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R Moll

Publications and source records attributed to R Moll.

At least 235 records · Page 13Linked to original sources
PubMed1983

Cytokeratins of normal epithelia and some neoplasms of the female genital tract.

Cytokeratins are a family of polypeptides of intermediate filaments which in diverse epithelia are expressed in different, yet specific, combinations. We have studied the cytokeratins present in normal epithelia of the female genital tract, in comparison with those present in genital tract carcinomas, by two-dimensional gel electrophoresis of cytoskeletal proteins from microdissected tissues and by immunofluorescence microscopy. Cells of ovarian mesothelium, oviduct, endometrium, and endocervix contain cytokeratin polypeptides nos. 7, 8, 18, and 19. By contrast, tonofilaments of the stratified squamous epithelia of vagina and exocervix contain cytokeratins 4, 5, 6, 13, 14, 15, 16, and 19. Exocervical regions distant from the endo-exocervical junction as well as vagina contain, in addition, the large (Mr 68,000) and basic cytokeratin component no. 1, previously described in epidermis. Endocervical squamous metaplasia at the endo-exocervical border displays a complex cytokeratin pattern, probably due to cell-type heterogeneity. Similar cytokeratin patterns are also observed in genital tract epithelia of the cow and mouse. In human carcinomas of the female genital tract, two main types of cytokeratin patterns can be distinguished. Ovarian carcinomas and endometrial adenocarcinomas express cytokeratins 7, 8, 18, and 19 and, thus, maintain the pattern of the cells of their origin. In endocervical adenocarcinomas the additional presence of component no. 17 has been noted. Nonkeratinizing squamous cell carcinomas of the cervix show a very complex pattern (cytokeratins 5, 6, 7, 8, 13, 14, 15, 17, 18, and 19). Keratinizing squamous cell carcinomas of the cervix display lower complexity and lack cytokeratins 7, 8, and 18. When frozen sections are examined by immunofluorescence microscopy, all epithelia of the genital tract are stained with the monoclonal cytokeratin antibody KG 8.13. Simple epithelia but not the stratified epithelia of vagina and exocervix also react with monoclonal antibodies specific for cytokeratins 8 or 18. The value of cytokeratin polypeptide patterns in distinguishing diverse epithelial cell types of the female genital tract, in elucidating the histogenesis of neoplasms, and in providing a new tool for the differential diagnosis of tumors is discussed.

Adenocarcinoma↗
PubMed1982

Detection of a cytokeratin determinant common to diverse epithelial cells by a broadly cross-reacting monoclonal antibody.

A monoclonal antibody derived from a mouse immunized with bovine epidermal prekeratin has been characterized by its binding to cytoskeletal polypeptides separated by one- or two-dimensional gel electrophoresis and by immunofluorescence microscopy. This antibody (KG 8.13) binds to a determinant present in a large number of human cytokeratin polypeptides, notably some polypeptides (Nos. 1, 5, 6, 7, and 8) of the 'basic cytokeratin subfamily' defined by peptide mapping, as well as a few acidic cytokeratins such as the epidermis-specific cytokeratins Nos. 10 and 11 and the more widespread cytokeratin No. 18. This antibody reacts specifically with a wide variety of epithelial tissues and cultured epithelial cells, in agreement with previous findings that at least one polypeptide of the basic cytokeratin subfamily is present in all normal and neoplastic epithelial cells so far examined. The antibody also reacts with corresponding cytokeratin polypeptides in a broad range of species including man, cow, chick, and amphibia but shows only limited reactivity with only a few rodent cytokeratins. The value of this broad-range monoclonal antibody, which apparently recognizes a stable cytokeratin determinant ubiquitous in human epithelia, for the immunohistochemical identification of epithelia and carcinomas is discussed.

Animals↗
PubMed1982

Intermediate filaments and their interaction with membranes. The desmosome-cytokeratin filament complex and epithelial differentiation.

Intermediate-sized filaments represent a class of morphologically similar but biochemically and immunologically distinguishable cytoplasmic protein polymer structures. Five major filament types have been identified (cytokeratin, vimentin, desmin, neurofilament protein, glia filament protein) and antibodies to these proteins have been used for distinguishing different cell types and tumors derived therefrom. Epithelial and carcinoma cells are characterized by the presence of cytokeratin filaments and desmosomal elements identified by antibodies to certain high molecular weight proteins of desmosomal plaques. However, the specific pattern of cytokeratin polypeptides is different in different epithelia. The potential value of cell type identification by immunological reactions with antibodies to cytoskeletal proteins in tumor diagnosis is discussed.

Animals↗
PubMed1982

Immunological localization of a major karyoskeletal protein in nucleoli of oocytes and somatic cells of Xenopus laevis.

Oocyte nuclei of Xenopus laevis contain two major karyoskeletal proteins characterized by their resistance to extractions in high salt buffers and the detergent Triton X-100, i.e. a polypeptide of 68,000 mol wt which is located in the core complex-lamina structure and a polypeptide of 145,000 mol wt enriched in nucleolar fractions. Both proteins are also different by tryptic peptide maps and immunological determinants. Mouse antibodies were raised against insoluble karyoskeletal proteins from Xenopus oocytes and analyzed by immunoblotting procedures. Affinity purified antibodies were prepared using antigens bound to nitrocellulose paper. In immunofluorescence microscopy of Xenopus oocytes purified antibodies against the polypeptide of 145,000 mol wt showed strong staining of nucleoli, with higher concentration in the nucleolar cortex, and of smaller nucleoplasmic bodies. In various other cells including hepatocytes, Sertoli cells, spermatogonia, and cultured kidney epithelial cells antibody staining was localized in small subnucleolar granules. The results support the conclusion that this "insoluble" protein is a major nucleus-specific protein which is specifically associated with--and characteristic of--nucleoli and certain nucleolus-related nuclear bodies. It represents the first case of a positive localization of a karyoskeletal protein in the nuclear interior, i.e. away from the pore complex-lamina structure of the nuclear cortex.

Animals↗
PubMed1982

Different keratin polypeptides in epidermis and other epithelia of human skin: a specific cytokeratin of molecular weight 46,000 in epithelia of the pilosebaceous tract and basal cell epitheliomas.

Cytokeratin polypeptides of human epidermis, of epithelia microdissected from various zones of the pilosebaceous tract (outer root-sheath of hair follicle, sebaceous gland), and of eccrine sweat-glands have been separated by one- and two-dimensional gel electrophoresis and characterized by binding of cytokeratin antibodies and by peptide mapping. The epithelium of the pilosebaceous tract has three major keratin polypeptides in common with interfollicular epidermis (two basic components of mol wts 58,000 and 56,000 and one acidic polypeptide of mol wt 50,000); however, it lacks basic keratin polypeptides in the mol wt range of 64,000-68,000 and two acidic keratin-polypeptides of mol wts 56,000 and 56,500 and contains an additional characteristic acidic cytokeratin of mol wt 46,000. Another cytokeratin polypeptide of mol wt 48,000 that is prominent in hair-follicle epithelium is also found in nonfollicular epidermis of foot sole. Both epidermis and pilosebaceous tract are different from eccrine sweat-gland epithelium, which also contains two major cytokeratins of mol wts 52,500 and 54,000 (isoelectric at pH 5.8-6.1) and a more acidic cytokeratin of mol wt 40,000. A striking similarity between the cytokeratins of human basal-cell epitheliomas and those of the pilosebaceous tract has been found: all three major cytokeratins (mol wts 58,000; 50,000; 46,000) of the tumor cells are also expressed in hair-follicle epithelium. The cytokeratin of mol wt 46,000, which is the most prominent acidic cytokeratin in this tumor, is related, by immunological and peptide map criteria, to the acidic keratin-polypeptides of mol wts 48,000 and 50,000, but represents a distinct keratin that is also found in other human tumor cells such as in solid adamantinomas and in cultured HeLa cells. The results show that the various epithelia present in skin, albeit in physical and ontogenic continuity, can be distinguished by their specific cytokeratin-polypeptide patterns and that the cytoskeleton of basal-cell epitheliomas is related to that of cells of the pilosebaceous tract.

Basal Cell Carcinoma↗
PubMed1982

An unusual type of cytokeratin filament in cells of a human cloacogenic carcinoma derived from the anorectal transition zone.

Epithelia-derived tumors (carcinomas) can be distinguished from mesenchymally derived tumors by the presence of intermediate-sized filaments of the cytokeratin type, which usually coincides with the absence of other types of intermediate-sized filaments such as vimentin filaments. In the course of diagnostic examinations of human tumors, using immunofluorescence microscopy, we have come across a case of an unusual carcinoma (Primary tumor and lymph node metastasis) positively stained not only with cytokeratin antibodies but also with immunoglobulins present in vimentin antisera. Therefore, this tumor, a cloacogenic carcinoma apparently derived from the rectal-anal transitional region, has been examined in greater detail using both immunofluorescence microscopy and immuno-electron microscopy as well as gel electrophoretic analysis of cytoskeletal polypeptides from total tumor tissue and from microdissected nodules enriched in carcinoma cells. The unusual reaction of the carcinoma cells with immunoglobulins present in seven different (rabbit or guinea pig) antisera raised against vimentin, has been found to be diminished after absorption on purified cytokeratin or total epidermal cytoskeletal material, but not after absorption on purified vimentin. Gel electrophoretic analysis of tumor cytoskeletons showed an unusual complex pattern of cytokeratin polypeptides containing relatively large (Mr 68,000 and Mr 58,000) neutral-to-slightly basic cytokeratins, as are typically found in epidermis and other stratified squamous epithelia, as well as several smaller acidic cytokeratins, including a Mr 40,000 polypeptide found in certain nonstratified epithelial such as colon and small intestine. Total tumor also showed the inclusion of some vimentin which, however, was significantly decreased in analysis of excised carcinoma nodules. Examining antibody binding to polypeptides separated by gel electrophoresis and blotted on nitrocellulose paper, we have found that antisera raised against vimentin contained not only vimentin antibodies but also immunoglobulins which specifically bound to the largest cytokeratin component. We conclude that the unusual reaction of immunoglobulins present in vimentin antisera with cytokeratin filament bundles does not represent specific binding to vimentin in these carcinoma cells, but is due to a component obviously widespread in vimentin antisera which binds specifically to a cytokeratin present in this type of tumor but not in most other carcinomas. It is proposed that use is made in diagnostic examinations of vimentin antisera or affinity-purified vimentin antibodies that have been pre-absorbed on cytokeratin protein, in order to eliminate such disturbing reactions.

Aged↗
PubMed1982

Desmoplakins of epithelial and myocardial desmosomes are immunologically and biochemically related.

Guinea pig antibodies against desmoplakins from bovine muzzle epidermis showed specific reaction in several epithelial tissues with desmoplakin I (Mr 250,000) and desmoplakin II (Mr 215,000). By immunofluorescence microscopy, prominent punctate staining was observed in various lines of cultured epithelial cells, revealing desmosomal junctions at sites of established cell-to-cell contacts as well as hemidesmosomes and internalized desmosome-derived membrane domains. On frozen tissue sections punctate staining was observed along plasma membranes of epithelial cells, and electron microscopy using the immunoperoxidase technique revealed that the antibodies were specifically localized at the plaques associated with desmosomes and hemidesmosomes. Of a large number of non-epithelial cells examined positive staining was only observed on desmosome-like junctions of myocardial cells and Purkinje fiber cells. In both epithelial and myocardial tissues the antibodies showed a broad range of cross-reactivity between diverse vertebrate species such as man, cow, rodent, and chicken, indicating that desmoplakins contain determinants strongly conserved during evolution. When binding of these antibodies to cytoskeletal polypeptides separated by gel electrophoresis and blotted on nitrocellulose paper sheets was examined, specific reaction was noted with desmoplakin I and, to a variable degree, also desmoplakin II from various epithelial cells. Reaction was also observed with a myocardial polypeptide from bovine and human hearts which had a similar Mr value (250,000) and isoelectric pH range as desmoplakin I. We conclude that desmoplakins are the major proteins present in the desmosomal plaques of both epithelial and myocardial cells and that the desmoplakin polypeptides present in these two different cell types are very similar, if not identical.

Animals↗
PubMed1981

Antibodies to high molecular weight polypeptides of desmosomes: specific localization of a class of junctional proteins in cells and tissue.

Desmosome-enriched fractions were isolated from bovine muzzle epidermis either as desmosome-tonofilament complexes using a procedure involving treatment at pH9 or in the form of desmosomal residue fractions using a modification of the citric acid buffer (pH 2.3) method of Skerrow and Matoltsy [1]. Major polypeptides of high molecular weights (mol. wt.) were separated by gel electrophoresis, individual polypeptide bands were excised, and protein was eluted and used for immunization. Guinea pig antibodies raised against two prominent polypeptides of high mol. wt. (250,000 and 215,000) showed, on nitrocellulose paper blots of desmosome-tonofilament polypeptides separated by gel electrophoresis, extensive cross-reaction between a group or large polypeptides characteristic of desmosome-containing fractions, most notably polypeptides of 250 K, 215 K, 200 k, 175 K, and 164 K. These antibodies allowed, when used in immunofluorescence microscopy, the specific localization of desmosomal junctions (i) in sections through epithelia-containing tissue (e.g., epidermis, mucosae of tongue and esophagus, cornea, mammary gland, small intestine, liver, thymus, urothelium of bladder) and myocardium; (ii) on dissociated cells from these tissues; (iii) on various epithelial cells grown in culture; an (iv) in tumor-like proliferations of cultured epithelial cells injected into nude mice. Individual desmosomes could be visualized and resolved at the light microscopic level. No reaction was found in cells devoid of desmosomes and on other classes of intercellular junctions. Electron microscopic localization using immunoperoxidase techniques indicated that these proteins are located in, or close to, the desmosomal plague structure. It is proposed to use such antibodies against desmosomal proteins as markers specific to this so far only morphologically define class of junctions. Use of these markers will (i) improve identification and classification of intercellular junctions; (ii) facilitate determinations of the specific patterns of distributions of desmosomes and desmosomal protein in various cells and tissue; (iii) allow studies of formation and disintegration of desmosomes, and of the biosynthesis and possible recycling of their constituents; and (iv) provide tissue group-specific markers valuable in histology and diagnosis, especially for identification of epithelial and carcinoma cells.

Animals↗
PubMed1976

Synthesis of yeast histones in the cell cycle.

The yeast, Saccharomyces cerevisiae, contains four types of histones resembling histones H3, H2b, H2a, and H4 of animal cells. These proteins are synthesized primarily, if not exclusively, in the S-phase of the cell cycle. This result is discussed with reference to the insensitivity of ongoing DNA replication in yeast to inhibitors of protein synthesis.

Cell Division↗
PubMedDate not supplied

Pulmonary artery sarcoma mimicking chronic thromboembolic disease: computed tomography and magnetic resonance imaging findings.

PURPOSE: The diagnosis of the rare primary malignant tumors of the pulmonary arteries is often delayed as symptoms are nonspecific. METHODS: Computed tomography (CT) and magnetic resonance imaging (MRI) of three patients with occlusion of the right pulmonary artery, two with sarcoma and one with chronic thromboembolic disease were analyzed for discriminating diagnostic criteria. RESULTS: Criteria suggesting pulmonary artery sarcoma are inhomogeneous high or low attenuation (hemorrhage, necrosis), soft-tissue density in pulmonary arteries, vascular distension, enhancement after administration of gadopentetate dimeglumine. Criteria for chronic thromboembolic disease are homogeneous soft-tissue lesions, abrupt vascular narrowings and cut-offs, as well as regional parenchymal hyperdensities. CONCLUSION: CT and MRI provide complementary findings suggesting advanced pulmonary artery sarcoma instead of chronic thromboembolism.

Adult↗