Nestin (protein)

α-internexin in nerve cells, synemin α and desmuslin/synemin β (two alternative transcripts of the DMN gene) in muscle cells, and syncoilin (also in muscle cells). Members of this group mostly preferentially coassemble as heteropolymers in tissues. Steinert et al. has shown that nestin forms homodimers and homotetramers but does not form IF by itself in vitro. In mixtures, nestin preferentially co-assembles with purified vimentin or the type IV IF protein internexin to form heterodimer coiled-coil molecules.^[5]

cDNA using two primers located in the first and fourth exon, respectively. The resulting 270 base pair (bp) long fragment was then sequenced directly in its entirety, and intron positions precisely located by comparison with the genomic sequence. Putative initiation and stop codons for the human nestin gene were found at the same positions as in the rat gene, in regions where overall similarity was very high. Based on this assumption, the human nestin gene encodes a protein with 1618 amino acids, i.e. 187 amino acids shorter than the rat protein.^[7]

neurofilaments and glial fibrillary acidic protein (GFAP). Nestin expression is reinduced in the adult during pathological situations, such as the formation of the glial scar after central nervous system injury and during regeneration of injured muscle tissue.^[4]

neural stem cells, is also expressed in follicle stem cells and their immediate, differentiated progeny. The hair follicle bulge area is an abundant, easily accessible source of actively growing pluripotent adult stem cells. Green fluorescent protein (GFP), whose expression is driven by the nestin regulatory element in transgenic mice, serves to mark hair follicle stem cells. These cells can differentiate into neurons, glia, keratinocytes, smooth muscle cells and melanocytes in vitro. Thus, hair follicle stem cells provide an effective, accessible, autologous source of stem cells for treatment of peripheral nerve injury.^[8]

interact with Cyclin-dependent kinase 5.^[10]