Vimentin expression

Ikeda, D., Wada, C., Yoneda, C., Abe, H., and Watabe, S. (1999). Carnosine stimulates vimentin expression in cultured rat fibroblasts. Cell Struct. Fund. 24, 79-87. 

Foisner, R., Bohn, W., Mannweiler, K., and Wiche, G. (1995). Distribution and ultrastructure of plectin arrays in subclones of rat glioma C6 cells differing in intermediate filament protein (vimentin) expression./. Struct. Biol. 115, 304—317. 

Heatley M, Whiteside C, Maxwell P, et al. Vimentin expression in benign and malignant breast epithelium. J Clin Pathol. 1993 46 441-445. 

Vimentin coexpression is especially useful in differentiating endometrial endometrioid carcinomas in uterine curettage specimens from endocervical adenocarcinomas including the endometrioid variant of endocervical adenocarcinoma. Endometrial endometrioid carcinomas immunostain strongly for vimentin, but endocervical carcinomas rarely stain (weak focal staining in up to 13% of endocervical carcinomas). i > i However, with the current antigen retrieval techniques, moderate to occasionally strong vimentin expression may be seen in endocervical carcinomas, and a panel approach is more useful in this distinction. ... 

Histopathologic features of malignancy do not accurately predict poor survival. This problem may eventually be solved by IHC. The combination of increased vimentin expression and decreased GFAP expression may predict poor survival in infratentorial anaplastic ependymomas. Anaplastic ependymomas are more likely to overexpress p53 or EGER protein than low-grade ependymomas. ... 

WaUin A, Zhang G, Jones TW, Jaken S, Stevens JL. 1992. Mechanism of the nephrogenic repair response. Studies on prohferation and vimentin expression after 35S-l,2-dichlorovi-nyl-L-cysteine nephrotoxicity in vivo and in cultured proximal tubule epithehal cells. Lab Invest 66(4) 474—484. 

Not all neurons have NFs. Indeed, one entire phylum in the animal kingdom, arthropods, expresses only type V nuclear lamins so arthropod cells have no IF cytoskeletal structures at all. In addition, mature oligodendrocytes lack IFs although their embryonic precursors contain vimentin. Clearly, the IFs are not essential for cell survival. Yet, in large myelinated fibers, NFs make up the bulk of axonal volume and represent a substantial fraction of the total protein in brain. In most organisms, IFs in both glia... 

Schwartz, B., P. Vicart, C. Delouis, and D. Paulin. 1991. Mammalian cell lines can be efficiently established in vitro upon expression of the SV40 large T antigen driven by a promoter sequence derived from the human vimentin gene. Biol Cell 73(1) 7-14. 

Dent, J. A., Poison, A. G., and Klymkowsky, M. W. (1989) A whole-mount immnnocytochemical analysis of the expression of the intermediate filament protein vimentin in Xenopns. Develop. 105, 61-74. 

The five intermediate filaments and their respective tissues are listed in Table 3. Only the intermediate filament, cytokeratin, is selected as useful in the initial classification of tumors. The other intermediate filaments can cause diagnostic confusion because (1) they are usually not expressed in their poorly differentiated counterparts (especially GFAP, NFP, and Desmin) and (2) they are often coexpressed on many types of tumors. Poorly differentiated neuroectodermal tumors may often express more than two intermediate filaments. Vimentin demonstrates the most lineage infidelity. 

In fact, because of the ubiquitous expression of vimentin in tissues and its partial susceptibility to formalin fixation, some authors advocate including vimentin routinely as an internal positive control on all cases (/7). Since many useful molecules also show sensitivity to fixation or processing for histology, vimentin positivity may be used as a gauge of the general preserved antigenicity of the tissue being examined. 

Some sarcomas besides epithelioid sarcoma or synovial sarcoma show coexpression of vimentin and keratin (18). Examining these tumors for the expression of other epithelial markers will help clarify their true nature. 

Carnosine can affect gene expression. Ikeda et al. (1999) showed that carnosine markedly upregulates vimentin synthesis in cultured rat fibroblasts, while an association between carnosine and vimentin, a cytoskele-tal, intermediate filament protein has been noted in glial cells and neurons (Bonfanti et al., 1999). Interestingly, it has also been shown that the protease, oxidized protein hydrolase (OPH), is coexpressed with vimentin in COS cells (Shimizu et al., 2004). Thus, it is at least possible that carnosine could induce synthesis of OPH in the cultured human fibroblasts and thereby increase the cellular ability to eliminate oxidized... 

SUMMERHAYES, I.C., Cheng, Y.E., SuN, T.T., AND Chen, L.B. (1981). Expression of keratin and vimentin intermediate filaments in rabbit bladder epithelial cells at different stages of benzo[a]pyrene-induced neoplastic progression, J. Cell Bio. 90,63. 

The transition from mesenchyme to epithelium involves biochemical changes in the cells and the extracellular matrix, N-CAM expression on cell surfaces disappears, replaced by L-CAM (uvomorulin). Vimentin, a characteristic cytoskeletal component of mesenchyme, disappears, and cytokeratin, characteristic of epithelia, appears. There is a decrease in collagen I extracellularly and an increase in the basement membrane components laminin and collagen IV. 

After epithelialization and the formation of the S-shaped tubule, there is still much that needs to occur in order for the nephron to function. Cells destined to form the podocyte layer of the glomerulus flatten out and lose some of the markers that characterized their earlier transition to epithelium, including c-MYC, HOX-c9, LFB-1 and LFB-3, while keeping a high level of WT1. Expression of more classical mesenchymal markers such as vimentin takes place, but the cells also keep a number of epithelial proteins such as desmosomal components. The result is a tissue that is more organized than most connective tissue but leakier than most epithelium, the optimum design for urine filtration. 

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