Disease relevance of VIM

• We studied the expression of transfected chicken and hamster vimentin genes in murine erythroleukemia (MEL) cells [1].
• In dorsal root ganglion cell cultures, IFAPa-400 and vimentin were absent from mature neurons but were coexpressed into supportive cells [2].

High impact information on VIM

• We have assessed the mechanism of intermediate filament assembly by assaying the sites of incorporation of chicken vimentin subunits expressed under the control of an inducible promoter in transfected mouse fibroblasts [3].
• Additionally, a remarkable induction (40- to 50-fold) in the abundance of the vimentin mRNA is observed in erythroid cells as chicken development proceeds from 4 to 15 days, which suggests that the level of expression of vimentin during erythroid development is regulated at the transcriptional level [4].
• We have isolated chicken cDNA and genomic clones for the intermediate filament subunit vimentin and show that the gene for this protein, which exists in a single copy in the haploid chicken genome, is transcribed into two mature mRNA species with approximate lengths of 2.0 and 2.3 kb [4].
• Structural associations of synemin and vimentin filaments in avian erythrocytes revealed by immunoelectron microscopy [5].
• Intermediate filaments containing vimentin and synemin form a three-dimensional network in these cells, interlinking the nucleus and plasma membrane [5].

Biological context of VIM

• The chicken vimentin gene. Nucleotide sequence, regulatory elements, and comparison to the hamster gene [6].
• Desmin/vimentin intermediate filaments are dispensable for many aspects of myogenesis [7].
• Taken together with previous results (Inagaki et al., 1987) on the phosphorylation of vimentin by kinase A, a new view on IFs emerges [8].
• Alignment with partial data available for vimentin, glial fibrillary acid protein, neurofilament 68 K, two wool alpha-keratins, and a recently described DNA clone covering 90% of an epidermal keratin shows that all seven proteins have extensive homologies and therefore form a complex multigene family, the intermediate filament proteins [9].
• To investigate the role of the intermediate filament protein vimentin in the normal differentiation and morphogenesis of the eye lens fiber cells, we generated transgenic mice bearing multiple copies of the chicken vimentin gene [10].

Anatomical context of VIM

• Not surprisingly, vimentin is more homologous across animal species than it is to other intermediate filament protein members (e.g. desmin) within the same species [6].
• By immunogold labeling, we demonstrate that "millipede-like" structures seen previously in mammalian cell cytoskeletons after removal of actin by treatment with gelsolin are composed of the cores of vimentin IFs with sidearms containing plectin [11].
• Plectin binding to microtubules was significantly increased in cells from transgenic mice lacking IFs and was reversed by microinjection of exogenous vimentin [11].
• Two-dimensional gel electrophoresis has revealed that vimentin, the predominant subunit of intermediate filaments in cells of mesenchymal origin, is a component of isolated skeletal myofibrils [12].
• Desmin and vimentin may thus be involved in maintaining the lateral registration of sarcomeres by transversely linking adjacent myofibrils at their Z discs [12].

Associations of VIM with chemical compounds

• These results suggest that arginine residues play an essential role in the assembly of vimentin in vivo [13].
• Canavanine inhibits vimentin assembly but not its synthesis in chicken embryo erythroid cells [13].
• Here we show that incubation of chicken embryo erythroid cells in a medium in which arginine has been substituted by its amino acid analogue, canavanine, results in the inhibition of the posttranslational assembly of vimentin into the TX-100-insoluble filaments [13].
• Fractionation of the RNA on formamide-containing sucrose gradients before translation indicates that the desmin messenger RNA is larger than the vimentin messenger RNA and contains an extensive noncoding segment [14].
• In contrast, in the mesonephroi cultured in the presence of TDG and lactose, the epithelial tubular cells expressing E-cadherin also express vimentin [15].

Regulatory relationships of VIM

• During differentiation of most myogenic tissues, vimentin is transiently expressed as the intermediate filament (IF) protein subunit and is progressively replaced by desmin [16].

Other interactions of VIM

• Modulation of tensin and vimentin expression in chick embryo developing cartilage and cultured differentiating chondrocytes [17].
• The combination of insulin and FGF2 caused postmitotic Muller glia to transiently increase their expression of vimentin and putative neuron specific filamentous proteins such as neurofilament, beta3 tubulin and RA4 [18].
• These morphological traits together with the distribution of vimentin, the ES/130 protein, and the JB3/fibrillin-associated antigen suggested a localized transformation of some epicardial mesothelial cells into mesenchyme [19].
• In correctly laminated spheroids, staining for vimentin and glutamine synthetase was much more pronounced than in rosetted spheroids; in particular, a well-established inner limiting membrane stood out wherever the retinal lamination was complete [20].
• In vivo, expression of the epithelial-specific cell adhesion molecule E-cadherin is restricted to differentiated tubular epithelial cells, whereas the intermediate filament protein vimentin is present in mesonephrogenic mesenchyme and is undetectable in tubular epithelial cells [15].

Analytical, diagnostic and therapeutic context of VIM

• We have analyzed intracellular distributions of mRNAs for the cytoskeletal proteins actin, vimentin, and tubulin by in situ hybridization [21].
• Distributions of vimentin and desmin in developing chick myotubes in vivo. I. Immunofluorescence study [22].
• By immunoautoradiography and immunoprecipitations with vimentin antibodies, this protein was identified as vimentin [23].
• The vimentin in the soluble fraction is not sedimented by high speed centrifugation, suggesting that it does not consist of short filaments [23].
• By double indirect immunofluorescence and immunoelectron microscopy, we have now examined the endothelial cells of the micro- and macrovasculature of a variety of tissues and organs of adult chicken in vivo for their content of desmin and vimentin [24].

References