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B F Odermatt

Publications and source records attributed to B F Odermatt.

49 records · Page 3Linked to original sources
PubMed1986

[Cytodiagnosis and marker determination in pleural effusion].

Malignant cells can be identified in 70-85% of all tumor-induced serous effusions by cytological examination. Carcinoma and malignant lymphoma can be frequently found in pleural fluids, while sarcoma is rare. In many cases, morphological criteria allow these tumors to be distinguished and may even lead to identification of the primary site of carcinoma. This may be of considerable therapeutic relevance. It may however be impossible to classify undifferentiated tumors on the basis of morphology alone. In these cases a diagnosis may be established by immunocytochemical typing. The most commonly employed markers and their applications are discussed.

Antibodies, Monoclonal↗
PubMed1986

Monoclonal antibodies to human cytokeratins: application to various epithelial and mesothelial cells.

Immunohistological analysis of human tissue using monoclonal antibodies against cytokeratins, which are confined to cells of epithelial origin, is a valuable technique. Using human epidermal keratins as antigen, we prepared monoclonal antibodies against cytokeratins (ZK1, ZK7, ZK61 and ZK99) and against a desmosomal protein (ZK31). Immunohistochemical staining of human skin sections using these antibodies showed a specific reaction with the epidermis: ZK1 stained the entire epidermis, ZK7 only the basal layer, ZK61 and ZK99 the suprabasal layers, and ZK31 the cellular interfaces. In order to test for antibody specificity, immunoblots with human epidermal and amnion epithelial cytokeratin polypeptides, as well as immunofluorescence microscopy of simple epithelia (glandular and simple columnar epithelia) were performed. ZK1, ZK61 and ZK99 reacted preferentially with cytokeratin polypeptides of stratified squamous epithelia and ZK7 recognized cytokeratins of stratified and simple epithelia. When the ZK antibodies were tested on mesothelial cells in pleural effusions, only ZK7 reacted with these cells. Biochemical analysis of cytokeratin accumulation in cells of primary and long-term cultures indicated that the cytokeratin pattern of mesothelial cells was quite unstable, while that of amnion epithelial cells showed only minor quantitative changes. The use of these antibodies to determine the epithelial origin of cells present in pleural effusions is proposed.

Amnion↗
PubMed1985

Establishment and characterization of an Epstein-Barr virus nuclear antigen-negative hairy cell line.

Continuous cell lines have been established from spleen cells of patients with confirmed hairy cell leukemia (HCL). One cell line, HCL-Z1, lacks Epstein-Barr virus nuclear antigen (EBNA), grows attached to the substratum and retains typical features of hairy cells as revealed by transmission and scanning electron microscopy. HCL-Z1 differs morphologically from the three other EBNA-positive lymphoblastoid cell lines obtained (HCL-Z2, HCL-Z3, HCL-Z4) as well as from normal spleen cells or lymphocytes. The three lymphoblastoid cell lines derived from HCL patients show similar surface features as a line from a myeloma patient. Therefore, not all cell lines derived from HCL patients may be considered as representative of the patients leukemia cells.

Antigens, Viral↗
PubMed1984

Monoclonal antibodies to human type IV collagen: useful reagents to demonstrate the heterotrimeric nature of the molecule.

Monoclonal antibodies (mAbs) have been prepared against type IV collagen isolated from human kidney. Two mAbs, designated CIV 22 and CIV 16, were extensively characterized. CIV 22 reacted only with native type IV collagen, whereas CIV 16 also bound to fragments derived from the alpha 1(IV) chain after reduction and alkylation of the molecule. Therefore, CIV 22 recognizes a conformational epitope on the triple helical type IV collagen, whereas CIV 16 binds to a sequential determinant in the carboxyl-terminal half of the alpha 1(IV) chain. By immunofluorescence, typical basement membrane structures were stained with both mAbs on frozen sections of different human organs. The mAbs were used to investigate the chain composition of type IV collagen. Radiolabeled type IV collagen bound to CIV 22, proving its triple helical configuration. These native probes, containing both the alpha 1(IV) and the alpha 2(IV) chains, also bound to CIV 16. Since CIV 16 does not react with the isolated alpha 2(IV) chain, both chains must be arranged in a single triple helical molecule (heterotrimer).

Antibodies, Monoclonal↗
PubMed1984

The localization and secretion of type IV collagen in synovial capillaries by immunohistochemistry using a monoclonal antibody against human type IV collagen.

The localization and the secretion of type IV collagen in synovial capillaries have been investigated by detecting the antigenic determinant of the major triple helix of human type IV collagen. Type IV collagen was indicated to be localized mainly in the lamina densa of basement membranes (BM) and to be secreted by both endothelial cells and pericytes. The pericytes secreted this collagen to both surfaces facing endothelial cells and the interstitial connective tissue. On the contrary, the direction of type IV collagen secretion by the endothelial cells was strictly confined to one side, namely towards the surface facing the BM. The absence of the antigenic determinant in rough endoplasmic reticulum and Golgi apparatus of the endothelial cells and pericytes indicated that the major triple helix of type IV collagen is mainly formed in the secretory vesicles after budding from the Golgi apparatus.

Adult↗
PubMed1984

Electron and immunoelectron microscopic investigation of basal lamina thickening in synovial capillaries and post-capillary venules in rheumatoid arthritis.

Capillaries and post-capillary venules in the synovium obtained from 12 rheumatoid arthritis (RA) patients have been investigated by electron microscopy and immunoelectron microscopy with a monoclonal antibody against human type IV collagen, which is one of the major basal lamina (BL) components. The level of BL thickening in RA synovial vessels is roughly parallel with that of cellular exudation. The BL thickening may be due to excessive production of BL components, in which the accelerated rate of death and replenishment of endothelial cells and pericytes plays an important role. These cells may not only produce a single layer of BL in their life-time but also produce excessive amounts of BL components to make several layers in their life-time.

Adult↗
PubMed1983

The thickening of basement membrane in synovial capillaries in rheumatoid arthritis.

Synovial tissues from seven rheumatoid arthritis (RA) patients were used for the ultrastructural investigation of capillary cellular components and basement membranes (BM). Attention has been specially paid to the mechanism of BM thickening of the capillaries in the inflammatory sites. The capillary BM were multilamellated in the inflammatory sites. The multilamellation was characteristic not only in the BM surrounding the endothelial cells and pericytes but also in the BM between these two types of cells. Cell debris was frequently encountered between the multilamellated BM. The hyperplasia and various stages of degeneration of the endothelial cells were observed in these regions. Some endothelial cells were activated and occasionally located in capillaries containing degenerated endothelial cells. The high incidence of these findings indicates the following hypotheses. The accelerated rate of death and replenishment of capillary cellular components may play a role in BM thickening in the inflammatory sites of RA synovium. These cells may not only produce one layer of BM in their life-time but may also be activated to produce excessive amounts of BM components to make several layers.

Adult↗
PubMed1982

Basement membrane (type IV) collagen is a heteropolymer.

Type IV collagen was isolated in high yield from bovine kidney cortex. The protein revealed Mr = 380,000 and contained, in a 2:1 ratio, two different disulfide-linked polypeptide chains, C-1 and D-1 (Mr = 125,000). Carboxymethyl-cellulose chromatography before and after reduction proved that the two polypeptide chains are arranged in a single triple helical molecule with the chain composition (C-1)2(D-1). The disulfide bridges appear to be located 180 amino acid residues from the NH2 terminus of the chains.

Amino Acids↗
PubMed1980

Type IV collagen is a heteropolymer with the formula C2D.

Native type IV collagen was purified from bovine kidney cortex homogenate by a method involving pepsin-solubilization and heat gelation. The near homogenous protein has a molecular weight of approximately 380K and the chain composition C2D. The subunits are linked by disulfide bridges.

Animals↗