Petra Olivova, Xiaokui Kate Zhang, Shu-Chuan Chiang, Ni-Chung Lee, Joan Keutzer, Wuh-Liang Hwu. (2011) Elevation of urinary globotriaosylceramide (GL3) in infants with Fabry disease. Molecular Genetics and Metabolism 102:1, 57-60
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Noriyuki Katsumata, Akira Ishiguro, Hiroshi Watanabe. (2011) Fabry Disease Superimposed on Overt Autoimmune Hypothyroidism. Clinical Pediatric Endocrinology 20:4, 95-98
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Bouwien E Smid, Saskia M Rombach, Johannes MFG Aerts, Symen Kuiper, Mina Mirzaian, Hermen S Overkleeft, Ben JHM Poorthuis, Carla EM Hollak, Johanna EM Groener, Gabor E Linthorst. (2011) Consequences of a global enzyme shortage of agalsidase beta in adult Dutch Fabry patients. Orphanet Journal of Rare Diseases 6:1, 69
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Brigette L. Tippin, Larisa Troitskaya, Shih-hsin Kan, Amanda K. Todd, Steven Q. Le, Patricia I. Dickson. (2011) Biochemical characterization of fluorescent-labeled recombinant human alpha-l-iduronidase in vitro. Biotechnology and Applied Biochemistryn/a-n/a
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Scott E. Kasner, Brett L. Cucchiara. 2011. Treatment of “Other” Stroke Etiologies. , 1084-1105.
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V. A. Polito, S. Abbondante, R. S. Polishchuk, E. Nusco, R. Salvia, M. P. Cosma. (2010) Correction of CNS defects in the MPSII mouse model via systemic enzyme replacement therapy. Human Molecular Genetics 19:24, 4871-4885
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Daniel P. Judge, Rosanne Rouf. (2010) Use of Genetics in the Clinical Evaluation and Management of Heart Failure. Current Treatment Options in Cardiovascular Medicine 12:6, 566-577
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Christiane Auray-Blais, Aimé Ntwari, Joe T.R. Clarke, David G. Warnock, João Paulo Oliveira, Sarah P. Young, David S. Millington, Daniel G. Bichet, Sandra Sirrs, Michael L. West, Robin Casey, Wuh-Liang Hwu, Joan M. Keutzer, X. Kate Zhang, René Gagnon. (2010) How well does urinary lyso-Gb3 function as a biomarker in Fabry disease?. Clinica Chimica Acta 411:23-24, 1906-1914
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Thomas D. Bird. (2010) Approaches to the Patient with Neurogenetic Disease. Clinics in Laboratory Medicine 30:4, 785-793
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Lucie Vojtová, Tomáš Zima, Vladimír Tesař, Jana Michalová, Petr Přikryl, Gabriela Dostálová, Aleš Linhart. (2010) Study of urinary proteomes in Anderson-Fabry disease. Renal Failure 32:10, 1202-1209
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Markus A. Hölzl, Miriam Gärtner, Johannes J. Kovarik, Johannes Hofer, Hanno Bernheimer, Gere Sunder-Plassmann, Gerhard J. Zlabinger. (2010) Quantification of α-galactosidase activity in intact leukocytes. Clinica Chimica Acta 411:21-22, 1666-1670
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Stephan vom Dahl, Eugen Mengel. (2010) Lysosomal storage diseases as differential diagnosis of hepatosplenomegaly. Best Practice & Research Clinical Gastroenterology 24:5, 619-628
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Adriana M. Doldan-Silvero, Gretl Nunnemacher, Michael Germain, Giovanna M. Crisi. (2010) Electron Microscopy in End Stage Renal Disease: A Case of Fabry's Disease. Ultrastructural Pathology 34:5, 307-313
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D.A. Hughes, U. Ramaswami, M.-Á. Barba Romero, P. Deegan. (2010) Age adjusting severity scores for Anderson–Fabry Disease. Molecular Genetics and Metabolism 101:2-3, 219-227
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Olivier Lidove, Michael L. West, Guillem Pintos-Morell, Ricardo Reisin, Kathy Nicholls, Luis E. Figuera, Rossella Parini, L. R. Carvalho, Christoph Kampmann, Gregory M. Pastores, Atul Mehta. (2010) Effects of enzyme replacement therapy in Fabry disease—A comprehensive review of the medical literature. Genetics in Medicine1
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Raphael Schiffmann. (2010) Agalsidase treatment for Fabry disease: Uses and rivalries. Genetics in Medicine1
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Atul Mehta, Michael L. West, Guillem Pintos-Morell, Ricardo Reisin, Kathy Nicholls, Luis E. Figuera, Rossella Parini, Luiz R. Carvalho, Christoph Kampmann, Gregory M. Pastores, Olivier Lidove. (2010) Therapeutic goals in the treatment of Fabry disease. Genetics in Medicine1
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Atul Mehta. (2010) Agalsidase alfa for enzyme-replacement therapy in Fabry disease. Expert Review of Endocrinology & Metabolism 5:5, 641-652
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Chih-Kang Chiang, Reiko Inagi. (2010) Glomerular diseases: genetic causes and future therapeutics. Nature Reviews Nephrology 6:9, 539-554
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M.G. Bouwman, F.A. Wijburg, S.M. Rombach, G.E. Linthorst, C.E.M. Hollak, J.M.F.G. Aerts. (2010) Hevige pijnklachten aan handen en voeten bij koorts en huidafwijkingen: de ziekte van Fabry. Tijdschrift voor Kindergeneeskunde 2010:2, 69-73
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A. Mehta, M. Beck, F. Eyskens, C. Feliciani, I. Kantola, U. Ramaswami, A. Rolfs, A. Rivera, S. Waldek, D. P. Germain. (2010) Fabry disease: a review of current management strategies. QJM 103:9, 641-659
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Mary N. Sheppard, Paul Cane, Richard Florio, Nicholas Kavantzas, Lydia Close, Jaymin Shah, Philip Lee, Perry Elliott. (2010) A detailed pathologic examination of heart tissue from three older patients with Anderson–Fabry disease on enzyme replacement therapy. Cardiovascular Pathology 19:5, 293-301
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S.M. Rombach, N. Dekker, M.G. Bouwman, G.E. Linthorst, A.H. Zwinderman, F.A. Wijburg, S. Kuiper, M.A. vd Bergh Weerman, J.E.M. Groener, B.J. Poorthuis, C.E.M. Hollak, J.M.F.G. Aerts. (2010) Plasma globotriaosylsphingosine: Diagnostic value and relation to clinical manifestations of Fabry disease. Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease 1802:9, 741-748
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Tadayasu Togawa, Ikuo Kawashima, Takashi Kodama, Takahiro Tsukimura, Toshihiro Suzuki, Tomoko Fukushige, Takuro Kanekura, Hitoshi Sakuraba. (2010) Tissue and plasma globotriaosylsphingosine could be a biomarker for assessing enzyme replacement therapy for Fabry disease. Biochemical and Biophysical Research Communications 399:4, 716-720
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Torquil Watt, Alessandro P. Burlina, Chiara Cazzorla, Dorothee Schönfeld, Maryam Banikazemi, Robert J. Hopkin, Ana Maria Martins, Katherine Sims, Dana Beitner-Johnson, Fanny OʼBrien, Ulla Feldt-Rasmussen. (2010) Agalsidase beta treatment is associated with improved quality of life in patients with Fabry disease: Findings from the Fabry Registry. Genetics in Medicine1
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Laura Bannach Jardim, Maria Mercedes Villanueva, Carolina F. Moura de Souza, Cristina B. Oliveira Netto. (2010) Clinical aspects of neuropathic lysosomal storage disorders. Journal of Inherited Metabolic Disease 33:4, 315-329
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Kazuhiko Matsuoka, Daisuke Tsuji, Sei-ichi Aikawa, Fumiko Matsuzawa, Hitoshi Sakuraba, Kohji Itoh. (2010) Introduction of an N-Glycan Sequon Into HEXA Enhances Human β-Hexosaminidase Cellular Uptake in a Model of Sandhoff Disease. Molecular Therapy 18:8, 1519-1526
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Wuh-Liang Hwu, Yin-Hsiu Chien, Ni-Chung Lee. (2010) Newborn screening for neuropathic lysosomal storage disorders. Journal of Inherited Metabolic Disease 33:4, 381-386
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B. Manger. (2010) Lysosomale Speicherkrankheiten. Zeitschrift für Rheumatologie 69:6, 527-538
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Tamás Constantin, Annamária Székely, Andrea Ponyi, Vera Gulácsy, Csaba Ambrus, Krisztina Kádár, Ildikó Vastagh, Angéla Dajnoki, Beáta Tóth, Gergely Bokrétás, Veronika Müller, Mária Katona, Márta Medvecz, Orsolya Fiedler, Rita Széchey, Edit Varga, Gábor Rudas, Attila Kertész, Sándor Molnár, Sarolta Kárpáti, Viktor Nagy, Pál Magyar, Mohamed Mahdi, Éva Rákóczi, Krisztina Németh, Dániel Bereczki, Miklós Garami, Melinda Erdős, László Maródi, György Fekete. (2010) Fabry-betegség – terápiás útmutató. Orvosi Hetilap 151:31, 1243-1251
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A. B. Fogo, L. Bostad, E. Svarstad, W. J. Cook, S. Moll, F. Barbey, L. Geldenhuys, M. West, D. Ferluga, B. Vujkovac, A. J. Howie, A. Burns, R. Reeve, S. Waldek, L.-H. Noel, J.-P. Grunfeld, C. Valbuena, J. P. Oliveira, J. Muller, F. Breunig, X. Zhang, D. G. Warnock, . (2010) Scoring system for renal pathology in Fabry disease: report of the International Study Group of Fabry Nephropathy (ISGFN). Nephrology Dialysis Transplantation 25:7, 2168-2177
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Maja Cikes, George R. Sutherland, Lisa J. Anderson, Bart H. Bijnens. (2010) The role of echocardiographic deformation imaging in hypertrophic myopathies. Nature Reviews Cardiology 7:7, 384-396
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Max J Hilz, Harald Marthol, Stefan Schwab, Edwin H Kolodny, Miroslaw Brys, Brigitte Stemper. (2010) Enzyme replacement therapy improves cardiovascular responses to orthostatic challenge in Fabry patients. Journal of Hypertension 28:7, 1438-1448
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Frank Weidemann, Claudia Sommer, Thomas Duning, Ines Lanzl, Matthias Möhrenschlager, Dennis Naleschinski, Kathrin Arning, Ralf Baron, Markus Niemann, Frank Breunig, Roland Schaefer, Jörg Strotmann, Christoph Wanner. (2010) Department-related Tasks and Organ-targeted Therapy in Fabry Disease: An Interdisciplinary Challenge. The American Journal of Medicine 123:7, 658.e1-658.e10
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Akemi Tanaka, Taisuke Takeda, Takao Hoshina, Kazuyoshi Fukai, Tsunekazu Yamano. (2010) Enzyme replacement therapy in a patient with Fabry disease and the development of IgE antibodies against agalsidase beta but not agalsidase alpha. Journal of Inherited Metabolic Disease
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J. C. Wu, C. Y. Ho, H. Skali, R. Abichandani, W. R. Wilcox, M. Banikazemi, S. Packman, K. Sims, S. D. Solomon. (2010) Cardiovascular manifestations of Fabry disease: relationships between left ventricular hypertrophy, disease severity, and -galactosidase A activity. European Heart Journal 31:9, 1088-1097
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F. Weidemann, A. Linhart, L. Monserrat, J. Strotmann. (2010) Cardiac challenges in patients with Fabry disease. International Journal of Cardiology 141:1, 3-10
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Raphael Schiffmann, Rick A. Martin, Tyler Reimschisel, Karen Johnson, Victoria Castaneda, Y. Howard Lien, Gregory M. Pastores, Christoph Kampmann, Markus Ries, Joe T.R. Clarke. (2010) Four-Year Prospective Clinical Trial of Agalsidase Alfa in Children with Fabry Disease. The Journal of Pediatrics 156:5, 832-837.e1
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Juan M. Politei. (2010) Treatment with agalsidase beta during pregnancy in Fabry disease. Journal of Obstetrics and Gynaecology Research 36:2, 428-429
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James B. Seward, Grace Casaclang-Verzosa. (2010) Infiltrative Cardiovascular Diseases. Journal of the American College of Cardiology 55:17, 1769-1779
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S. Sirrs, J.T.R. Clarke, D.G. Bichet, R. Casey, K. Lemoine, G. Flowerdew, D.S. Sinasac, M.L. West. (2010) Baseline characteristics of patients enrolled in the Canadian Fabry Disease Initiative. Molecular Genetics and Metabolism 99:4, 367-373
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R. P. E. Sarkany, S. M. Breathnach, A. A. M. Morris, K. Weismann, P. D. Flynn. 2010. Metabolic and Nutritional Disorders. , 1-103.
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