Can I read Biochemical Characterization of S100A2 in Human Keratinocytes: Subcellular Localization, Dimerization, and Oxidative Cross-Linking11Portions of this work were presented at the Annual Meeting of the Society for Investigative Dermatology, Washington, DC, April, 1997. on EtoBox?

Biochemical Characterization of S100A2 in Human Keratinocytes: Subcellular Localization, Dimerization, and Oxidative Cross-Linking11Portions of this work were presented at the Annual Meeting of the Society for Investigative Dermatology, Washington, DC, April, 1997. by Rohini Deshpande; Timothy L. Woods; Jian Fu; Tong Zhang; Stefan W. Stoll; James T. Elder is a Medicine article available to read on EtoBox.

What is Biochemical Characterization of S100A2 in Human Keratinocytes: Subcellular Localization, Dimerization, and Oxidative Cross-Linking11Portions of this work were presented at the Annual Meeting of the Society for Investigative Dermatology, Washington, DC, April, 1997. about?

S100A2 is a calmodulin-like protein of unknown function, whose transcription is positively regulated in response to ErbB and p53 signaling. Expression of S100A2 is markedly increased in the context of ErbB-driven reactive epidermal hyperplasia, and decreased in the context of hypofunctional p53 mutations in carcinoma cell lines and tumors. This bimodal pattern of regulation suggests an important function for S100A2 in keratinocyte differentiation and carcinogenesis. Taking the biochemical approach to the determination of S100A2 function, we have characterized its physical state and subcellular localization in normal human keratinocytes. S100A2 in hypotonic lysates remained soluble after centrifugation at 100 000 x g, indicating that it is not associated with cell membranes. Permeabilization experiments confirmed the lack of membrane association and revealed a digitonin-insoluble nuclear fraction of S100A2, which was confirmed by immunofluorescence microscopy. Pulldown assays of epitope-tagged S100A2 and yeast two-hybrid screening revealed that S100A2 displays a strong propensity to homodimerize. Naturally expressed S100A2 dimers in normal human keratinocytes readily underwent inter

Who reads Biochemical Characterization of S100A2 in Human Keratinocytes: Subcellular Localization, Dimerization, and Oxidative Cross-Linking11Portions of this work were presented at the Annual Meeting of the Society for Investigative Dermatology, Washington, DC, April, 1997.?

Author

Rohini Deshpande; Timothy L. Woods; Jian Fu; Tong Zhang; Stefan W. Stoll; James T. Elder

Publisher

Nature Publishing Group; Elsevier ; Elsevier Inc.; Elsevier BV; Springer Science and Business Media LLC; Wiley (ISSN 0022-202X)

Published

2000

Language

EN

Field

Medicine (Health Sciences)