Distribution Of S-100 Protein Research Articles

Demonstration of S-100 protein distribution in human lymphoid tissues by the avidin-biotin complex immunostaining method

Immunoreactivity for S-100 protein was investigated immunohistochemically in a series of 49 fixed and paraffin-embedded normal, reactive, and neoplastic human lymphoid tissue specimens. The avidin-biotin complex immunoperoxidase method was used, with overnight (12-hour) incubation with a commercially available antiserum to S-100 protein. In addition, cryostat sections were tested with DRC 1 monoclonal antibody to dendritic reticulum cells (DRCs) in three cases and with OKT6 antibody to interdigitating reticulum cells (IRCs) in nine cases. All tissues, including lymph nodes, tonsils, adenoid, spleens, appendices, thymuses, and tissues containing nodular reactive lymphoid infiltrates, demonstrated a consistent immune staining pattern. A striking network composed of dendritic processes that showed finely granular S-100 protein immunoreactivity was observed in most of the follicular germinal centers; a similar dendritic pattern was observed in the follicular centers when the corresponding frozen sections were immunostained with DRC 1. In the extrafollicular areas, the S-100-positive cells topographically and morphologically resembled the IRCs that were demonstrated by OKT6 antibody in the corresponding frozen sections. The results seem to indicate that cells topographically and morphologically similar to IRCs and DRCs in human lymphoid tissues from different sites share immunoreactivity for S-100 protein. The present study confirms the unexpected presence of S-100 protein in dendritic cells of follicular germinal centers by a simple and currently available method.

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

Immunohistochemical localization of S-100 protein, its alpha and beta 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 alpha and beta subunits of S-100 protein showed almost identical distribution in normal and neoplastic salivary glands, but skeletal muscle cells were alpha-positive/beta-negative whereas Schwann cells and fat cells were alpha-negative/beta-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.

Immunohistological demonstration of S-100 protein in the cutaneous nervous system.

S-100 protein, isolated from mammalian brain, has widely been used for immunohistochemical marker of the glia cells and the cells derived from the neural crest. In the present study, we made anti S-100 protein antibody and studied the immunoreactive distribution of S-100 protein in the cutaneous nervous system. Albino rabbits were immunized with S-100 protein and complete Freund adjuvant, and antiserum was purified by ion-exchange chromatography. Formalin-fixed normal human skin and sciatic nerve of rat were examined by the PAP method. S-100 protein was detected in Schwann cells of sciatic nerve of rat and cutaneous nerve bundles of human skin specimens. Meissner corpuscles and inner core cells of Pacinian corpuscles of human skin were S-100 protein positive. These findings suggest that the staining of S-100 protein with PAP method is a simple and reliable method to demonstrate the cutaneous nervous system. Also, lamellar cells of Meissner corpuscles and inner core cells of Pacinian corpuscles are indicated to be Schwann cell origin.

STUDIES ON THE IMMUNOHISTOCHEMICAL LOCALIZATION OF S-100 AND GLIAL FIBRILLARY ACIDIC PROTEINS IN HUMAN BRAIN TUMORS

The presence and distribution of S-100 protein and glial fibrillary acidic protein (GFAP) were studied immunohistochemically in surgical and autopsy specimens from 130 human brain neoplasms. 115 cases of them were investigated in formalin-fixed paraffin embedded tissue, using the peroxidase-anti-peroxidase method, and in 37 cases cryostat sections were studied by direct immunoperoxidase or indirect immunoperoxidase method. In a case of astrocytoma immunoelectron microscopy was carried out to establish the ultrastructural localization of GFAP. The antisera raised against S-100 protein from bovine brain and GFAP from human astrocytoma in rabbits were used.Both paraffin and cryostat sections were investigated for GFA and S-100 proteins. Similar staining patterns were obtained, but cryostat sections demonstrated finer staining figures. By electron microscopy the reactive product for GFAP was found on glial filaments and diffusely throughout cytoplasm of neoplastic astrocyte.Positive immunostaining for GFA and S-100 proteins was observed in the glial neoplasms. Constituent cells of astrocytoma were found to contain S-100 protein in their nuclei and cytoplasms. GFAP was present in perikarya and processes. Rosenthal fibers and rounded granulated bodies showed different staining patterns for both protains. In malignant astrocytoma GFAP-negative small anaplastic cells were intermingled with positive neoplastic astrocytes, but some of the negative cells were stained for S-100 protein. Glioblastoma demonstrated variable immunoreactivity for both proteins from cell to cell and from case to case. In subependymal giant cell astrocytoma, most component cells stained for S-100 protein, but most of the component giant cells were negative for GFAP. In oligodendroglioma, immunoreactive material for GFAP was present in scanty cytoplasms of some tumor cells showing clear halo, and most cells were positive for S-100 protein. In mixed oligoastrocytoma a varying number of pale cells comprising area of oligodendroglioma showed similar staining pattern for GFAP. The finding suggests the presence of cells forms intermediate between oligodendroglia and astrocyte. In ependymoma, fine cytoplasmic processes forming perivascular pseudorosette were positive for both proteins, but the cells forming ependymal rosette were negative. A network of glial fibers constituting basic architecture of subependymoma was stained for both proteins, however some of the small component cells were negative for GFAP. In medulloblastoma, GFAP and S-100 protein-positive cells with processes were found around the stroma. In a case of desmoplastic medulloblastoma, cells staining for both proteins were present in pale area.In neuronal cell tumors, neuroblasts and mature nerve cells did not contain these proteins, but in a cerebral neuroblastoma S-100 protein-positive cells with long processes were found around blood vessels.S-100 protein was present in the component cells of neurilemmoma and choroid plexus papilloma. In 6 of 33 cases of meningioma, neoplastic cells contained S-100 protein, and in another 3 cases astrocytic cells with staining for both S-100 protein and GFAP were found in the stroma. Stromal cells in hemangioblastoma were negative for GFAP, although the tumor had scattered groups and fibers positive for both proteins.Osteochondroma and malignant melanoma were the other types of tumors which contained S-100 protein. Tumor cells of pituitary adenoma, craniopharyngioma, malignant lymphoma, germinoma and metastatic carcinoma did not contain either S-100 protein or GFAP.It is considered that the investigation of localization of S-100 protein and GFAP in brain neoplasms is helpful for classifying and precise identification.

S-100 protein distribution in liposarcoma. An immunoperoxidase study with special reference to the distinction of liposarcoma from myxoid malignant fibrous histiocytoma.

The presence and distribution of S-100 protein were studied in 63 cases of liposarcoma and 20 cases of myxoid malignant fibrous histiocytoma (MFH), using the immunoperoxidase technique. Normal adipose tissue and benign lipomatous tumours were also studied by the same technique, for purposes of comparison. In all liposarcomas, most of the adipocytes and vacuolated lipoblasts were positive for S-100 protein, although the tumour cells in non-lipogenic areas of dedifferentiated liposarcoma and the non-vacuolated giant cells with a deeply eosinophilic cytoplasm in the pleomorphic liposarcomas were devoid of S-100 protein immunoreaction products. One third of the myxoid type liposarcomas contained numerous immunoreactive, immature-appearing spindle or oval cells, reminiscent of the primitive fat organs of white adipose tissue. Conversely, none of the myxoid MFHs contained S-100 protein in the tumour cells, including the irregularly vacuolated ones. These results suggests that the immunohistochemical demonstration of S-100 protein is a useful diagnostic tool, particularly for the assessment of vacuolated tumour cells and for the diagnosis of myxoid tumours.

Immunohistochemistry of folliculo-stellate cells in normal human adenohypophyses and in pituitary adenomas.

Presence and distribution of S-100 protein (S-100), neuron-specific enolase (NSE), cytokeratin polypeptides, glial fibrillary acidic protein (GFAP), vimentin, actin, lysozyme and pituitary hormones (prolactin, hGH, ACTH, beta-FSH, beta-LH, beta-TSH, alpha subunit) in folliculo-stellate cells (FSC) were studied in seven normal human pituitary glands and 28 pituitary adenomas using peroxidase-antiperoxidase and the avidin-biotin immunohistochemical techniques. Approximately 5% of the cells of the adenohypophysis were agranular, non-hormone-producing FSC most of which showed a conspicuous and strong reaction with S-100 antibodies but some were, in addition, GFAP- and vimentin-positive. In contrast to endocrine cells (EC), FSC were not decorated by antibodies to NSE or cytokeratins. In addition to supportive functions, these cells, due to their close special relationship to EC, seem to have transport and other metabolic functions yet to be elucidated. By their S-100 reactivity and their distribution FSC are comparable to glial cells of the central and Schwann and satellite cells of the peripheral nervous system (PNS) as well as to supportive cells in neuroendocrine organs and related tumors (e.g., pheochromocytomas, paragangliomas, carcinoids). With one exception, S-100 reactive FSC were not found in pituitary adenomas. The immunohistochemical demonstration of S-100 protein in pituitary tissue is, therefore, a reliable aid in the discrimination between adenomas and normal pituitary tissue, particularly in small and poorly preserved specimens.(ABSTRACT TRUNCATED AT 250 WORDS)

Distribution of S-100 protein and glial fibrillary acidic protein in normal and gliotic human retina

Monoclonal antibodies and polyclonal antisera were used to examine the distribution of S-100 protein in human retinas both immunohistochemically and immunochemically and to compare it to that of glial fibrillary acidic protein (GFAP). S-100 was not found in normal retinas nor in retinas with areas of reactive gliosis. GFAP was found in perikarya and processes of cells the nuclei of which were in the nerve fiber layer of normal retina. In areas of reactive gliosis there was intense staining with antiserum against GFAP extending from the internal limiting membrane to the external limiting membrane. Some of the glial cells in human retina and fibrillary astrocytes in the brain are identical in their expression of GFAP. However, absence of S-100 from both quiescent and reactive retinoglia distinguishes them from astrocytes in brain and spinal cord.

The value of immunohistochemical studies using antibody to S100 protein in dermatopathology.

The distribution of S100 protein in normal skin and various tumors involving skin was assessed using rabbit antibody to S100 protein in an immunoperoxidase reaction. In normal skin, S100 protein was detected in the epidermis (melanocytes and Langerhans' cells), dermis (Schwann cells, Pacinian and Meissner's corpuscles, and interdigitating reticulum cells), cells of the sweat gland apparatus, and in chondrocytes. In tumors involving skin, S100 protein was present in nevi, malignant melanomas, histiocytosis X, mixed sweat gland tumors, neural tumors, chondromas, and chondrosarcomas. Detection of S100 protein by immunostaining was useful in understanding the histogenesis of various skin tumors and in assessing the diagnosis and prognosis of a variety of skin lesions encountered in surgical pathology.

Distribution of immunoreactive S-100 protein in pediatric brain tumors.

The distribution of S-100 proteins was examined in 98 pediatric brain neoplasms with rabbit antiserum to S-100 protein, utilizing the peroxidase-antiperoxidase (PAP) immunohistochemical technique. Positive cytoplasmic immunoreactivity was present in 22 of 24 astrocytomas, both oligodendrogliomas, eight of 13 ependymomas, all 11 choroid plexus tumors, all nine schwannomas, two of six meningiomas, and both meningeal melanomas. Mixed cytoplasmic immunoreactivity was present in both gangliogliomas, all seven craniopharyngiomas, and the only hemangioblastoma. No cytoplasmic immunoreactivity was found in primitive neuroectodermal tumors or germinoma. Nuclear immunoreactivity was present in some cases. Because of the broad spectrum of apparent immunoreactivity with S-100 antiserum, S-100 protein cannot be used as a specific marker of glial or Schwann cell tumors.

S-100 protein in "follicular dendritic" cells or rat lymphoid organs. An immunochemical and immunocytochemical study.

The presence as well as the cellular and subcellular distribution of S-100 protein were investigated in lymphoid organs of the adult rat by quantitative microcomplement fixation assay and by the immunocytochemical PAP method at the ultrastructural level. The protein appeared to be confined to the "follicular dendritic" cells both in the lymph node and the spleen, which are known to be exclusively associated with B lymphocytes in secondary follicles. The present data show an additional location for S-100 outside the nervous system. The protein may also be a useful tool to provide information on the origin and function of "follicular dendritic" cells, which are still poorly understood.

An immunoperoxidase study of S-100 protein distribution in normal and neoplastic tissues.

The presence of S-100 protein was immunohistochemically studied in many types of formalin-fixed and paraffin-embedded tumors (260 cases). Peripheral nerve tumors, i.e., schwannomas, neurofibromas, granular cell tumors, and neurogenic sarcomas were demonstrated to contain variable amounts of S-100 protein in the tumor cell cytoplasm and nuclei. In ganglioneuromas and ganglioneuroblastomas, neoplastic Schwann cells or satellite cells were positive for S-100 protein. About one-half of the cases of carcinoid tumors stained weakly for S-100 protein. In addition to these nervous tissue and carcinoid tumors, chondrosarcoma, chordomas, pleomorphic adenomas of the salivary gland, and Langerhans cell granulomatosis were also shown to produce S-100 protein. In many types of breast tumors and other lesions, S-100 protein positive cells were likely to correspond to the distribution of myoepithelial cells. These results indicate that S-100 protein is not strictly specific to nervous tissue and its tumors; however, the immunohistochemical demonstration of S-100 protein can be a useful diagnostic tool in tumor diagnosis.

Distribution of S-100 protein outside the central nervous system

The distribution of S-100 outside the central nervous system in humans and rats was explored using antiserum to S-100 and the peroxidase anti-peroxidase method of Sternberger. In peripheral nerves the Schwann cells and the outermost part of the myelin sheaths were stained; axons were not. In dorsal root ganglia and ganglia of the autonomic nervous system only satellite cells were stained. In the adrenal medulla a considerable number of cells were stained. In all other organs studied Schwann cells and satellite cells of ganglia were the only elements that were stained. We conclude that S-100 could serve as a marker for Schwann cells in situ.

S-100 protein in the breain of hypothyroid adult rats: an immunochemical and immunocytochemical study

The levels and the distribution of S-100 protein were studied in the brain of hypothyroid adult rats. The concentration of the protein was significantly increased in the soluble fraction of hypothyroid rat brain as compared with controls ( P < 0.001). This finding probably reflects the increased number of astroglial cells, which has been widely reported in hypothyroid adult rats. The immunocytochemical ultrastructural distribution of the protein in the cerebellar cortex was not affected by thyroid deficiency. The protein was thus confined to the cytoplasm and the nucleus of the astroglial cells both in treated and untreated rats.