Original Article
Evaluation of Systemic Amyloidosis by Scintigraphy with 123I-Labeled Serum Amyloid P Component
N Engl J Med 1990; 323:508-513August 23, 1990
- Abstract
- Abstract
Background.
In systemic amyloidosis the distribution and progression of disease have been difficult to monitor, because they can be demonstrated only by biopsy. Serum amyloid P component (SAP) is a normal circulating plasma protein that is deposited on amyloid fibrils because of its specific binding affinity for them. We investigated whether labeled SAP could be used to locate amyloid deposits.
Methods.
Purified human SAP labeled with iodine-123 was given intravenously to 50 patients with biopsy-proved systemic amyloidosis — 25 with the AL (primary) type and 25 with the AA (secondary) type — and to 26 control patients with disease and 10 healthy subjects. Whole-body images and regional views were obtained after 24 hours and read in a blinded fashion.
Results.
In the patients with amyloidosis the 123I-SAP was localized rapidly and specifically in amyloid deposits. The scintigraphic images obtained were characteristic and appeared to identify the extent of amyloid deposition in all 50 patients. There was no uptake of the 123I-SAP by the control patients and the healthy subjects. In all patients with AA amyloidosis the spleen was affected, whereas the scans showed uptake in the heart, skin, carpal region, and bone marrow only in patients with the AL type. Positive images were seen in six patients in whom biopsies had been negative or unsuccessful; in all six, amyloid was subsequently found on biopsy or at autopsy. Progressive amyloid deposition was observed in 9 of 11 patients studied serially.
Conclusions.
Scintigraphy after the injection of 123I-SAP can be used for diagnosing, locating, and monitoring the extent of systemic amyloidosis. (N Engl J Med 1990; 323:508–13.)
Media in This Article
Figure 1
Posterior Whole-Body Scintigraph Six Hours after the Intravenous Injection of 123I-SAP into a Patient with AL Amyloidosis.Figure 2
Serial 123I-SAP Scans of Patients with Systemic Amyloidosis.Article Activity
- Article
THERE are two main forms of acquired systemic amyloidosis.1 , 2 AL amyloidosis, formerly known as primary amyloidosis, occurs in patients with B-cell or plasma-cell dyscrasias, in whom fragments of monoclonal immunoglobulin light chains form amyloid fibrils. AA or reactive systemic (secondary) amyloidosis occurs in patients with chronic inflammatory conditions in whom the fibril protein is derived from the circulating acute-phase lipoprotein known as serum amyloid A. Both are serious and usually fatal conditions in which the accumulation of amyloid fibrils in the tissues destroys normal structure and function.1 , 2 In addition to the fibrils, all amyloid deposits contain amyloid P component, a nonfibrillar glycoprotein that is identical to and derived from serum amyloid P component (SAP), a normal circulating protein of the pentraxin family.2 3 4 5
The only means of diagnosing amyloidosis has been histologic examination, which provides very limited information on the tissue distribution, extent, or progress of the disease. In the absence of any effective therapy such concerns were largely academic, but it has lately been demonstrated that cytotoxic anti-inflammatory therapy in patients with rheumatoid arthritis or juvenile chronic arthritis whose disease has been complicated by AA amyloidosis can greatly improve their prognosis.6 7 8 There are also reports of longer survival in some patients with AL amyloidosis treated with the cytotoxic drugs used in myeloma9 10 11 12 or with colchicine.13 The proper evaluation of these approaches to therapy and any developed in the future, as well as the elucidation of the mechanisms of pathogenesis, require reliable information about the extent and progression of amyloid deposition.
SAP binds specifically to amyloid fibrils in vitro14 and in vivo.15 16 17 It is retained in tissue amyloid deposits for prolonged periods, apparently protected from the normal rapid catabolism to which it is subject in the circulation. In a group of patients with biopsy-proved AA or AL amyloidosis, we investigated the use of scintigraphy after the injection of purified human SAP labeled with iodine-123 as a noninvasive technique for diagnosing, locating, and monitoring amyloid deposits.
Methods
Preparation of SAP
Sterile, 99 percent pure SAP was isolated18 from the serum (heated at 56°C for 30 minutes) of a single accredited donor to the U.K. National Blood Transfusion Service. Such donors undergo clinical and serologic screening repeatedly and prospectively, and their serum is only released after 12 months.
Radiolabeling
SAP labeled with iodine-123 as described elsewhere17 , 19 was sterile and nonpyrogenic. Each lot had the same specific binding to amyloid fibrils in vitro17 and the same metabolism in vivo in normal and amyloidotic mice5 , 16 as unlabeled SAP. There have been no adverse effects in persons receiving any of the 25 lots of 123I-SAP used in the studies described here (a total of 100 injections) or in any subsequent studies.
Patients and Controls
There were 25 patients (13 men and 12 women; mean [±SD] age, 38.8±17.3 years; range, 17 to 69) with AA amyloidosis complicating chronic inflammatory diseases: rheumatoid arthritis (7 patients), juvenile rheumatoid arthritis (12), ankylosing spondylitis (1), psoriatic arthritis (1), Crohn's disease (1), bronchiectasis (1), osteomyelitis (1), and mesothelioma (1). The diagnosis was made before scanning in 22 patients by the detection of deposits with apple-green birefringence when histologic sections of liver-, renal-, or rectal-biopsy specimens stained with alcoholic alkaline Congo red20 were viewed in polarized light. In three patients amyloidosis was confirmed after scanning by histologic examination of renal-, gastric-, and vascular-biopsy specimens, respectively.
There were 25 patients with AL amyloidosis (13 men and 12 women; mean age, 66.6±10.9 years; range, 43 to 87). Fifteen had monoclonal λ protein, 4 had κ protein, and in 6 the type of protein was not known. In 22 of these patients the diagnosis had been established by histologic examination of the liver, kidney, spleen, lung, skin, heart, rectum, or stomach before scanning, and in 3 patients it was histologically confirmed after scanning (in 1 by cardiac biopsy and in 2 at autopsy).
A total of 26 patients were studied as controls with disease. Eighteen with no clinical or laboratory evidence suggesting amyloidosis had chronic inflammatory diseases: rheumatoid arthritis (9 patients), juvenile rheumatoid arthritis (5), ankylosing spondylitis (1), Behçet's disease (1), bronchiectasis (1), and familial Mediterranean fever (1). These 18 patients had no visible lesions or visceral-organ dysfunction other than that caused directly by their primary disease, no proteinuria, and no organomegaly. All patients with arthritis had had their disease for less than five years. The patients with familial Mediterranean fever and bronchiectasis had had rectal biopsies that were negative for amyloid. The additional controls with disease included six patients with monoclonal gammopathy but no evidence of amyloidosis (i.e., no visible lesions, organ dysfunction, or organomegaly, and negative results on staining of bone marrow—biopsy specimens for amyloid) and two patients with restrictive cardiomyopathy in whom echocardiography suggested infiltration but in whom endomyocardial-biopsy specimens were negative for amyloid.
The healthy subjects consisted of five men and five women with a mean age of 59.1 ± 13.0 years (range, 22 to 78). Informed consent was given by all subjects, and the project was approved by the Research Ethics Committee of Hammersmith Hospital and the Administration of Radioactive Substances Advisory Committee of the Department of Health and Social Security, United Kingdom.
Imaging Procedure
After we verified that no subject had a history of adverse reactions to iodide, all subjects received 60 mg of potassium iodide orally twice daily for two days before and three days after the imaging procedure. Two hundred megabecquerels (containing 200 μg) of 123I-SAP was administered in a bolus intravenous injection, the precise amount being established by weighing the syringe before and after injection. The effective dose-equivalent of 4.5 millisieverts was comparable with that of a routine bone scan, intravenous urogram, or barium series. Anterior and posterior whole-body images, regional views, and in some cases, single-photon-emission computed tomograms were obtained after 24 hours with a gamma camera (General Electric Starcam) with a medium-energy parallel-hole collimator. Scintigraphs were also recorded 30 minutes after injection and 6, 24, and 48 hours later in five patients with amyloidosis and five healthy subjects. The images were reviewed at the time of acquisition and then in blinded fashion by a radiologist specializing in nuclear medicine.
Analysis of, 23I-SAP Clearance
Venous-blood samples were obtained from the contralateral forearm in all subjects 5, 15, and 30 minutes and 6 hours after the injection of 123I-SAP, and all urine was collected for two days. Samples of urine and plasma (1 ml) were counted in a gamma counter (NE 1612 Turbo, Nuclear Enterprises) together with an aliquot of the injected material. Plasma radioactivity after six hours was expressed as a percentage of the extrapolated time-zero (T0) value. The whole-body retention of radioactivity after 48 hours was calculated by subtracting the cumulative radioactivity excreted in the urine at each interval from the total injected dose, and also from the scanning data with use of the geometric means of the whole-body counts after correction for isotope decay (half-life of iodine-123, 13.21 hours), as compared with the value immediately after injection. The statistical significance of differences between groups and in serial studies was determined by t-tests, unpaired or paired as appropriate, with calculation of the 95 percent confidence intervals of the differences between means.
Autopsy Studies
A 76-year-old man with a monoclonal IgG-λ gammopathy who presented with severe autonomic neuropathy and hypotension, who had had several episodes of circulatory collapse and loss of consciousness, and who had been confined to bed for the previous three months, died suddenly eight hours after the administration of 123I-SAP. The cause of death established at autopsy 16 hours later was a massive pulmonary embolus. He had been a heavy smoker, and there was substantial emphysema. The precise distribution of 123I-SAP among the organs was determined, tissue sections were stained with Congo red to assess the distribution of amyloid,20 and the location of 123I-SAP in several organs was determined by autoradiography.5 Autopsies were also performed in five other patients who died of disorders clearly related to systemic amyloidosis between 2 weeks and 12 months after study. In each patient the distribution of amyloid was established by Congo-red staining.
Results
Images in Healthy Subjects and Control Patients
Scintigraphs obtained after the intravenous injection of 123I-SAP in the 10 healthy subjects and the 26 control patients with disease showed a distribution of tracer activity that was confined to the blood pool, with rapid breakdown leading to the excretion of radioactive fragments in the urine. About 45 percent of the injected dose was cleared from the body within 48 hours. Despite the administration of potassium iodide, a small amount of radioactivity (comprising less than 1 percent of the injected dose) was occasionally seen in the thyroid, salivary glands, and stomach, reflecting the known distribution of free radioiodide.
Images in Patients with Amyloidosis
All 44 patients with histologically proved amyloidosis had rapid uptake of 123I-SAP into one or more sites, including the viscera, the bone marrow, the carpal region, and occasionally the skin and tongue. This produced characteristic scintigraphic images (Fig. 1Figure 1
Posterior Whole-Body Scintigraph Six Hours after the Intravenous Injection of 123I-SAP into a Patient with AL Amyloidosis. and 2Figure 2Serial 123I-SAP Scans of Patients with Systemic Amyloidosis.). In patients with massive amyloidosis of the liver, the spleen, or both, up to 95 percent of the injected dose had become concentrated in those areas 30 minutes after injection, when the first image was obtained.The specificity of the localization of 123I-SAP in amyloid deposits was demonstrated at autopsy in six patients who died of their disease at various intervals after imaging. The histologic distribution of amyloid at autopsy and the previous in vivo images corresponded precisely. In one patient who had a pulmonary embolism and died suddenly eight hours after injection, the images obtained six hours after injection showed intense uptake in the spleen and adrenal glands (Fig. 1). The density of amyloid deposition demonstrated histologically in the various tissues corresponded exactly to the quantity of tracer present in the in vivo images. Autoradiography confirmed the microscopic correspondence in the distribution of radioactivity and amyloid (Table 1Table 1
Distribution of 123I-SAP and Amyloid in the Organs of a Patient with AL Amyloidosis Who Died Eight Hours after the Injection of Tracer.).In a further group of six patients with diseases predisposing to amyloidosis, clinical features suggestive of the disease, or both, but in whom tissue examination was negative (four patients) or not undertaken (two patients), positive images were also obtained. The diagnosis of amyloidosis was subsequently corroborated histologically in each case.
The distribution of AA amyloid was fairly constant, with the spleen involved in every case, but the distribution of AL amyloid was extremely variable (Table 2Table 2
Organ Distribution of 123I-SAP in Patients with Systemic AA Amyloidosis and Patients with AL Amyloidosis.). Uptake into the heart, skin, carpal region, and skeleton was specific for the AL type in this series. Tracer frequently accumulated in sites where amyloid deposition had not been previously suspected clinically and where no suggestive clinical or laboratory features could be detected after scintigraphy. The specificity of these observations was confirmed in each of the six patients who subsequently died and were studied at autopsy. Another interesting finding was that of the nonhomogeneous uptake of tracer, particularly in affected livers and spleens, despite homogeneity on CT scanning. This may reflect patchy amyloid deposition and, in view of the extremely small samples obtained by needle biopsy, suggests that histologic monitoring of amyloid is unlikely to be reliable.Studies of 123I-SAP Clearance
After an initial distribution phase during the first six hours after injection, SAP is cleared from the circulation of healthy people with a half-time of 24 to 30 hours.17 In the 10 healthy subjects we studied, the mean (±SD) quantity of 123I-SAP remaining in the plasma six hours after injection was 74.5±4.9 percent of the notional T0 value. In five healthy subjects the same results for whole-body retention of radioactivity were obtained by monitoring urinary excretion and by scanning — indicating that substantial excretion occurred only in the urine. The mean value for 48-hour whole-body retention of 10 healthy subjects by the urinary-excretion method was 53.1±7.1 percent of the injected dose (Fig. 3Figure 3
Plasma Clearance and Whole-Body Retention of 123I-SAP in Healthy Subjects and Control Patients (Upper Panel) and Patients with Amyloidosis (Lower Panel).). The results for mean 6-hour plasma content (72.5±4.9 percent) and mean 48-hour whole-body retention of 123I-SAP in the 26 control patients with disease (56.3±9.0 percent) were not significantly different from those in the healthy subjects (Fig. 3).In most patients with systemic amyloidosis, the initial six-hour plasma clearance and whole-body retention of 123I-SAP were increased (Fig. 3), and in both the patients with AA amyloidosis and those with the AL type these measures were significantly different from those of the two control groups (P<0.001 for both variables in both groups). The values observed corresponded to the proportion of tracer that had accumulated in the amyloid deposits, which correlated closely with clinical estimates of the quantity of amyloid present, subsequent pathological estimates, or both. In several advanced cases, over 90 percent of the tracer had become concentrated in the amyloid deposits within six hours of injection, where it persisted throughout the study period. These observations, supported by the imaging results, indicated that the 123I-SAP sequestered in the amyloid deposits was degraded much more slowly than that remaining in the circulation. The resulting abnormal patterns of SAP turnover were in themselves frequently diagnostic of amyloidosis and, furthermore, suggest a simple method of quantifying the deposits.
Serial Studies
Serial studies were performed at intervals of 6 to 12 months. In each of three healthy subjects, the values obtained for SAP turnover were within 1 percent of the original results. In two patients with AA amyloidosis and three patients with AL amyloidosis whose condition had deteriorated clinically, suggesting increased amyloid deposition, the images in the second study developed more rapidly and were more intense, with a higher target:background ratio (Fig. 2). In each patient, early plasma clearance and whole-body retention of 123I-SAP were significantly increased (Fig. 3). The means of the differences for these five patients were as follows: for 6-hour plasma tracer content, − 7.8 percent of the injected dose (95 percent confidence interval, −10.5 to −3.6; P<0.02); and for 48-hour whole-body retention, 7.2 percent of the injected dose (95 percent confidence interval, 0.9 to 13.5; P<0.05). Among a further three patients with AA amyloidosis and three patients with AL amyloidosis who had no measurable clinical changes, scanning and SAP-turnover results indicated increased SAP deposition in one patient with AA amyloidosis and all three with AL amyloidosis (Fig. 3). In the other two patients with AA amyloidosis, whose underlying rheumatic disease had been treated in the meantime with cytotoxic antiinflammatory drugs, there were no changes in SAP turnover or images (Fig. 3).
Discussion
Amyloid deposits contain amyloid P component, which is derived from the normal circulating protein SAP. In patients with amyloidosis, SAP leaves the circulation and is deposited on the amyloid fibrils, presumably because of its specific calcium-dependent binding affinity for them.14 After earlier studies in animals5 , 15 , 16 and humans17 that elucidated this mechanism, SAP labeled with iodine-123 was used in this study as an in vivo targeting agent for amyloid in order to study patients with systemic amyloidosis and controls. Scintigraphy with 123I-SAP produces high-quality images because a high proportion of the tracer is deposited in amyloid and retained there for prolonged periods, whereas circulating SAP that has not been deposited is rapidly catabolized and excreted. Radionuclide imaging of amyloid with pyrophosphate or diphosphonate labeled with technetium-99m, both of which are sometimes deposited in amyloid, gives very variable results and is too nonspecific and insensitive to be clinically useful.22 23 24 25 26 27 28 29 In contrast, we have shown here that the uptake and retention of SAP in amyloid was highly specific and that the quantity of Radio-labeled SAP in each tissue correlated with the amount of amyloid present.
The presence of clinically silent amyloid was demonstrated by SAP imaging in vivo in the spleen and adrenal glands, in which biopsies are not easily performed and in which amyloid was not otherwise detectable. Although these tissues are known from autopsy studies to be affected in systemic amyloidosis, it is clinically important to demonstrate this impairment in life. Indeed, three of the seven patients with positive adrenal scintigraphy in our study were subsequently found to have impaired adrenal functional reserve. Marked skeletal uptake of SAP was observed in two patients with AL amyloidosis in whom all the following had been normal: serum calcium, phosphate, and alkaline phosphatase levels; x-ray films; skeletal isotope bone scan; and bone marrow. One patient had had pathologic fractures of the femurs, and the presence of extensive amyloid deposits in bone, corresponding precisely to the SAP images, was subsequently confirmed at autopsy.
Despite the specific accumulation of tracer in myocardial amyloid deposits, demonstrable at autopsy, scintigraphic images of affected hearts were often less satisfactory than images of other amyloidotic organs. The motility of the heart and the blood-pool background may have accounted for this result, but in the future perhaps these factors could be overcome by electrocardiographic gating and subtraction of the blood pool. Attenuation of the signal by the surrounding tissues may also have been a factor — for example, even amyloid in the spleen seen readily in posterior scans was often invisible from the front. The uptake of 123I-SAP occurred in proportion to the quantity of amyloid present in particular tissues, and the relative quantity in the heart was often small. For example, in one patient with AL amyloidosis studied at autopsy the distribution of amyloid P component in the affected organs was as follows: heart, 54 mg (2.4 percent); liver, 1584 mg (69.4 percent); spleen, 566 mg (24.8 percent); kidneys, 80 mg (3.5 percent). When scintigraphic images of this patient were obtained during life, over 90 percent of the injected dose was rapidly concentrated in the deposits in the liver and spleen, leaving little available for other sites. After 24 hours a faint image of the kidneys was seen from the back, although not the front; not surprisingly, the myocardium could not be convincingly visualized.
In most patients with amyloidosis, early plasma clearance and whole-body retention of 123I-SAP were significantly higher than in controls. Serial studies of SAP turnover in healthy subjects produced notably stable results, but on retesting after 6 to 12 months, 9 of 11 patients with amyloidosis had significantly increased clearance and retention and correspondingly enhanced scintigraphic images, even though 6 of them had not deteriorated clinically. On the other hand, a gratifying absence of progression was observed in two patients with AA amyloidosis and rheumatic disease treated with cytotoxic drugs. The present method can thus be used by itself to quantify amyloid deposition, instead of relying on studies of the function of amyloid-laden organs, which may be affected by many other factors and do not reliably indicate the quantity of amyloid present.
Although a tissue diagnosis is clearly still the final arbiter, no single biopsy procedure with 100 percent efficacy in the detection of systemic amyloid has been reported, and repeated biopsies of kidney, liver, and even rectum are not without risk. Biopsy has a high degree of sensitivity in the diagnosis of systemic amyloidosis but requires a high degree of expertise. For example, of the most recent 87 patients with systemic amyloidosis referred to our unit, 47 had already had rectal biopsies performed elsewhere, of which 23 were reported as negative, and 2 of 31 patients who had undergone renal biopsy had had serious complications. In contrast, the use of labeled SAP as a targeting agent is noninvasive, safe, and on the basis of our present findings, capable of confirming or excluding serious amyloidosis rapidly and easily. It thus makes a valuable contribution to the diagnosis, monitoring, and treatment of patients with amyloidosis.
Supported by grants from the Medical Research Council. Dr. Hawkins was a Medical Research Council Training Fellow.
We are indebted to Dr. M.J. Walport, Dr. A.M. Peters, Dr. P. Royston, and Professor R. Wootton for helpful discussions; to Miss Belinda Henderson for radiographic expertise; and to Ms. Beth Sontrop for assistance in the preparation of the manuscript.
Source Information
From the Immunological Medicine Unit, Department of Medicine (P.N.H., M.B.P.), and the Nuclear Medicine Unit, Department of Radiology (J.P.L.), Royal Postgraduate Medical School, Hammersmith Hospital, London. Address reprint requests to Dr. Hawkins at the Immunological Medicine Unit, Royal Postgraduate Medical School, Hammersmith Hospital, Du Cane Rd., London W12 0NN, United Kingdom.
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