AuthorsMost P, Bernotat J, Ehlermann P, Pleger ST, Reppel M, Börries M, Niroomand F, Pieske B, Janssen PM, Eschenhagen T, Karczewski P, Smith GL, Koch WJ, Katus HA, Remppis A
JournalProc Natl Acad Sci U S A
PubMed ID11717446
'S100A1, a Ca(2+) binding protein of the EF-hand type, is preferentially expressed in myocardial tissue and has been found to colocalize with the sarcoplasmic reticulum (SR) and the contractile filaments in cardiac tissue. Because S100A1 is known to modulate SR Ca(2+) handling in skeletal muscle, we sought to investigate the ... More
Isolation of a YAC clone covering a cluster of nine S100 genes on human chromosome 1q21: rationale for a new nomenclature of the S100 calcium-binding protein family.
'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. More than 10 members of the S100 protein family have been described from human sources so far. We have ... More
Altered expression of the Ca(2+)-binding protein S100A1 in human cardiomyopathy.
AuthorsRemppis A, Greten T, Schäfer BW, Hunziker P, Erne P, Katus HA, Heizmann CW
JournalBiochim Biophys Acta
PubMed ID8898862
'The Ca(2+)-binding protein S100A1 displays a tissue-specific expression pattern with highest levels in myocardium and has been shown to interact with SR-proteins regulating the Ca(2+)-induced Ca(2+)-release. We, therefore, hypothesized that changes in S100A1 gene expression might correlate with the pathognomonic finding of altered SR Ca(2+)-transients in human end stage heart ... More
Identification of an S100A1/S100B target protein: phosphoglucomutase.
AuthorsLandar A, Caddell G, Chessher J, Zimmer DB
JournalCell Calcium
PubMed ID8894274
Phosphoglucomutase was identified as a potential intracellular S100 target protein because it interacted with two members of the S100 family of calcium-modulated proteins, S100A1 and S100B, in gel overlay experiments. These results were confirmed by affinity chromatography experiments demonstrating that S100A1 and S100B bound to phosphoglucomutase-Sepharose in a calcium-dependent manner. ... More
S100A1 is a novel molecular chaperone and a member of the Hsp70/Hsp90 multichaperone complex.
AuthorsOkada M, Hatakeyama T, Itoh H, Tokuta N, Tokumitsu H, Kobayashi R
JournalJ Biol Chem
PubMed ID14638689
Although calmodulin is known to be a component of the Hsp70/Hsp90 multichaperone complex, the functional role of the protein remains uncertain. In this study, we have identified S100A1, but not calmodulin or other S100 proteins, as a potent molecular chaperone and a new member of the multichaperone complex. Glutathione S-transferase ... More