Immunohistochemical distribution of S-100 protein and glial fibrillary acidic protein in normal and neoplastic salivary glands

Summary Immunohistochemical localization of S-100 protein, its and subunits, and glial fibrillary acidic protein (GFAP) in normal and neoplastic salivary glands was studied by the peroxidase-antiperoxidase method and immunoblot analysis. Positive immunostaining for S-100 protein was observed in pleomorphic adenoma, adenolymphoma, tubular adenoma, adenoid cystic carcinoma, acinic cell tumour, adenocarcinoma and carcinoma in pleomorphic adenoma. S-100 protein was localized in myoepithelial cells, epithelial cells of intercalated ducts and serous acinar cells of normal salivary gland. Both and subunits of S-100 protein showed almost identical distribution in normal and neoplastic salivary glands, but skeletal muscle cells were -positive/-negative whereas Schwann cells and fat cells were -negative/-positive in the stroma and neighbouring tissue. GFAP was only found in pleomorphic adenoma and its malignant counterpart. Immunoblot analysis showed that the GFAP-related antigen consisted of several polypeptide bands with a molecular weight ranging between 35,000 to 50,000 daltons.     

An immunohistochemical study on the distribution of glial fibrillary acidic protein, S-100 protein, neuron-specific enolase, and neurofilament in medulloblastomas

In order to clarify the differentiation of medulloblastomas, the authors studied on the morphological features and immunohistochemical expression of glial fibrillary acidic protein (GFAP), S-100 protein, neuron-specific enolase (NSE), and neurofilament (NF) in 31 medulloblastomas. GFAP was detected only in a small number of tumor cells of 5 medulloblastomas; S-100 protein in both small tumor cells and some so-called spongioblastic cells in 16 medulloblastomas; NSE in the more abundant tumor cells and the matrix in 28 medulloblastomas; NF in a few tumor cells of 12 medulloblastomas; GFAP and NF in 2 medulloblastomas, but each of them in different tumor cells. These results suggest that medulloblastomas have a capacity of differentiation along neuronal and/or glial lines. The conventional morphological markers of differentiation in medulloblastomas such as spongioblastic cells and Homer Wright rosettes were not necessarily compatible with expression of immunohistochemical markers such as GFAP or NF. NSE and S-100 protein seem less valuable markers of differentiation because they were detected in both neuronal and glial elements. But NSE, which was observed in most medulloblastomas, might have a value as a marker for medulloblastomas.     

An immunohistochemical study of pleomorphic adenomas of the salivary gland: glial fibrillary acidic protein-like immunoreactivity identifies a major myoepithelial component

An immunohistochemical study of 34 pleomorphic adenomas of the major salivary glands demonstrated phenotypic differences among the various morphologic regions in these tumors. The phenotypes expressed were comparable to those of normal salivary gland cells. In the normal glands, myoepithelial cells were immunoreactive for glial fibrillary acidic protein (GFAP), S-100 protein, and keratin; acinic cells exhibited strong, predominantly nuclear S-100 staining and weaker keratin staining; intercalated ducts had both cytoplasmic and nuclear S-100 positivity; and several epithelial antigens were observed throughout the ductal system. In the tumors, the presence of classic epithelial markers (including carcinoembryonic antigen, epithelial membrane antigen, secretory component, and keratin) in the luminal cells of ducts and the intense immunoreactivity with GFAP (with weaker keratin and S-100 staining) in periductal and stromal cells indicated distinct epithelial and myoepithelial differentiation. Solid epithelioid areas consisted phenotypically of intercalated duct/acinic cells and/or myoepithelial cells, the former exhibiting predominant nuclear S-100 positivity. The presence of GFAP-like immunoreactivity in normal myoepithelial cells strongly supports the extensive involvement of this cell in pleomorphic adenomas. The spectrum of phenotypes expressed adds weight to existing evidence for pleomorphism rather than a mixed origin of this tumor. The combination of keratin, S-100, and GFAP immunostaining is particularly useful in identifying the component cells in pleomorphic adenomas of the salivary glands.     

Expression of S-100 protein and glial fibrillary acidic protein in cultured submandibular gland epithelial cells and salivary gland tissues. Histogenetic implication for salivary gland tumors.

S-100 protein and glial fibrillary acidic protein (GFAP) were studied in human salivary gland tissues and human cultured submandibular gland epithelial cells. Immunohistochemically, ductal cells in normal salivary gland tissues were positive for S-100 protein and GFAP, but myoepithelial cells were uniformly negative. Immunocytochemically, cultured submandibular gland ductal cells were positive for S-100 protein and GFAP. By immunoblotting analysis of the cultured cell lysates, a 6.5-kd S-100 protein was detected. This band corresponded to S-100 protein purified from bovine brain. The cultured submandibular gland cells expressed 49- and 54-kd GFAP polypeptides. These results have important implications for the histogenesis of salivary gland tumors.     

Localization of S-100 protein and glial fibrillary acidic protein-related antigen in pleomorphic adenoma of the salivary glands

Pleomorphic adenoma of the salivary glands was studied by the peroxidase-antiperoxidase method and Ouchterlony's double diffusion for the presence of so-called nervous system-specific proteins, S-100 protein, glial fibrillary acidic protein (GFAP), and astroprotein. Positive immunostaining for S-100 protein was observed in tumor cells of epithelial, myxomatous, and chondroid areas. An immunodiffusion test confirmed its presence in the tumor. Normal salivary glands were also stained with anti-S-100 serum, but the reaction was less intense than that of tumor. Specific immunostaining for GFAP and astroprotein was found in a small number of cells of myxomatous and chondroid areas and occasionally in cells in epithelial areas. An immunodiffusion test suggests that the GFAP-related antigen of the pleomorphic adenoma showing a minor heterogeneity of antigenic determinants is almost identical with GFAP. Normal salivary glands did not stain with GFAP or astroprotein antisera, nor did they react with anti-GFAP serum by immunodiffusion. Thus, the S-100 protein and GFAP-related antigen may be actively synthesized in adenoma cells during the course of tumor development. In addition, the GFAP-related antigen is considered to be a tumor-associated antigen of pleomorphic adenoma of the salivary glands.     

Immunohistochemical investigation of vimentin, neuron-specific enolase, alpha 1-antichymotrypsin and alpha 1-antitrypsin in adenoid cystic carcinoma of the salivary gland

Fifty-four adenoid cystic carcinomas (ACC) arising in major and minor salivary glands as well as in normal salivary glands were studied by immunohistochemistry for the presence of vimentin, neuron-specific enolase (NSE), alpha 1-antichymotrypsin (alpha 1-ACT) and alpha 1-antitrypsin (alpha 1-AT). Five patterns of histological differentiation were found in ACC, and for the cellular components of each, it was possible to establish a special immunohistochemical profile. In ACC, vimentin-positive cells were observed in the outer tubular, cyst-lining and small angular cells. NSE was positive in the myoepithelial cells of normal salivary gland. Neoplastic cells of ACC showed NSE positivity mainly in the small angular cells and partly in the duct luminal cells. alpha 1-ACT was localized in the intercalated duct cells and serous acinar cells of normal salivary gland, and in the duct luminal cells of ACC. alpha 1-AT could not be detected in any of the epithelial cells of normal salivary gland. In ACC, eosinophilic hyaline material in the cribriform spaces was positive for alpha 1-AT, but no positivity was demonstrated in tumor cells. The present study showed that there are at least two populations of tumor cells in ACC: duct luminal cells that express alpha 1-ACT, thus indicating their ductal character, and small angular cells that express vimentin, characteristic of non-luminal cells. Moreover, our results indicate that alpha 1-AT is a useful marker of basement membrane-like material.     

Immunohistochemical expression of neural tissue markers (neuron-specific enolase, glial fibrillary acidic protein, S100 protein) in ameloblastic fibrodentinoma: a comparative study with ameloblastic fibroma

Formalin-fixed paraffin-embedded sections of three cases of ameloblastic fibrodentinoma (AFD) were studied by the avidin-biotin-peroxidase complex method using antibodies against neuron-specific enolase (NSE), glial fibrillary acidic protein (GFAP) and S100 protein and the results were compared with those in ameloblastic fibroma (AF). A striking histopathological characteristic of AFD was the formation of abortive dentin with various degrees of maturation at the epithelial-mesenchymal tissue interface. Central cells of enamel organ-like epithelia with various stages of abortive dentin induction in AFD were generally positive for NSE. Dental lamina-like epithelial cells also showed positive staining in some areas. No cells were positive for NSE in AF. Positive staining for GFAP was observed in the juxta-epithelial mesenchymal tissue of the formation stage of immature dentin with various numbers of entrapped cells in AFD, but GFAP staining was negative in other mesenchymal and epithelial tissues at other stages. In AF, no GFAP-positive cells were found. There were a few S100 protein-positive cells found in the foci of epithelial components in both AFD and AF. Mesenchymal cells showing a dendritic or spindle shape were positive for S100 protein in some areas of AFD and AF. Although such cells in the mesenchymal component of pigmented AFD were more numerous than in non-pigmented AFD and AF, their distribution pattern in the former condition was basically similar to that in the latter. Although the present results, obtained from conventional immunohistochemical procedures, do not directly reflect the expression of neural crest-derived cells in the dentinogenesis of AFD, such results do not disprove the possibility of the expression of neural proteins probably related to neural crest-derived cells in dentinogenesis under certain pathologic conditions in odontogenic mixed tumors. Such a phenomenon may also occur during dentinogenesis in other odontogenic mixed tumors and in normal tooth differentiation, but at an undetectable level.     

Immunohistochemical localization of intermediate filament and S-100 proteins in several non-endocrine cells of the human pituitary gland

The presence and distribution of glial fibrillary acidic protein, vimentin, neurofilament protein, cytokeratins No. 8 (52 Kd), No. 18 (45 Kd) and No. 19 (40 Kd) and S-100 protein in pituicytes, folliculo-stellate cells, the epithelium of the Rathke's cysts and squamous cell nests of the pars tuberalis were investigated immunohistochemically by the peroxidase-antiperoxidase (PAP) method in eleven normal human pituitary glands. An identical immunostaining pattern was expressed by both folliculo-stellate cells and pituicytes. In both cell types the immunostaining for glial fibrillary acidic protein (GFAP), S-100 protein and vimentin was strongly positive. These results indicate the probable glial origin of the folliculo-stellate cell, and enlarge the group of glial cell types expressing vimentin. The co-expression of cytokeratins No. 8 and 19, both characteristic for simple epithelia, and S-100 protein was evident in the epithelial cells lining the Rathke's cysts and the squamous cell nests of the pars tuberalis. Furthermore, some epithelial cells of the Rathke's cysts co-expressed cytokeratins, S-100 protein and GFAP, a fact seldom reported and only in relation to rare neoplasms. The cytokeratin No. 18, characteristic for glandular epithelia, was not clearly demonstrated. Finally, the neurofilament protein was detected only in axons of the neurohypophysis; no immunopositive cells could be found throughout the adenohypophysis. Similarities in the antigenic patterns of these cell populations and the possible relation with their origin and nature are discussed.     

Immunohistochemical localization of lysozyme, lactoferrin, alpha 1-antichymotrypsin, and alpha 1-antitrypsin in salivary gland of human fetuses.

26 human fetuses were examined to elucidate the immunohistochemical distributions of lysozyme, lactoferrin, alpha 1-antichymotrypsin, and alpha 1-antitrypsin in prenatal salivary glands. Development of fetal salivary glands was divided into 4 stages: The early developmental stage (EDS), the early intermediate developmental stage (EIDS), the late intermediate developmental stage (LIDS), and the late developmental stage (LDS) and were used to compare antigen localization during salivary gland development. Lysozyme (LY) staining was prominent in serous or demilune cells of the mucous acinar compartment. Lactoferrin (LF) was rarely seen in the fetal glands; only trace amounts were seen in serous cells, alpha 1-antichymotrypsin (alpha 1-ACT) was diffusely positive particularly in glandular ducts, alpha 1-antitrypsin (alpha 1-AT) was also diffusely distributed in all salivary gland elements and was more abundant in ductal cells than acinar cells. During the EDS, immunohistochemical staining of LY, LF, alpha 1-ACT, and alpha 1-AT could be observed with glandular intensity increases corresponding to the advance of cytodifferentiation of granular epithelium occurring in the subsequent EIDS and LIDS. Staining intensities were continuous during the LDS even though the amount of those materials in the fetal salivary glands was not of the extent seen in the adult salivary gland. These results suggest that production of LY, LF, alpha 1-ACT, and alpha 1-AT was positive during prenatal development of human salivary glands. The present study discusses the protective roles and defense mechanisms of LY, LF, alpha 1-ACT, and alpha 1-AT in developing human salivary glands.     

Immunohistochemistry of glial fibrillary acidic protein, vimentin and S-100 protein for study of astrocytes in hippocampus of rat

The distribution of astrocytes was studied in the hippocampus of mature Wistar rats. Immunohistochemistry was performed using antibodies against glial fibrillary acidic protein (GFAP), vimentin and S-100 protein and peroxidase anti-peroxidase techniques. Material from fresh-frozen brain, post-fixed in acetone, yielded a complex picture of the glial populations when stained for GFAP. Astrocytes immunoreactive for GFAP were seen in white matter tracts but also in the large dendritic layers of the hippocampus. Frozen material also contained different types of astrocytes following staining with a monoclonal antibody to vimentin. Stellate astrocyte types in the dendritic layers contained vimentin-stained processes. In addition a form of residual radial glia was found in the dentate gyrus. Material from brains perfusion-fixed with formaldehyde remained positive for astrocytic GFAP, but was negative for vimentin. Staining for S-100 protein antibodies revealed numerous astrocytes and diffuse background staining in fixed material. This study allows one to make predictions concerning the use of astrocytic markers in experimental pathological material.     

Cytokeratins, smooth muscle actin and vimentin in human normal salivary gland and pleomorphic adenomas. Immunohistochemical studies with particular reference to myoepithelial and basal cells.

The distribution of immunostaining in normal major salivary gland and in 12 pleomorphic adenomas was studied using monospecific monoclonal antibodies to a number of cytokeratins, including cytokeratin 14, to smooth muscle actin and vimentin. A number of these antibodies enabled a distinction to be made between structural components of the normal gland, and to relate this to the different structures of pleomorphic adenomas. In the normal gland, the luminal duct cells expressed cytokeratins 7, 8, 18 and 19. Three antibodies were of particular value for the characterization of normal myoepithelial and basal cells; while the antibody to smooth muscle actin and the cytokeratin antibody Ks8.12 mutually exclusively stained the myoepithelial (basket) cells and the basal duct (light) cells, respectively, the recently established monospecific antibodies to cytokeratin 14 showed specific immunostaining with both cell types. These three antibodies left luminal cells virtually unstained. Ck 13 was found occasionally in single luminal excretory duct cells. Antibodies to cytokeratins 1/2, 10 and 10/11 did not show any staining in the normal gland. In the pleomorphic adenomas, the staining pattern of the two-layered tubular formation resembled that of the normal gland ducts: tumour luminal cells showed the characteristic, although more irregular, expression of cytokeratins 7, 8, 18 and 19; the outer cells resembled normal ductal basal cells with their anti-cytokeratin 14/Ks8.12-epitope staining and in that they virtually lacked staining for smooth muscle actin. Trabecular formations and cells in myxoid areas were reactive with Ks8.12 and for cytokeratin 14, occasionally also for cytokeratins 7, 18 and 19. Epidermoid cell islets expressed mainly cytokeratin 14 and inconsistently the squamous epithelial cytokeratin 13 and the epidermal cytokeratin 10/11. Vimentin was found in cells of myxoid areas. The results support the postulate that some of the normal duct basal cells act as reserve cells and can give rise to tumour formation with a primitive myxoid or trabecular pattern and a more differentiated tubular or epidermoid configuration.     

Immunohistochemical evaluation of factor VIII related antigen,filament proteins and lectin binding in haemangiomas

Summary Immunohistochemical identification of factor VIII related antigen (F VIII RAG) filament proteins (actin, myosin, filamin, vimentin and desmin) and lectin binding patterns of Con A, PNA, SBA, WGA, RCA-1, UEA-1 and DBA in the endothelial cells and the musclar layers of haemangiomas and normal blood vessels are reported, using paraffin sections with the HRP method.The endothelial cells of haemangiomas were usually strongly positive to F VIII RAG as were those from capillary vessels and other small vessels. Some of the endothelium from haemangiomas and angiokeratomas was negative for factor VIII. The vessel walls of hemangiomas showed staining slightly positive for microfilaments (actin, myosin, filamin). The smooth muscle layer in small vessels showed a more marked staining with actin. Vimentin and desmin reactions in the vessel walls of, haemangioma and in normal vessels were slight or moderate. UEA-1 lectin binding was constantly positive in endothelial cells from hemangiomas and in blood vessels. SBA and WGA binding appeared in the border layer of endothelium in haemangiomas and normal vessels.     

Rosenthal fibers share epitopes with alpha B-crystallin, glial fibrillary acidic protein, and ubiquitin, but not with vimentin. Immunoelectron microscopy with colloidal gold.

Ultrastructural immunoreactivities of alpha B-crystallin, glial fibrillary acidic protein (GFAP), ubiquitin, and vimentin in Rosenthal fibers (RFs) isolated from an Alexander's disease brain were investigated using nonosmium and low-temperature embedding technique. The morphology of RFs embedded in Lowicryl K4M resin was well preserved after treatment with 0.5% Triton X-100. alpha B-crystallin immunoreactivity was present in RFs of various sizes and was the strongest in loosely scattered deposits, which were considered to be the initial stage of RFs. Glial fibrillary acidic protein immunoreactivity in RFs was heavy, homogeneous throughout RFs, and equivalent to that in networks of glial filaments. Immunoreactivities of both alpha B-crystallin and GFAP were mainly restricted to the high electron-dense areas within RFs and were proved to exist close to each other by double immunolabeling. Rosenthal fibers were negative for vimentin. Ubiquitin immunoreactivity was relatively homogeneous in RFs with small diameters, but in RFs with large diameters, the immunoreactivity diminished in the center. Based on these observations, combined with the tendency of self-aggregation of alpha B-crystallin, it is conceivable that RFs are huge aggregation products of alpha B-crystallin involving GFAP, and that ubiquitination may be a consequent phenomenon, as it may be in other intracytoplasmic inclusions, such as neurofibrillary tangles and Lewy bodies.     

Complexity of expression of intermediate filament proteins, including glial filament protein, in endometrial and ovarian adenocarcinomas.

The expression patterns of intermediate filament proteins of primary and metastatic endometrial (n = 18) and ovarian (n = 24) adenocarcinomas were analyzed by immunocytochemistry using a panel of specific antibodies and by gel electrophoresis of cytoskeletal preparations, followed by immunoblotting. All cells of all endometrial adenocarcinomas studied contained the "simple epithelial"-type cytokeratins (CKs) 8, 18, and (mostly) 19, with variable numbers of cells also positive for CK 7 and vimentin. In addition, most of these tumors contained individual cells or groups of cells that were positive for the stratification-related CKs 4, 5, 6, 13, 14, and 17. The latter CKs were often associated with squamous cell foci, but were also found in some single (nonsquamous) tumor cells, indicative of early stages of squamous cell differentiation. Ovarian carcinomas of various histologic types and grades contained predominantly CKs 7, 8, 18, and 19. Serous, endometrioid, and anaplastic tumors, but not mucinous and clear cell tumors, also contained minor amounts of stratification-related CKs in variable combinations, mostly including CK 4. In all tumor types except mucinous tumors, vimentin was consistently detected in variable proportions of tumor cells which, however, were rather low in anaplastic carcinomas. Surprisingly, glial filament protein was detected in a minor proportion (< or = 20%) of tumor cells in seven of 14 serous and endometrioid ovarian carcinomas and in three of 18 endometrial carcinomas. These different intermediate filament expression patterns of müllerian duct-type carcinomas, only partly related to the morphologic appearance of the specific type of tumor, might reflect the multipotentiality of differentiation of müllerian duct-derived epithelia. Cytoskeletal features of potential diagnostic value, especially in metastatic carcinomas, are discussed.     

Importance of immunohistochemistry for neuro-oncology. III. Demonstration of glial fibrillary acidic proteins (GFAP) in anaplastic astrocytomas and glioblastomas

Expression of gliofibrillary acidic protein in 23 anaplastic astrocytomas and 33 glioblastomas has been investigated and correlated with tumor behavior as reflected in both the length of the preoperative history and in the post-operative survival time. Three degrees of positive immunoreactivity to anti-GFAP can be distinguished: positive GFAP reaction in more than 2/3 of cells; in 1/3 to 2/3 of all cells; in less than 1/3 of all cells; negative reaction. All anaplastic astrocytomas and 27 of 33 glioblastomas showed GFAP positive reactions. The proportion of highly reactive tumors is higher by anaplastic astrocytomas than by glioblastomas (7 of 33). For both astrocytomas and glioblastomas there is a tendency for a decrease in the expression of GFAP to be associated with a shorter preoperative history and with a shorter survival time. This is more prominent for astrocytomas than for glioblastomas. This finding supports the opinion expressed in previous publications that the GFAP expression is reversely related to the level of tumor anaplasticity.     

Basaloid carcinoma of salivary glands, a variety of undifferentiated adenocarcinoma. Immunohistochemical study of intermediate filament proteins in 24 cases.

Among adenoid cystic carcinomas of salivary glands (ACCs), the solid basaloid type has a poor prognosis similar to that of undifferentiated adenocarcinomas. We studied 24 cases in immunohistochemistry using antibodies reactive with keratins of various molecular weights, vimentin, S-100 protein, and its A and B subunits. Our findings were correlated with the histological pattern and with the variable degree of differentiation of these carcinomas. In comparison with other types of ACC, intermediate filament proteins in this group were weakly expressed. The co-expression of cytokeratin and vimentin was noted in some cases. Additional features noted were the presence of cribriform cavities associated with solid lobules and areas of necrosis giving a comedocarcinomatous pattern. In these two variants, cells characterized by the dual expression of cytokeratin and S-100 protein were seen. In the highly malignant anaplastic variety, only a few cells were weakly positive with antisera to cytokeratin and vimentin. This group shows similarities to undifferentiated adenocarcinomas of salivary glands. Such similarities could be explained by the common origin of these tumours from intercalated ducts.     

Subepithelial neuroendocrine cells and carcinoid tumours of the human small intestine and appendix. A comparative immunohistochemical study with regard to serotonin, neuron-specific enolase and S-100 protein reactivity

A comparative immunocytochemical study was performed of subepithelial neuroendocrine cells of the human small intestine and appendix and carcinoid tumours of these sites, using a monoclonal antibody to serotonin and polyclonal antisera against neuron-specific enolase (NSE) and S-100 protein. Subepithelial neuroendocrine cells were easily identified in the lamina propria of the appendix. These cells, which sometimes occurred in aggregates, displayed serotonin and NSE immunoreactivity and were surrounded by S-100 protein immunoreactive cells, presumably of Schwann cell origin. In the appendix scattered cells with corresponding morphological features and immunoreactivity were also observed deep in the submucosa. In addition, subepithelial neuroendocrine cells were sparsely present in the lamina propria of the small intestine, occurring only as single cells in the deeper part of the mucosa below or between the epithelial crypts. Most appendiceal carcinoid tumours (11 of 12 examined cases) were biphasic and consisted of neuroendocrine tumour cells with intermingled S-100 protein immunoreactive cells (Schwann cells) with long cytoplasmic extensions. However, small intestinal (11 cases) and caecal (10 cases) carcinoids lacked S-100 protein immunoreactive cells as an integral component. The results indicate that the appendiceal carcinoids are mostly closely related structurally to the subepithelial neuroendocrine and Schwann cell aggregates of the lamina propria and are thus presumed to be histogenetically related to this cell system, while the histogenesis of small-intestinal and caecal carcinoids remains less clear.     

Expression of pan-neuroendocrine proteins in 53 neuroblastic tumors. An immunohistochemical study with neuron-specific enolase, chromogranin, and synaptophysin

The presence and distribution of pan-neuroendocrine markers such as neuron-specific enolase (NSE), chromogranin (CG), and synaptophysin (SYP) were investigated by immunohistochemistry in 53 cases of neuroblastic tumors, including three cases of ganglioneuromas, 17 ganglioneuroblastomas, and 33 neuroblastomas. In ganglioneuromas, all three markers were observed both in ganglion cells and in neurofibrils. All cases of ganglioneuroblastoma were positive for these markers, however, some variability of staining intensity was noted. Of the 33 cases of neuroblastomas, all were positive for NSE, 23 (70%) for CG, and 31 (94%) for SYP. Neuron-specific enolase was detected not only in the majority of the neuroblasts showing signs of differentiation, but also in some undifferentiated neuroblasts. Chromogranin was found mainly in differentiated neuroblasts with enlarged cytoplasm and nuclei, but was scarcely found in undifferentiated cells. Synaptophysin was detected in some undifferentiated neuroblasts, as well as in differentiated neuroblasts. Two cases without SYP-positive cells were also negative for CG. Our observations conclude that antibodies against NSE and SYP are helpful as a diagnostic aid for neuroblastic tumors.     

Expression of glial fibrillary acidic protein in the CNS and PNS of murine globoid cell leukodystrophy, the twitcher.

The expression of glial fibrillary acidic protein (GFAP) was found to be markedly enhanced immunohistochemically and biochemically both in the central (CNS) and peripheral (PNS) nervous systems of the twitcher mutant, an authentic murine model of human globoid cell leukodystrophy. The astrocytes in the CNS, the unmyelinated Schwann cells in the sciatic nerve, and the satellite cells in the trigeminal ganglion stained heavily with anti-GFAP antiserum. These changes in GFAP expression occurred shortly before the initiation of demyelination and coincided chronologically and topographically with infiltration of macrophages, suggesting that the same or closely related factors trigger the infiltration of macrophages and activate expression of GFAP. Cytoskeletal protein preparations showed increases in GFAP as well as in vimentin in the brainstem, spinal cord, and sciatic nerve. These results demonstrate that at least two types of peripheral glia (the unmyelinated Schwann cell and the satellite cell), in addition to the astrocyte, respond to some pathologic stimuli with an increased expression of GFAP. However, two other GFAP-positive structures, the Bergmann and radial glia, showed no significant changes in their immunostaining.