Disease relevance of VIM

• The demonstration of CKs but not vimentin in the neoplastic cells of a serous superficial ovarian papilloma suggested an origin from the ovarian surface epithelium, while the coexpression of CKs and vimentin in serous papillary and mucinous cystadenomas pointed to a possible origin from the rete ovarii [1].
• Two anaplastic and metastatic tumors originating from spinal cord root, immunonegative for S-100 protein and positive for vimentin, were classified as malignant peripheral nerve sheath tumors (MPNSTs) [2].
• Schwannoma morphology was characterized by the presence of Antoni type A and B pattern and immunoreactivity for S-100 protein and vimentin [2].
• Expression of vimentin in the tubular epithelium of bovine kidneys with interstitial nephritis [3].
• Dual-parameter flow cytometry using specific staining for vimentin proves to be a better method for studying changing mitotic and meiotic steps during the involution and recrudescence of testes in seasonally breeding ruminants, as it relates proliferative processes directly to both spermatogenic and somatic cells [4].

High impact information on VIM

• Foreign epidermal keratins are excluded from vimentin filaments and other structures but readily coassemble with the endogenous keratins and appear to be integrated into the meshwork of the preexisting kidney-type keratin filaments [5].
• Poly(A)+ RNA isolated from bovine muzzle epidermis was microinjected into nonepithelial cells containing only intermediate-sized filaments of the vimentin type [6].
• The intermediate filament proteins, desmin and vimentin, are phosphorylated in skeletal muscle cells in vivo [7].
• A small fraction of the vimentin phosphorylation is cAmP-independent [7].
• Cytoplasmic and nuclear membranes are fragmented and dispersed in the cytoplasm and some bind to vimentin during mitosis [8].

Biological context of VIM

• Nucleotide sequence of the bovine vimentin-encoding cDNA [9].
• The amino-acid sequence of bovine vimentin shows 97.2, 96.8, 96.3 and 84.9% homology with reported aa sequences of human, mouse, hamster and chicken Vim, respectively [9].
• By contrast, the disruption of subcellular compartmentalization of interphase cells led to vimentin phosphorylation by PKC [8].
• Conversely, the plasma membrane contains binding sites that interact in a noncooperative, saturable fashion with vimentin, recognizing its amino-terminal head domain [10].
• The gene (4377 bp, seven introns) which codes for a representative of the glycine-rich subtype of cytokeratins of this subfamily, is compared with genes coding for: another subtype of type I cytokeratin; a basic (type II) cytokeratin gene; and vimentin, a representative of another intermediate filament (IF) protein class [11].

Anatomical context of VIM

• Double immunolabeling revealed that newly assembled keratin was not codistributed with microfilament bundles, microtubules or vimentin filaments [6].
• Desmin and vimentin phosphorylation by the rabbit skeletal muscle catalytic subunit is inhibited by the addition of its regulatory subunit [7].
• The expression of cytokeratins and vimentin was investigated in Madin-Darby bovine epithelial cells (MDBK) in culture under conditions of varied cell spreading and cell-cell contact [12].
• Site specificity in vimentin-membrane interactions: intermediate filament subunits associate with the plasma membrane via their head domains [13].
• Inside-out membrane vesicles (IOVs), depleted of spectrin and actin, bind I125-vimentin in a saturable manner unlike resealed, right-side-out membranes which bind negligible amounts of vimentin in an unsaturable fashion [14].

Associations of VIM with chemical compounds

• These data, taken together with the observation that the NH2-terminal end of vimentin is implicated in the polymerization process (Traub, P., and C. Vorgias, J. Cell Sci., 1983, 63:43-67), imply that intermediate filaments may contact the membrane in an end-on fashion, using the exposed head domains of their terminal subunits [13].
• Once associated with the lipid bilayer, the vimentin polypeptide resists urea treatment, suggesting that it has become an integral constituent associated with part of the membrane [15].
• In the absence of MgCl2 we found a net permanent dipole moment, approximately 45-nm-long dimers for vimentin, approximately 65-nm-long tetramers, hexamers, and possibly octamers for both proteins, and 100-nm aggregates for glial fibrillary acidic protein [16].
• These results indicate that the organization of the intermediate-size filament protein vimentin is markedly affected by cholesterol oxides [17].
• The Triton-insoluble pellet fraction contained several major polypeptides (30-, 43-, 58-, and 240,000 mol-wt), two of which were identified by immunoblotting as cytoplasmic actin (43,000 mol-st) and vimentin (58,000 mol-wt) [18].

Other interactions of VIM

• We find that the alpha-crystallins dramatically inhibit the in vitro assembly of GFAP and vimentin in an ATP-independent manner [19].
• Membrane skeleton proteins include fodrin (nonerythroid spectrin), myosin-IIA, myosin-IG, alpha-actinin 1, alpha-actinin 4, vimentin, and the F-actin-binding protein, supervillin [20].
• Vimentin filaments, cytokeratin filaments, microtubules, E- and N-cadherins as molecules of cell adhesion plaques, and fibronectin filaments were localized by the application of specific antibodies in combination with epifluorescence microscopy [21].
• The cells do not produce vimentin and desmin filaments [22].
• Expression of markers of the contractile phenotype (alpha-actin, calponin) was decreased, and markers of the synthetic phenotype (vimentin, beta-actin) were increased [23].

Analytical, diagnostic and therapeutic context of VIM

• Using reverse transcription-polymerase chain reaction (RT-PCR), we have amplified vimentin (Vim)-encoding sequences from both total and polyadenylated bovine lens RNA [9].
• Immunoprecipitation of this soluble vimentin resulted in the co-precipitation of alpha-crystallins [19].
• Prostatic epithelial cells were negative for vimentin immunofluorescence [24].
• Purity (92%) of the isolated stromal cells was confirmed by indirect immunofluorescence of vimentin intermediate filaments [24].
• When added to soluble vimentin subunits this peptide induces, at fourfold molar excess or slightly above, the appearance of short, regular rod-like structures as determined by electron microscopy of negatively stained and rotary-shadowed preparations as well as by viscometry [25].

References