High impact information on VIM

• Degradation of calpain substrates spectrin and vimentin was assessed by immunoblotting [1].
• Filament proteins from non-keratinous tissues, such as desmin, vimentin, neurofilament proteins and the glial fibrillary acidic protein, which form monocomponent filaments, constitute a third type [2].
• Transcripts decreased by pregnancy and P4 and/or IFNT include COL3A1, LUM, PTMA, PUM1, RPL9, SPARC, and VIM [3].
• Expression of GLT1 in subsets of vimentin-positive astrocytes persists in white matter but not in cortex [4].
• Rete cells in culture express cytokeratin and vimentin in the cytoskeleton, whereas Sertoli cells prepared from testes of adult rams contain vimentin but not cytokeratin [5].

Biological context of VIM

• Vimentin and collagen I gene expression from freshly isolated or cultured ICs was measured by reverse transcriptase-polymerase chain reaction [6].
• Cells obtained from all three tissue sources exhibited a myofibroblast phenotype in vitro, as demonstrated by their immunoreactivity with antibodies directed against vimentin, alpha-smooth muscle actin, fibronectin, and chondroitin sulfate [7].
• Major findings were upregulation of cytokeratin on damaged tubules, desmin and vimentin in undifferentiated mesenchyme, and smooth muscle actin in mesenchyme and on smooth muscle "collars" around dilated tubules [8].
• Incubation of myofibrils with m-calpain resulted in the hydrolysis of troponin-T, desmin, and a 58-kDa molecular weight protein, possibly vimentin, and 5 mM ZnCl2 completely blocked these changes [9].
• The topographical distribution of glial fibrillary acidic protein (GFAP), vimentin, neuron-specific enolase (NSE) and neurofilament (NF) proteins in the developing neocortex and cerebellum of sheep fetuses of different gestational ages (60-149 days) was described [10].

Anatomical context of VIM

• Myosin-staining cells had the typical spindle appearance of smooth muscle cells whereas the vimentin-positive cells could either be branched or more closely resemble the smooth muscle cells [11].
• The intermediate filament proteins nestin, vimentin, and glial fibrillary acidic protein was used as markers for astroglial maturation and astrogliosis, and myelin basic protein as a marker for oligodendrocytes and myelin formation [12].
• Antibodies to Kit and vimentin, which are widely used to label specialised pacemaking cells in the gastrointestinal tract (known as interstitial cells of Cajal), demonstrated the existence of an axially orientated subpopulation of cells lying between the endothelium and the bulk of the smooth muscle [11].
• In addition, some cases showed reexpression of vimentin and desmin on proximal tubular epithelial cells [8].
• The distribution pattern of actin, desmin, vimentin and tubulin in the ovine testis during postnatal development was investigated by means of immunohistochemical methods [13].

Associations of VIM with chemical compounds

• Expression of phosphotungstic acid hematoxylin, glial fibrillary acidic protein and vimentin indicates that the second cell population in the developing ovine pineal gland is, in fact, a combination of glial-astrocyte cells at varying stages of maturity [14].

Other interactions of VIM

• GLT1 protein expression within astrocytes is developmentally regulated, appearing first in vimentin positive radial glia at 60 and 71 days and then switching to GFAP positive parenchymal and perivascular astrocytes at 136 days [4].
• The neoplastic cells were positive for neuron-specific enolase, synaptophysin and vimentin [15].

Analytical, diagnostic and therapeutic context of VIM

• Immunocytochemical stainings of vimentin, alpha-smooth muscle actin (ASMA), smooth muscle myosin, and procollagen I were performed on aortic VICs [6].
• All embryos were processed for examination by light and transmission electron microscopy or immunohistochemical labelling for alpha-1-fetoprotein and vimentin [16].
• Vimentin and S-100 protein expression was studied in the kidneys of adult sheep and goat using immunohistochemistry [17].

References