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PubMed1983

Antibodies to intermediate filament proteins in the immunohistochemical identification of human tumours: an overview.

Intermediate-sized filament proteins (IFP) are tissue specific in that antibodies to keratin, vimentin, desmin, glial fibrillary acidic protein (GFAP) and the neurofilament proteins can distinguish between cells of epithelial and mesenchymal origin as well as of myogenic and neural origin respectively. Malignant cells retain their tissue-specific IFP, which makes it possible to use these antibodies in tumour diagnosis. Carcinomas are exclusively detected by antibodies to keratin. Monoclonal antibodies to keratin have allowed the differentiation between subgroups of epithelial tumours until now between adenocarcinomas and squamous cell carcinomas. Lymphomas, melanomas and several soft tissue tumours are distinctly recognized by antibodies to vimentin. On the other hand, rhabdomyosarcomas and leiomyosarcomas are positive for desmin, while astrocytomas give a strong reaction with GFAP antibodies. Thus, antibodies to IFP are useful tools for differential diagnosis in surgical pathology.

Antibodies↗
PubMed1980

Nucleus-associated intermediate filaments from chicken erythrocytes.

Chicken erythrocyte nuclei prepared by isolation in isotonic KCl and Nonidet P-40 detergent were found to contain numerous attached filaments with a mean diameter of 11.0 nm. In polypeptide content and solubility properties, they resembled the vimentin type of intermediate filament found in cells of mesenchymal origin. Examination of their association with the nucleus suggests that more than a simple membrane attachment is involved.

Animals↗
PubMed1991

A mathematical model for protein-induced lipid vesicle leakage: interaction of the intermediate filament protein vimentin and its isolated N-terminus with phosphatidylinositol vesicles.

A mathematical model was developed to analyze the leakage of phosphatidylinositol small unilamellar vesicles induced by the intermediate filament protein vimentin and its isolated N-terminal polypeptide. This model describes the kinetic and steady-state characteristics of this vesicle leakage as a direct action of protein on the lipid bilayer. Moreover, qualitative information at the molecular level can be deduced about protein-protein or protein-lipid interactions from the derived initial rate of vesicle leakage and the value of vesicle leakage at steady-state condition as a function of the protein concentration. Additionally, quantitative data on the inhibitory effect of various substances (here Ca2+ or Mg2+) can also be derived. This approach offers a possibility to compare interactions occurring within different protein-lipid systems by determining the characteristic parameters for the respective kinetic and steady-state conditions.

Lipid Bilayers↗
PubMed1984

Distinctive immunofluorescent labeling of epithelial and mesenchymal elements of carcinosarcoma with antibodies specific for different intermediate filaments.

A carcinosarcoma of the lung, as well as the paratracheal lymph nodes from the same patient, were subjected to immunofluorescent labeling with antibodies to tissue-specific intermediate-filament subunits, including desmin, vimentin, and prekeratin. Within the tumor mass two distinct populations of malignant cells were found: prekeratin-positive cells, corresponding to the carcinomatous component of the tumor, and vimentin-positive cells, corresponding to the sarcomatous elements. Tumor cells were also detected in lymph node metastases in which only the prekeratin-containing carcinoma cells were found. In view of the strict specificity of antivimentin and anti-prekeratin for cells of mesenchymal or epithelial origin, respectively, it is proposed that the two components of the carcinosarcoma are derived from distinct cell types and are not morphologic variants of the same tumor.

Carcinosarcoma↗
PubMed2002

Mechanics of vimentin intermediate filaments.

It is increasingly evident that the cytoskeleton of living cells plays important roles in mechanical and biological functions of the cells. Here we focus on the contribution of intermediate filaments (IFs) to the mechanical behaviors of living cells. Vimentin, a major structural component of IFs in many cell types, is shown to play an important role in vital mechanical and biological functions such as cell contractility, migration, stiffness, stiffening, and proliferation.

Animals↗
PubMed1984

Localization of the centriole and keratin intermediate filaments in PtK1 cells by double immunofluorescence.

We present observations on the relative location of the centriole and keratin filament cap in motile PtK1 cells. Subconfluent cells were double labeled with anticentriole and antikeratin sera. These preparations revealed that the centriole is separate from, but neighboring, the keratin filament cap. Serial ultrathin sections confirm this observation. These observations are consistent with the idea that the microtubule organizing center and intermediate filament distribution center are not identical or concentric in PtK1 cells.

Centrioles↗
PubMed1999

Smoothelin and intermediate filament proteins in human aortocoronary saphenous vein by-pass grafts.

The aim of this immunohistochemical investigation was to study the distribution of the novel cytoskeletal protein smoothelin and the intermediate filament proteins vimentin and desmin in normal human great saphenous vein and in human aortocoronary by-pass vein grafts. Smoothelin was present in most smooth muscle cells in the media of the native vein. In the neointima of the vein grafts that had been in situ for three months or more, smoothelin was, in general, present only in few smooth muscle cells. Desmin was distributed in the same pattern as smoothelin in the native great saphenous vein. When desmin and smoothelin were present in the neointima, smoothelin was detected in more cells than desmin. Vimentin was present in most cells in all wall layers of both the native saphenous vein and the vein grafts. Vascular smooth muscle cells containing vimentin but not desmin or smoothelin are the principal cells in the neointima of human aortocoronary vein grafts. In some grafts, however, all three cytoskeletal proteins were detected in the neointima. The distribution of smoothelin and desmin in aortocoronary vein grafts support the postulate that these proteins are expressed mainly in the contractile smooth muscle cell phenotype.

Aged↗
PubMed1989

Subcellular localization of an intermediate filament protein and its mRNA in glial cells.

Eucaryotic mRNAs are generally localized in the cell body, where most protein synthesis occurs. We have found that mRNAs encoding the glial intermediate filament protein are spatially distributed in the glial cell cytoplasm close to the location of the glial filaments. Whereas the glial filament protein mRNA was located predominantly in the distal process, actin mRNA was found almost exclusively in the apical portion of the glial cell. This pattern of mRNA localization might provide a mechanism for synthesis of proteins in specific subcellular compartments by mRNA translation locally.

Actins↗
PubMed1984

Oocytes and early embryos of Xenopus laevis contain intermediate filaments which react with anti-mammalian vimentin antibodies.

Previous studies have shown that Xenopus oocytes possess a cortical shell, which includes actin-containing microfilaments and cytokeratin-containing intermediate filaments. In this paper we show that oocytes of Xenopus laevis also contain filaments throughout their cytoplasm which are stained by several anti-vimentin antibody preparations. We also show that dramatic changes in pattern of these filaments occur during oocyte differentiation, first during vitellogenesis, and then during maturation of the oocyte to form an egg.

Animals↗
PubMed1983

Type I and type II keratins have evolved from lower eukaryotes to form the epidermal intermediate filaments in mammalian skin.

We have traced the evolutionary origins of keratin-like sequences to the genomes of lower eukaryotes. The proteins encoded by these genes have evolved to form the intermediate filaments that comprise the backbone of vertebrate skin cells. Two related but distinct types of keratins encoded by two separate multigene subfamilies are expressed in the epidermal keratinocytes of vertebrate species from fish to human. Both at the level of protein and at the level of DNA, these two classes of keratins are coordinately conserved throughout vertebrate evolution, indicating the central role that both types of keratins must play in the assembly and structure of the 8-nm filament.

Animals↗