Two-dimensional gel analysis of glandular keratin intermediate filament phosphorylation

✍ Scribed by Jiam Liao; Nam-on Ku; Dr. M. Bishr Omary

• Publisher: John Wiley and Sons
• Year: 1996
• Tongue: English
• Weight: 627 KB
• Volume: 17
• Category: Article
• ISSN: 0173-0835
• DOI: 10.1002/elps.1150171104

✦ Synopsis

Intermediate filament (IF) proteins, in contrast to microtubules and microfilaments, are preferentially expressed in higher eukaryotes, are relatively insoluble, and are made up of a large and diverse family of proteins (reviewed in [1][2][3][4][5]). Aside from the nuclear lamins, members of the cytoplasmic IF protein family are expressed in a tissue-specific manner, as for example keratins in epithelial cells, vimentin in mesenchymal cells, desmin in muscle, and neurofilaments (NF) in neuronal cells. IF proteins undergo several post-translational modifications (Table 1) including phosphorylation (reviewed in [6-1 1]), glycosylation [12-151, acetylation [16], 181, retinoylation [19,20], methylation [21], isoprenylation and proteolysis (reviewed in [lo]). Similar to the tissue-specific expression of I F proteins, keratins are also expressed in an epithelial cell-type specific manner. To date, at least 20 different keratin gene products have been described [22-271, which consist of the acidic (pl < 6) type I keratin 9 to 20 (K9-K20) or the relatively basic ( P I > 6) type I1 keratins 1 to 8 (Kl-K8