Disease relevance of VIM

• Triple expression of GFAP, VIM and CK was found in the papillary meningioma (in patterns suggesting frequent co-localization), in the metastatic carcinoma (in patterns suggesting little co-localization), and in the pleomorphic adenoma (only few GFAP-positive cells) [1].
• VIM C6, an antibody recognizing cells of the granulocyte series, showed surface labeling of normal and reactive glial cells and of all types of glioma regardless of the grade of malignancy [2].
• VIM is also positive in glial processes of cerebellar pilocytic astrocytomas, in Schwann cells of neurinomas and in endothelial cells of all oncotypes [3].
• In medulloblastomas, VIM decorates reactive glia cells [3].
• In hemangioblastomas, besides intervascular and endothelial cells, groups of polygonal cells are intensely positive for both VIM and GFAP [3].

Psychiatry related information on VIM

• GFAP and vimentin increased with aging and in Alzheimer's disease (AD) [4].
• The purpose of this in vitro study was to calibrate occlusal restorative decision-making based on visual inspection (VI), and to compare it with visual inspection with magnifying (x1.25) lenses (VIM), and fibre-optic transillumination (VIF) [5].

High impact information on VIM

• As cells enter mitosis, the intermediate filament (IF) networks of interphase BHK-21 cells are depolymerized to form cytoplasmic aggregates of disassembled IFs, and the constituent IF proteins, vimentin and desmin are hyperphosphorylated at several specific sites [6].
• Intermediate filament reorganization during mitosis is mediated by p34cdc2 phosphorylation of vimentin [6].
• Therefore, vimentin is a substrate of p34cdc2 and phosphorylation of vimentin contributes to M phase reorganization of the IF network [6].
• Remarkably, the intervening sequences map at positions that fully correspond to those of the vimentin gene [7].
• They reacted with vimentin, the major polypeptide of the intermediate-filament cytoskeleton of mesenchymal cells [8].

Chemical compound and disease context of VIM

• An immunohistochemical study of 15 ovarian formalin-fixed, paraffin-embedded dysgerminomas showed positive staining of tumor cells for vimentin in all cases [9].
• We therefore undertook the present study to determine the relationships between glial and vimentin intermediate filaments (IFs), actin microfilaments, and CD44, a cell surface glycoprotein important in cell migration and invasion, in human astrocytoma cells [10].
• Our findings indicate that in the differential diagnosis of MGH versus MA, the presence of subnuclear vacuoles favors the former, whereas luminal squamous metaplasia, stromal foam cells, mitotic activity, vimentin expression, and MIB-1 expression favor the latter [11].
• Dibutyryl cyclic AMP induces vimentin and GFAP expression in cultured medulloblastoma cells [12].
• Acridine orange fluorochrome distinguished vimentin/desmin-reactive myofibres that were regenerating from those of developmental myopathies because the RNA fluorescence was strong in regenerating myofibres and in fetal myotubes, but was absent from myofibres in developmental disorders of muscle [13].

Biological context of VIM

• These findings are consistent with previous observations that phosphorylation of vimentin affects its intracellular localization and that vimentin is a substrate for protein kinase C (PKC) [14].
• Vimentin is a widely expressed intermediate filament protein thought to be involved mainly in structural processes, such as wound healing [14].
• Indirect immunofluorescence analysis of cultured cells transfected with a plasmid encoding an epitope-tagged ATDC protein localizes the protein to vimentin filaments [15].
• Vimentin was detected in ductal plate and biliary epithelial cells from 9 to 36 weeks' gestation, but not in hepatoblasts or hepatocytes [16].
• A complementary DNA clone 1.8 kilobases long included the entire protein-coding region for vimentin [17].

Anatomical context of VIM

• However, blastemal cells demonstrated coexpression of CYTO and VIM intermediate filaments when grown in a serum-free medium on a matrix material [18].
• However, nearly all cases of CHB showed stromal cell staining with VIM (19/22) [19].
• Co-expression of GFAP and VIM was seen in epiglottic chondrocytes and reactive astroglia; another metastatic carcinoma was labeled only for CKs [1].
• Furthermore, prominent anti-VIM immunoreactivity and anti-EMA cell membrane staining including ring-like staining pattern is characteristic for CCEs [20].
• RESULTS: RhCTGF(C) induced striking changes in epithelial cells, including changes in cellular morphology, loss of CK, gain VIM and alpha-SMA, and increased levels of fibronectin [21].

Associations of VIM with chemical compounds

• Neither PMA nor dbcAMP influenced the VIM mRNA expression [22].
• We show that secretion of vimentin, which is phosphorylated at serine and threonine residues, is enhanced by the phosphatase inhibitor okadaic acid and blocked by the specific protein kinase C inhibitor GO6983 [14].
• Furthermore, the coalignment of specific DP proteins along keratin IF but not vimentin IF was correlated with resistance to extraction by Triton [23].
• Vimentin and desmin differ most dramatically in their NH2-terminal "head" regions [24].
• In astrocytes we studied the phosphorylation of the two major cytoskeletal proteins, vimentin and GFAP, which is normally stimulated by isoproterenol, and found that gp120 partially (40-50%) prevented such stimulation [25].

Physical interactions of VIM

• Immunoelectron microscopy showed vimentin filaments attached to desmoplakin-positive plaques of desmosomes [26].
• Overexpression of the plectin IF-binding domain in the T cell line Jurkat induces the perinuclear aggregation of vimentin IFs [27].
• Oxysterol-binding-protein (OSBP)-related protein 4 binds 25-hydroxycholesterol and interacts with vimentin intermediate filaments [28].
• Varying with the cellular background, a diminution of this up-regulation was observed when the putative beta-catenin/TCF binding site of the vimentin promoter was mutated [29].
• The 3' untranslated region of human vimentin mRNA interacts with protein complexes containing eEF-1gamma and HAX-1 [30].

Enzymatic interactions of VIM

• Retaining of the assembly capability of vimentin phosphorylated by mitogen-activated protein kinase-activated protein kinase-2 [31].
• During viral replication, all of vimentin were degraded and phosphorylated keratin 18 increased [32].

Co-localisations of VIM

• Double immunofluorescence staining showed that the newly formed desmin filaments colocalize with preexisting vimentin filaments, but not with preexisting keratin filaments [7].
• In addition we have isolated pure populations of synovial endothelial cells in culture and demonstrate an extensive cytokeratin intermediate filament network which co-localizes with vimentin filaments [33].
• Vimentin coimmunoprecipitated and colocalized with Raf-1 in fibroblasts [34].
• Indeed, TGase 5 co-localize with vimentin and it is able to cross-link vimentin in vitro [35].

Regulatory relationships of VIM

• In contrast, the pro-inflammatory cytokine tumour necrosis factor alpha (TNF-alpha) can trigger secretion of vimentin [14].
• All N-terminal deletion mutants of GFAP share the same phenotype of diffuse cytoplasmic staining when expressed in vimentin-negative SW13 cells [36].
• Menin's interaction with glial fibrillary acidic protein and vimentin suggests a role for the intermediate filament network in regulating menin activity [37].
• Confocal microscopy demonstrated that adult glomeruli display nestin immunoreactivity in vimentin-expressing cells with the podocyte morphology and not in cells bearing the endothelial marker CD31 [38].
• Vimentin was coexpressed with keratin only in epidermoid tumor cells [39].

Other interactions of VIM

• We also show that the anti-inflammatory cytokine interleukin-10 (IL-10), which inhibits PKC activity, blocks secretion of vimentin [14].
• This marked association is not seen with simple epithelial type II keratins, vimentin, or with type I keratins, providing a possible explanation for the greater stability of the epidermal keratin filament architecture over that of other cell types [40].
• In most myogenic systems, synthesis of the intermediate filament (IF) protein vimentin precedes the synthesis of the muscle-specific IF protein desmin [24].
• To investigate the function of GFAP, we have studied the human astrocytoma cell line, U251, which constitutively expresses GFAP and vimentin in the same 10-nm filaments [41].
• We have found that the ATDC protein physically interacts with the intermediate-filament protein vimentin, which is a protein kinase C substrate and colocalizing protein, and with an inhibitor of protein kinase C, hPKCI-1 [15].

Analytical, diagnostic and therapeutic context of VIM

• Our data indicate that immunohistochemistry using anti-NEUN, anti-VIM, and anti-EMA on representative tumor specimens allows clear-cut distinction of CNs vs OGs and CCEs [20].
• Among the panel of antibodies anti-NEUN, anti-VIM and anti-EMA proved most useful for differential diagnosis [20].
• Other immunofluorescence results indicate that the aorta may differ from smaller blood vessels which appear to contain both desmin and vimentin [42].
• Indirect immunofluorescence studies on frozen sections of aorta showed intense staining of the tunica media by antibodies to vimentin, whereas no reaction could be detected with antibodies to desmin [42].
• Microinjection of HIV-1 PR into cultured human fibroblasts resulted in a 9-fold increase in the percentage of cells with an altered and abnormal distribution of vimentin intermediate filaments [43].

References