S100 proteins are low-molecular-weight calcium-binding proteins of the EF-hand superfamily and appear to be involved in the regulation of a number of cellular processes such as cell cycle progression and differentiation (1). Also, S100 proteins have been reported to localize to the plasma membrane in differentiated keratinocytes, suggesting a role in regulating calcium-dependent, membrane-associated events (3). The Calpactin I light chain (S100 calcium-binding protein A10; S100A10) is a member of the S100 family and it forms a heterotetrameric complex with another light chain, p11, and two heavy chains, annexin II and p36 (2). S100A10 is present in basal and spinous cells, in the cytoplasm, and is associated with the plasma membrane. S100A10, as well as a few other members of the S100 family, are suggested as transglutaminase substrates (3).
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