Original Article
Selective Expression of Purkinje-Cell Antigens in Tumor Tissue from Patients with Paraneoplastic Cerebellar Degeneration
N Engl J Med 1990; 322:1844-1851June 28, 1990
- Abstract
- Abstract
Paraneoplastic cerebellar degeneration is a rare syndrome that occurs in patients with gynecologic cancer and is characterized by widespread loss of Purkinje cells. To determine whether Purkinje-cell antigens are selectively expressed in the tumors of patients with the syndrome, we examined tumor tissue from 10 patients whose serum contained anti—Purkinje-cell (anti-Yo) antibodies. The origins of the cancers were the breast (five patients), ovary (three), endometrium (one), and fallopian tube (one). We used as controls tumor tissue from 11 patients with ovarian cancer and 10 patients with breast cancer who were neurologically normal.
Using immunohistochemical and Western blot analysis, we found that Purkinje-cell antigens were expressed in all the tumors from the 10 patients with paraneoplastic cerebellar degeneration but in none of the tumors from the 21 neurologically normal patients. When IgG from patients with paraneoplastic cerebellar degeneration was affinity-purified to cerebellar Purkinje-cell antigen, immunohistochemical analysis showed that it reacted specifically with the tumor tissue from those patients.
We conclude that in patients with paraneoplastic cerebellar degeneration, the anti-Yo antibody results from an immune response to neural antigens expressed by the gynecologic tumors in the patients. (N Engl J Med 1990; 322:1844–51.)
Media in This Article
Figure 1
Western Blot Analysis of Tumor Tissue from Patients with Paraneoplastic Cerebellar Degeneration.Figure 2
Analysis of Expression of CDR 62 in Samples of Breast and Ovarian Tumors from Neurologically Normal Patients and from a Patient with Paraneoplastic Cerebellar Degeneration.Article Activity
- Article
PARANEOPLASTIC cerebellar degeneration is a rare remote effect of cancer characterized clinically by rapidly evolving pancerebellar symptoms (nystagmus, dysarthria, and appendicular and gait ataxia) and pathologically by widespread loss of cerebellar Purkinje cells, which is sometimes accompanied by perivascular and leptomeningeal inflammatory infiltrates.1 , 2 The neurologic disorder usually develops before the underlying cancer is identified. In some instances clinical evidence of cancer does not appear for months or even years after the patient has been disabled by the neurologic disorder.3 In a clinically definable subgroup of patients with paraneoplastic cerebellar degeneration due to gynecologic tumors, high titers of anti—Purkinje-cell autoantibody (now called anti-Yo) have been found, and the antibody has been characterized.3 4 5 6 The unique occurrence of the anti-Yo antibody in such patients prompted the hypothesis that the cerebellar deficit is a result of an autoimmune-induced destruction of Purkinje-cell function.
Anti-Yo serum has been characterized by its reactivity with the cytoplasm of Purkinje cells and by its recognition of two Purkinje-cell antigens, of 62 and 34 kd.7 We have called these antigens CDR (cerebellar-degeneration—related) 62 and CDR 34. All samples of anti-Yo serum analyzed to date recognize both antigens. CDR 62 is the major antigen; reactivity against CDR 34 is typically an order of magnitude less. Little is known of the function of these proteins in the Purkinje cell. The gene encoding CDR 34 has been isolated, sequenced,8 , 9 and mapped to the long arm of the X chromosome.10 The gene encoding CDR 62 has also recently been cloned and characterized.11
The antigenic stimulus of this autoimmune response has hitherto been unidentified. In this paper we report the selective expression of Purkinje-cell antigens by tumor tissue from patients with paraneoplastic cerebellar degeneration but not by similar tumors from patients without paraneoplastic cerebellar degeneration. These findings indicate that the expression of neural antigens by tumors may trigger paraneoplastic neurologic dysfunction.12
Methods
Tissues and Cell Lines
Purkinje-cell neurons were purified from human cerebellar tissue according to the method of Yanagihara and Hamberger,13 as modified by Cunningham et al.7 Tumor tissue, serum, and cerebrospinal fluid were obtained from patients with paraneoplastic cerebellar degeneration by their physicians. Tumor tissue from patients without detectable paraneoplastic cerebellar degeneration (as determined by chart review) was obtained from the tumor-procurement service of the Memorial Sloan-Kettering Cancer Center as tissue became available. Tissue samples from controls and patients with paraneoplastic cerebellar degeneration were processed identically.
Western Blot Analysis
Tissues were homogenized in phosphate-buffered saline with 0.1 percent Nonidet P-40 and centrifuged at 15,000×g for 10 minutes, and the supernatant was retained. The protein content was measured according to the method of Bradford.14 The indicated amounts of protein were subjected to electrophoresis on 10 percent sodium dodecyl sulfate–polyacrylamide gel and transferred to nitrocellulose as described by Towbin et al.15 The nitrocellulose filters were then blocked by incubation with 5 percent Blotto (5 percent Carnation evaporated milk in phosphate-buffered saline) and incubated with the indicated amount of anti-Yo IgG for two hours at room temperature. The nitrocellulose filters were washed with TRIS buffer (0.1 M TRIS, pH 8.0; 0.2 M sodium chloride; 0.2 percent Triton X-100; and 0.1 percent bovine serum albumin), incubated with 125I-labeled protein A (0.1 μCi per milliliter) for 1 hour at room temperature, washed again with TRIS buffer, and exposed to x-ray film for 18 hours. The molecular-weight markers in the figures are Amersham Rainbow Markers. These marker proteins are conjugated to chromophores and migrate substantially more slowly than the unconjugated protein. The apparent molecular weights in the text are the original determinants used to characterize the Yo antigens.7
Preparation of Biotinylated IgG and Anti-CDR 62 IgG
IgG was purified from serum from controls and from the patients with paraneoplastic cerebellar degeneration by adsorption to protein A–Sepharose gel and elution with sodium citrate (pH 2.5). After neutralization and dialysis against phosphate-buffered saline, the purified IgG (3.4 mg in a volume of 2.0 ml) was reacted with 50 μg of biotin N-hydroxysuccinimide ester (Vector Laboratories) for two hours at room temperature. The reaction was terminated by the addition of glycine (10 mg), and the free biotin removed by dialysis against phosphate-buffered saline. We checked the completeness of the reaction by measuring the quantitative binding of the biotinylated IgG to avidin—agarose.
Extracts of Purkinje cells (200 μg of protein) were resolved by preparative (continuous "curtain" well) 8 percent polyacrylamide gel electrophoresis. The proteins were transferred to nitrocellulose14 , 15 and blocked with Blotto. The sheet of nitrocellulose was incubated for two hours at room temperature with biotinylated anti-Yo IgG (10 μg per milliliter) and washed with phosphate-buffered saline. A representative strip was then cut from the nitrocellulose and stained with 125I-labeled protein A to determine the location of the CDR 62 band. Two strips (in the horizontal dimension) were cut from the nitrocellulose sheet; one was obtained from the area containing the CDR 62 band, and the other from an irrelevant area of the gel to provide a background control. IgG was eluted from these strips by a two-minute incubation with 10 ml of 0.1 M sodium citrate (pH 2.5). The eluates were recovered, neutralized with Trizma base, and precipitated with both ammonium sulfate (40 percent final concentration) and 0.7 mg of human serum. The resulting pellets were suspended in 0.8 ml of phosphate-buffered saline and subjected to dialysis against phosphate-buffered saline overnight at 4°C.
Immunohistochemical Analysis
Tissues were snap-frozen and embedded in OCT (optimal-cutting-temperature) compound. Frozen sections (6 μm thick) were cut on a cryostat, fixed for 10 minutes in acetone, and washed with phosphate-buffered saline. The sections were then treated at room temperature with 0.3 percent hydrogen peroxide diluted in phosphate-buffered saline. The sections were washed with phosphate-buffered saline and then incubated with 10 percent normal human serum for 10 minutes at room temperature to suppress any nonspecific binding. After the excess serum was removed, the sections were incubated for two hours at room temperature with the indicated amounts of biotinylated IgG diluted in phosphate-buffered saline containing 10 percent normal human serum and 0.5 percent Triton X-100. The sections were washed with phosphate-buffered saline and then incubated with avidin–biotin–peroxidase complex (Vectastain ABC complex; Vector) for 30 minutes. The sections were washed again with phosphate-buffered saline, and the substrate reaction developed with 0.05 percent diaminobenzidine hydrochloride.16
Results
Protein extracts were prepared from Purkinje cells, nonneoplastic tissue, and tumor tissue from patients with paraneoplastic cerebellar degeneration and then separated by 8 percent polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate and 2-mercaptoethanol. The separated proteins were transferred to nitrocellulose and incubated with a high-titer anti-Yo IgG. Western blotting revealed a band identical in size to that for CDR 62 in all seven of the extracts of tumor tissue from patients with paraneoplastic cerebellar degeneration that were tested, but not in the extracts of tissue from controls (Fig. 1Figure 1
Western Blot Analysis of Tumor Tissue from Patients with Paraneoplastic Cerebellar Degeneration.A and Table 1Table 1
Expression of Yo Antigen in Tumor Tissue of Patients with or without Paraneoplastic Cerebellar Degeneration.*). To determine whether the proteins detected in tumor tissue were recognized specifically by anti-Yo autoantibodies, tumor extract from Patient 2 was separated by preparative 8 percent polyacrylamide gel electrophoresis and transferred to nitrocellulose. The nitrocellulose sheet was then cut into strips of equal size and incubated with various control and anti-Yo—positive serum and cerebrospinal fluid samples. In all four preparations of tumor extract incubated with anti-Yo antibodies (three from cerebrospinal fluid and one from serum), a 62-kd band was present (Fig. 1B, lanes 3 through 6). In contrast, in samples incubated with normal human serum and serum from a patient with breast cancer but no neurologic disorder, only a 55-kd band was present, which corresponds to the heavy chain of IgG. The 55-kd band was detected in the absence of added antibody and indicates direct binding of 125I-labeled protein A. A similar analysis was performed on all 7 samples of tumor tissue available from patients with paraneoplastic cerebellar degeneration and on 21 samples of ovarian and breast tumors from patients who had no clinical signs of paraneoplastic cerebellar degeneration. As can be seen in Figure 2Figure 2Analysis of Expression of CDR 62 in Samples of Breast and Ovarian Tumors from Neurologically Normal Patients and from a Patient with Paraneoplastic Cerebellar Degeneration. and Table 1, CDR 62 was selectively expressed in the tumor tissue from the patients with paraneoplastic cerebellar degeneration.Previous attempts to demonstrate the expression of the Yo antigens in tumor tissue from patients with paraneoplastic cerebellar degeneration by conventional immunohistochemical methods that use human serum have been unsuccessful because the more forceful reaction of the secondary antibody reagent (goat anti-human IgG) with endogenous IgG obscures the expression of the Yo antigens. In a Western blot analysis endogenous IgG can be easily identified by its molecular weight and antibody-dependent reactivity with protein A. To develop an immunohistochemical assay for the Yo antigens, we covalently conjugated the primary antibody (anti-Yo IgG) to biotin. The histochemical detection of this biotinylated antibody does not require a secondary reagent and can be visualized with use of the avidin–biotin–peroxidase complex. Anti-Yo IgG and normal human IgG were conjugated to biotin as described in Methods and assayed according to their reactivity with cerebellar sections. Biotinylated IgG from anti-Yo serum or cerebrospinal fluid reacted with Purkinje cells in a manner similar to that of untreated serum (Fig. 3Figure 3
Frozen Sections of Human Cerebellum Incubated with Biotinylated IgG (1 μg per Milliliter) from Normal Subjects (Panel A) and from a Patient with Paraneoplastic Cerebellar Degeneration (Panel B) (Avidin–Biotin–Peroxidase Complex with Hematoxylin Counterstain, ×50).).3 4 5 6 The reaction was detectable at 0.3 μg of biotinylated IgG per milliliter, and the intensity of staining increased proportionately with increasing IgG concentrations until saturation was reached at 6 μg per milliliter. In a comparable range of concentration, biotinylated IgG prepared from normal human serum (i.e., from patients without paraneoplastic cerebellar degeneration) did not specifically stain any structure in the cerebellum (Fig. 1). All sections assayed were from the same sample of cerebellum and contained the same number of Purkinje cells. When relatively high concentrations (30 μg per milliliter) of human IgG were used, there was weak staining of Purkinje-cell nuclei, but the typical granular cytoplasmic staining seen with anti-Yo was not present.Immunohistochemical screening with biotinylated anti-Yo revealed selective staining of tumor cells from all 10 patients with paraneoplastic cerebellar degeneration (Fig. 4Figure 4
Reaction of Normal and Anti-Yo Biotinylated IgG with Tumor Tissue from Patients with or without Paraneoplastic Cerebellar Degeneration. and Table 1), regardless of which patient served as the source of the IgG. None of the tumor cells from the 21 controls were positive (Fig. 4). Biotinylated IgG from normal human serum prepared in the same way as the anti-Yo serum did not react with any of the tumor samples (Fig. 2B). The numbers of tumor cells reacting with the anti-Yo serum varied from a few (but always more than 10 percent) to virtually every cell. When serum was incubated with tumor tissue from a lymph node, the lymphocytes did not react. In all specimens the reaction appeared to be cytoplasmic.We next sought to determine whether the antigens identified in the tumor tissue from patients with paraneoplastic cerebellar degeneration were identical to those in Purkinje cells. Anti-Yo biotinylated IgG that specifically recognizes the CDR 62 species expressed in Purkinje cells was affinity-purified by adsorption to and elution from a preparative Western blot. A negative control was provided by the elution of material from an irrelevant area of the nitrocellulose sheet after Western blotting. The CDR 62 biotinylated IgG reacted specifically with tumor cells from patients with paraneoplastic cerebellar degeneration. The negative control showed no reactivity (Fig. 5Figure 5
Adjacent Frozen Sections of Ovarian Tumor Tissue from Patient 2 Reacted with a Control IgG Eluate (Panel A) and Affinity-Purified Anti-CDR 62 Biotinylated IgG (Panel B) (Avidin–Biotin–Peroxidase Complex with Hematoxylin Counterstain, ×50).).These data demonstrate that breast and ovarian carcinomas from patients with paraneoplastic cerebellar degeneration express a gene product characteristic of Purkinje cells. To determine whether such tumors express other genes characteristic of Purkinje cells or neurons in general, tumor tissue from Patient 1 was subjected to Western blot analysis with human autoantibodies that recognize other Purkinje-specific antigens (anti-Nb)17 and neural antigens that are expressed in all classes of neurons (anti-Hu and anti-Ri) (Fig. 6Figure 6
Reactivity of Tumor Tissue from Patients with Paraneoplastic Cerebellar Degeneration with Other Neural-Specific Autoantibodies.).18 , 19 Neither the Purkinje-cell-specific antigens recognized by anti-Nb nor the neural antigens recognized by anti-Hu and anti-Ri were expressed in tumor tissue from patients with paraneoplastic cerebellar degeneration (Fig. 6B). A control sample in which purified Purkinje cells were used as the antigen source was reactive to all the autoantibodies (Fig. 6A).The detection of anti-Yo antibody in the serum was a crucial factor in the treatment of three of our patients. Because the antibody is closely associated with gynecologic tumors, its presence narrowed the search for cancer in these patients. In Patient 8, who was 26 years old, a second set of mammograms revealed a suspicious area that biopsy showed to be a breast cancer. In Patient 6, a diagnostic dilation and curettage revealed an asymptomatic uterine cancer. After all other diagnostic tests were negative, a laparotomy, hysterectomy, and salpingo-oophorectomy in Patient 4 revealed cancer of the fallopian tube identifiable only microscopically.
Discussion
A fundamental issue in all paraneoplastic neurologic syndromes is the causative link between the occurrence of the primary tumor and the nervous system disorder. At least two models have been proposed to explain this linkage. In the first, tumor cells secrete some neurotoxic or neuromodulating substance that causes the neurologic disease. There is a precedent for this model, since some tumor cells associated with other paraneoplastic syndromes (small-cell lung cancer cells) secrete neuroendocrine peptides.20 Neuromodulating substances that are specific for the cerebellum have not been identified in patients with paraneoplastic cerebellar degeneration, but this does not prove that substances toxic to the cerebellum do not exist. Moreover, since the functions of the two Yo antigens (CDR 34 and CDR 62) are currently unknown, we cannot dismiss this model. If either CDR 62 or CDR 34 is a specific neuromodulating substance, the aberrant expression of such molecules outside the central nervous system might lead them to compete with those normally expressed in the cerebellum, and such competition might result in a cerebellar lesion.
In the second model, which we favor, an immune response is invoked that is directed against a tumor antigen. If the tumor antigen corresponds to a specific cerebellar neural protein, the tumor-generated immune response might be misdirected specifically against Purkinje-cell neurons in the cerebellum, with disastrous effects on the function of the cerebellum. Our results support this model of paraneoplastic cerebellar degeneration. Tumors from patients with paraneoplastic cerebellar degeneration express a specific Purkinje-cell protein, CDR 62, that has not been detected in the breast and ovarian tumors of patients without paraneoplastic cerebellar degeneration. Similar results have also recently been found by Dropcho et al. (personal communication). We have also recently documented the expression of the minor Yo antigen (CDR 34) in a single tumor from a patient with paraneoplastic cerebellar degeneration, using a rabbit antibody directed against the cloned gene product.9 Our present working hypothesis is that paraneoplastic cerebellar degeneration is a result of an immunologic response directed against the Purkinje cell but provoked by tumor-induced expression of a highly specific neural antigen. Since this immune response is not strictly autoimmune (since the tumor is not "self"), we propose that it be termed the "anti-onconeural immune response."
There are several ways in which an anti-onconeural immune response might cause the loss of cerebellar function. These include the destruction of Purkinje cells by cytotoxic T cells, a direct antibody-mediated cytotoxicity reaction, or antibody-mediated inhibition of CDR 62 and CDR 34. An analysis of the nature of the lymphocytes associated with the lesion may show which of these possibilities is correct. It is clear, however, that a physiologic assay employing an animal model must be devised to test the putative pathogenic effect of this anti-onconeural immune response. The hypothesis is also strengthened by our recent observation that the anti-Yo antibody is synthesized in the central nervous system of patients with paraneoplastic cerebellar degeneration,21 indicating that such an anti-onconeural immune response can cross the blood–brain barrier to involve the central nervous system directly.
The findings reported here for paraneoplastic cerebellar degeneration are similar to those described for the Lambert-Eaton myasthenic syndrome,22 , 23 the paraneoplastic sensory neuronopathy-encephalomyelitis syndrome,24 , 25 and cancer-associated retinopathy, all of which are associated with small-cell lung cancer.26 , 27 A specific anti-onconeural response has also been described in these syndromes.22 23 24 25 26 27 However, the expression of the onconeural antigen in these disorders, unlike paraneoplastic cerebellar degeneration, is not confined to tumor tissue from patients with the neurologic syndrome.
Although paraneoplastic cerebellar degeneration is a rare complication of cancer, the investigation of this and other antibody-associated paraneoplastic syndromes may well yield insights into poorly understood aspects of immunology. One of these concerns the relation between the immune system and cancer in general. The Yo antigens CDR 62 and CDR 34 can be considered Class II tumor antigens — that is, antigens shared by some tumors and some normal tissues.27 , 28 These antigens are not uncommon, and many, particularly oncofetal antigens, are used as markers to suggest the presence of an underlying cancer or to follow the course of treatment of a previously discovered cancer. It is, however, decidedly unusual to find high titers of antitumor antibodies in the serum of patients with cancer whether or not specific antigens are identified in the tumor. The paucity of this kind of information may reflect the difficulties in assaying the reaction of human IgG with human tumor tissue. Our initial attempts to use human serum to investigate the expression of the Yo antigens were unsuccessful because of the presence of large amounts of endogenous IgG in tumor tissue. The use of biotinylated IgG and an avidin–biotin–peroxidase detection system allowed us to demonstrate the expression of the Yo antigen. Thus, it is possible that antitumor antibodies exist in many patients with cancer but have not yet been detected.
Our findings also offer insight into the relation between the immune system and proteins specifically expressed in neurons. The brain has traditionally been viewed as an immunologically privileged site.29 Indeed, the fact that the expression of major-histocompatibility-complex (MHC) antigens is undetectable in brain tissue suggests that proteins specifically expressed in neuronal cells (e.g., the Yo antigens) may not have been presented to the immune system during the establishment of immune tolerance.30 Such neuronal-specific proteins, although obviously "self," may therefore be regarded as "foreign" by the immune system. In normal persons, these "foreign" neuronal proteins are not recognized by the immune system, since they are expressed only in cells without MHC. The implication is that the expression of neuronal-specific proteins in a tumor tissue that expresses MHC may result in a profound immune reaction. We speculate that the exaggerated antitumor response we noted in the patients with paraneoplastic cerebellar degeneration may result from the de novo (de novo with respect to extraneural tissues) expression of such a neuronal-specific protein (the Yo antigen) in tumor tissue. Although the antigens described here are not evident on the surface of the tumor cell, it is reasonable to assume that they are present on the surface of the cell in conjunction with MHC Class I. The cloning of the Yo antigens and their directed expression in extraneural tissues of transgenic mice may provide an experimental system with which to investigate these interactions.
Supported in part by grants from the National Institutes of Health (NS26064) and the American Cancer Society (PDT-359), and by funds from the Fondo de Investigaciones Sanitarias de la Seguridad Social, Instituto Nacional de la Salud, Ministerio de Sanidad y Consumo, Madrid.
We are indebted to Kin Kong for preparing the photomicrographs.
Source Information
From the Departments of Neurology (H.M.F., J.D., E.W., P.W., J.B.P.) and Pathology (M.K.R), Memorial Sloan-Kettering Cancer Center, New York; Cornell University Medical Center, New York(H.M.F., J.B.P.);and the Department of Neurology, Hospital Clinic, Barcelona, Spain (F.G.). Address reprint requests to Dr. Furneaux at the Department of Neurology, Memorial Sloan-Kettering Cancer Center, 1275 York Ave., New York, NY 10021.
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