Vimentin (D21H3) Rabbit mAb

The cytoskeleton consists of three types of cytosolic fibers: microfilaments (actin filaments), intermediate filaments, and microtubules. Major types of intermediate filaments are distinguished by their cell-specific expression: cytokeratins (epithelial cells), glial fibrillary acidic protein (GFAP) (glial cells), desmin (skeletal, visceral, and certain vascular smooth muscle cells), vimentin (mesenchyme origin), and neurofilaments (neurons). GFAP and vimentin form intermediate filaments in astroglial cells and modulate their motility and shape (1). In particular, vimentin filaments are present at early developmental stages, while GFAP filaments are characteristic of differentiated and mature brain astrocytes. Thus, GFAP is commonly used as a marker for intracranial and intraspinal tumors arising from astrocytes (2). Research studies have shown that vimentin is present in sarcomas, but not carcinomas, and its expression is examined in conjunction with that of other markers to distinguish between the two (3). Vimentin's dynamic structural changes and spatial re-organization in response to extracellular stimuli help to coordinate various signaling pathways (4). Phosphorylation of vimentin at Ser56 in smooth muscle cells regulates the structural arrangement of vimentin filaments in response to serotonin (5,6). Remodeling of vimentin and other intermediate filaments is important during lymphocyte adhesion and migration through the endothelium (7).During mitosis, CDK1 phosphorylates vimentin at Ser56. This phosphorylation provides a PLK binding site for vimentin-PLK interaction. PLK further phosphorylates vimentin at Ser83, which might serve as a memory phosphorylation site and play a regulatory role in vimentin filament disassembly (8,9). Additionally, studies using various soft-tissue sarcoma cells have shown that phosphorylation of vimentin at Ser39 by Akt1 enhances cell migration and survival, suggesting that vimentin could be a potential target for soft-tissue sarcoma targeted therapy (10,11). 1.Eng, L.F. et al. (2000) Neurochem Res 25, 1439-51. 2.Goebel, H.H. et al. (1987) Acta Histochem Suppl 34, 81-93. 3.Leader, M. et al. (1987) Histopathology 11, 63-72. 4.Helfand, B.T. et al. (2004) J Cell Sci 117, 133-41. 5.Tang, D.D. et al. (2005) Biochem J 388, 773-83. 6.Fomina, I.G. et al. (1990) Klin Med (Mosk) 68, 125-7. 7.Nieminen, M. et al. (2006) Nat Cell Biol 8, 156-62. 8.Yamaguchi, T. et al. (2005) J Cell Biol 171, 431-6. 9.Oguri, T. et al. (2006) Genes Cells 11, 531-40. 10.Zhu, Q.S. et al. (2011) Oncogene 30, 457-70. 11.Xue, G. and Hemmings, B.A. (2013) J Natl Cancer Inst 105, 393-404.