Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Four embryonal rhabdomyosarcomas, one tumor diagnosed as an undifferentiated sarcoma, probably a rhabdomyosarcoma, and six different non-muscular sarcomas were investigated with antibodies specific for different intermediate filament types. The tumor cells in the rhabdomyosarcomas and the undifferentiated tumor were stained clearly by antibodies to desmin, the intermediate filament type characteristic of muscle. The staining of tumor cell by antibodies to vimentin, the intermediate filament type characteristic of certain cell types of mesenchymal origin including myoblasts, was different in these 5 cases. In one case of embryonal rhabdomyosarcoma nearly all tumor cells were stained, but in the remaining cases few or no tumor cells were positive with the vimentin antibody. In these rhabdomyosarcomas not only the large rhabdomyoblasts, but also the small undifferentiated cells were labeled by antibodies to desmin. In the latter cell type the desmin filaments were arranged typically in coils. In contrast, tumor cells in the non-muscular mesenchymal sarcomas were stained only by antibodies to vimentin but not by antibodies to desmin or prekeratin. The retention of the desmin marker characteristic of normal muscle in cases of rhabdomyosarcoma not only allowed the undifferentiated desmin-positive sarcoma to be classified as rhabdomyosarcoma but also suggests that the use of antibodies to desmin could be very helpful in the future for the diagnosis of undifferentiated rhabdomyosarcomas.
Virchows Arch B Cell Pathol Incl Mol Pathol 1982
PMID:Diagnosis of human childhood rhabdomyosarcoma of antibodies to desmin, the structural protein of muscle specific intermediate filaments. 617 91

Four cases of classical biphasic synovial sarcoma were studied for intermediate filaments of keratin and vimentin type. Epithelial-like cells lining gland-like slits were strongly positive for keratin but negative for vimentin, whereas the spindle cell stroma was negative for keratin but positive for vimentin. The observations indicate epithelial differentiation in the glandular elements of biphasic synovial sarcomas, and are consistent with earlier ultrastructural observations suggesting epithelial properties of these cells.
Virchows Arch B Cell Pathol Incl Mol Pathol 1982 Aug
PMID:Keratin in the epithelial-like cells of classical biphasic synovial sarcoma. 618 81

Four adenomatoid tumors of the epididymis were evaluated immunohistologically for the expression of intermediate filaments and endothelial cell markers, factor VIII-related antigen and binding of Ulex europaeus I-lectin (UEA I). Immunofluorescence microscopy showed a strong reaction with antikeratin but not with anti-vimentin antibodies, indicating that adenomatoid tumor cells contain epithelial but not mesenchymal type of intermediate filaments. No staining of tumor cells was seen with anti-FVIII-related antigen antibodies or with fluorochrome-coupled UEA I. The results support the mesothelial, non-endothelial origin of adenomatoid tumors.
Virchows Arch B Cell Pathol Incl Mol Pathol 1983
PMID:Adenomatoid tumor: immunohistological features suggesting a mesothelial origin. 618 84

The expression of intermediate filament type was determined in 13 renal cell (Grawitz) tumors (10 primary renal tumors and 3 lymph node metastases). All of the tumors except one lymph node metastasis contained cells expressing vimentin intermediate filaments, generally a marker of mesodermally-derived tissues and their tumors, the sarcomas. In addition, the 10 primary renal tumors and two lymph node metastases contained cells expressing keratin proteins. Using a monoclonal antibody to keratins, specific for glandular epithelial cells, it has been shown that some of the tumor cells resemble adenocarcinomas, at least in this respect. Double immunofluorescence labeling demonstrated that some of the vimentin-containing cells contained keratin while others did not. Only occasional cells were found to contain keratin but not vimentin. However, one of the lymph node metastases was positive only for vimentin. Thus Grawitz tumor cells express intermediate filament types which are generally biological markers of both sarcomatous and carcinomatous tumors.
Virchows Arch B Cell Pathol Incl Mol Pathol 1983
PMID:Is renal cell (Grawitz) tumor a carcinosarcoma? Evidence from analysis of intermediate filament types. 619 7

Monophasic synovial sarcomas of spindle-cell type and fibrosarcomas were studied by electron and immunofluorescence microscopy for their intermediate filament expression and the binding of peanut agglutinin (PNA). In monophasic synovial sarcomas of spindle-cell type (two cases), frequent cell-to-cell junctions, irregular cytoplasmic processes, and occasional cytoplasmic, tonofilament-like bundles of intermediate filaments were seen by electron microscopy. These features were absent from fibrosarcomas. Immunohistologically, the monophasic synovial sarcomas showed arrays of prekeratin-positive cells in the midst of the vimentin-positive spindle cells. By double fluorescence microscopy, the prekeratin-positive cells also bound PNA, like the epithelial-like cells of the classical biphasic synovial sarcoma. In contrast to monophasic synovial sarcomas, prekeratin-positive cells and arrays of PNA-binding cells, were not seen by immunofluorescence microscopy in fibrosarcomas (seven cases). Thus the prekeratin-content, the binding of PNA lectin, and certain ultrastructural features suggesting early epithelial differentiation, help to distinguish monophasic synovial sarcomas of spindle-cell type from other spindle cell sarcomas.
Virchows Arch B Cell Pathol Incl Mol Pathol 1983
PMID:Monophasic synovial sarcoma of spindle-cell type. Epithelial differentiation as revealed by ultrastructural features, content of prekeratin and binding of peanut agglutinin. 619 6

The various epithelial cells of the lower respiratory tract and the carcinomas derived from them differ markedly in their differentiation characteristics. Using immunofluorescence microscopy and two-dimensional gel electrophoresis of cytoskeletal proteins from microdissected tissues we have considered whether cytokeratin polypeptides can serve as markers of cell differentiation in epithelia from various parts of the human and bovine lower respiratory tract. In addition , we have compared these protein patterns with those found in the two commonest types of human lung carcinoma and in several cultured lung carcinoma cell lines. By immunofluorescence microscopy, broad spectrum antibodies to cytokeratins stain all epithelial cells of the respiratory tract, including basal, ciliated, goblet, and alveolar cells as well as all tumor cells of adenocarcinomas and squamous cell carcinomas. However, in contrast, selective cytokeratin antibodies reveal cell type-related differences. Basal cells of the bronchial epithelium react with antibodies raised against a specific epidermal keratin polypeptide but not with antibodies derived from cytokeratins characteristic of simple epithelia. When examined by two-dimensional gel electrophoresis, the alveolar cells of human lung show cytokeratin polypeptides typical of simple epithelia (nos. 7, 8, 18 and 19) whereas the bronchial epithelium expresses, in addition, basic cytokeratins (no. 5, small amounts of no. 6) as well as the acidic polypeptides nos. 15 and 17. Bovine alveolar cells also differ from cells of the tracheal epithelium by the absence of a basic cytokeratin polypeptide. All adenocarcinomas of the lung reveal a "simple-epithelium-type" cytokeratin pattern (nos. 7, 8, 18 and 19). In contrast, squamous cell carcinomas of the lung contain an unusual complexity of cytokeratins. We have consistently found polypeptides nos. 5, 6, 8, 13, 17, 18 and 19 and, in some cases, variable amounts of cytokeratins nos. 4, 14 and 15. Several established cell lines derived from human lung carcinomas (SK-LU-1, Calu -1, SK-MES-1 and A-549) show a uniform pattern of cytokeratin polypeptides (nos. 7, 8, 18 and 19), similar to that found in adenocarcinomas. In addition, vimentin filaments are produced in all the cell lines examined, except for SK-LU-1.(ABSTRACT TRUNCATED AT 400 WORDS)
Virchows Arch B Cell Pathol Incl Mol Pathol 1984
PMID:Cytokeratins in normal lung and lung carcinomas. I. Adenocarcinomas, squamous cell carcinomas and cultured cell lines. 620 12

Cytoskeletal residues obtained after extraction of rat liver and cultured rat hepatoma cells (line MH1C1) were used to isolate cytokeratin subunit complexes by solubilization in low salt buffer containing 4 M-urea. Alternatively, the complexes were prepared by solubilization of total cytoskeletal proteins in 9.5 M-urea or 6 M-guanidinium hydrochloride (Gu . HCl), followed by separation using reversed phase high pressure liquid chromatography and dialysis first against either 9.5 M-urea or 6 M-Gu . HCl and then against buffers containing either 4 M-urea or 2 M-Gu . HCl, respectively. The complexes contained only two cytokeratin polypeptides in a 1 : 1 ratio as demonstrated by electrophoresis and isoelectric focusing, i.e. components A (Mr 55,000; isoelectric point in 9.5 M-urea, pH 6.4) and D (Mr 49,000; isoelectric point, pH 5.38) which were separated from each other at urea concentrations higher than 7 M. The complex had a sedimentation coefficient S25,w of 4.96 S in 2 M-Gu . HCl. Sedimentation equilibrium analysis gave an average Mr value of 207,000 which was interpreted as a tetramer containing two chains each of A and D. This complex was also directly demonstrated by gel electrophoresis under non-dissociating conditions. Using dimethyl suberimidate to cross-link the complex in solution of 4 M-urea or 2 M-Gu . HCl, we identified covalently linked heterodimers of A and D, and a tetrameric unit containing equal amounts of A and D which was the largest cross-link product obtained. This complex was similar to the tetrameric complex of rat and human vimentin formed under the same conditions. The constituents of the cross-linked products were identified by two-dimensional ("diagonal") gel electrophoresis, involving the cleavage of the bis(amidine) cross-links after the initial separation in the first dimension. Identical cross-link products were recognized when cytokeratin filaments were used. By electron microscopy the complexes appeared as threads of 2 to 3 nm diameter with a mean length of approximately 48 nm. On dialysis to low salt buffer, the complexes formed 2 to 3 nm protofilaments, intertwisted 3 to 4 nm protofilaments and typical 7 to 11 nm intermediate-sized filaments. Complexes formed from equivalent cytokeratins of other species such as man and cow, as well as heterologous recombinations such as human component A mixed with bovine component D and vice versa, showed the same characteristics.(ABSTRACT TRUNCATED AT 400 WORDS)
J Mol Biol 1984 Sep 15
PMID:Heterotypic tetramer (A2D2) complexes of non-epidermal keratins isolated from cytoskeletons of rat hepatocytes and hepatoma cells. 620 69

The intermediate filament proteins desmin and vimentin and the muscle tropomyosins were the major protein phosphate acceptors in 8-day-old myotubes incubated for 4 h in medium containing radiolabeled phosphate. The addition of isoproterenol or 8-bromo-cyclic AMP (BrcAMP) resulted in a two- to threefold increase in incorporation of 32PO4 into both desmin and vimentin, whereas no changes in the incorporation of 32PO4 into tropomyosin or other cellular proteins were observed. The BrcAMP- or hormonally induced increase in 32PO4 incorporation into desmin and vimentin was independent of protein synthesis and was not caused by stimulation of protein phosphate turnover. In addition, BrcAMP did not induce significant changes in the specific activity of the cellular ATP pool. These data suggest that the observed increase in 32PO4 incorporation represented an actual increase in phosphorylation of the intermediate filament proteins desmin and vimentin. Two-dimensional tryptic analysis of desmin from 8-day-old myotubes revealed five phosphopeptides of which two showed a 7- to 10-fold increase in 32PO4 incorporation in BrcAMP-treated myotubes. Four of the phosphopeptides identified in desmin labeled in vivo were also observed in desmin phosphorylated in vitro by bovine heart cAMP-dependent protein kinase. Although phosphorylation of desmin and vimentin was apparent in myogenic cells at all stages of differentiation, BrcAMP- and isoproterenol-induced increases in phosphorylation of these proteins were restricted to mature myotubes. These data strongly suggest that in vivo phosphorylation of the intermediate filament proteins desmin and vimentin is catalyzed by the cAMP-dependent protein kinases and that such phosphorylation may be regulated during muscle differentiation.
Mol Cell Biol 1982 Sep
PMID:Cyclic AMP-modulated phosphorylation of intermediate filament proteins in cultured avian myogenic cells. 629 4

The degradation of vimentin and desmin by the Ca2+-activated proteinase specific for these intermediate filament proteins proceeds in two stages in the form of a limited proteolysis. At first, the reaction is very rapid, with the stepwise and complete removal of a peptide (ca. 9,000 daltons) from the N-terminal of vimentin and desmin. This results in the production of a characteristic "staircase" of degradation products, as seen in two-dimensional polyacrylamide gel electrophoresis. The second stage of proteolysis is characterized by the accumulation of peptides which are resistant to further proteolysis; this is due not to product inhibition but to the fact that these peptides are not substrates for the proteinase and therefore do not protect the latter from inactivation (autodigestion). In vitro phosphorylation of the substrates does not affect proteinase activity, probably because the phosphorylation site is located towards the C-terminal of the molecules. The specific and limited proteolysis of vimentin and desmin results in the deletion of the nucleic acid binding and filament assembly site of these proteins, indicating that the Ca2+-activated proteinase plays a role in regulating the function(s) of these intermediate filament proteins, rather than their simple turnover during the cell cycle.
Mol Cell Biol 1983 Jun
PMID:Proteolysis of vimentin and desmin by the Ca2+-activated proteinase specific for these intermediate filament proteins. 630 28

Synemin, a 230-kilodalton polypeptide component of avian muscle and erythrocyte intermediate filaments, is also found in association with the vimentin filaments of lens tissue. In chicken lens cells, synemin is bound to the core vimentin polymer with the same 180-nm periodicity that it exhibits in erythrocytes. Its solubility properties are characteristic of those of intermediate filaments in general and similar to those of synemin in muscle cells and erythrocytes. Synemin appears at an early stage of lens development and undergoes a dramatic accumulation as the epithelial cells elongate and differentiate into fiber cells. In contrast to synemin in cultured skeletal muscle, lens synemin is not confined to postmitotic, terminally differentiating cells but is present in proliferative cells as well. It is lost from the fibers near the center of the lens, as are many other cellular structures including intermediate filaments. These findings provide new information about the occurrence and expression of avian synemin and new insight regarding its presumptive role as a modulator of intermediate-filament function.
Mol Cell Biol 1984 Oct
PMID:Expression of the intermediate-filament-associated protein synemin in chicken lens cells. 639 Jan 80


<< Previous 1 2 3 4 5 6 7 8 9 10 Next >>