Disease relevance of S100A11

• Cloned avian S100A11 expressed in Escherichia coli and purified by Ca(2+)-dependent hydrophobic interaction chromatography and ion-exchange chromatography was recognized by polyclonal antibodies raised against tissue-purified protein and, like tissue-purified S100A11, bound 45Ca2+ in a gel overlay assay [1].

High impact information on S100A11

• A novel Ca(2+)-binding protein, tentatively designated calgizzarin, has been purified to apparent homogeneity from chicken gizzard smooth muscle by W-7 (N-(6-aminohexyl-5-chloro-1-naphthalenesulfonamide))-Sepharose affinity chromatography and ion-exchange chromatography [2].
• On an alkaline/urea gel, calgizzarin migrated faster in the presence of EGTA than in the presence of CaCl2, thereby indicating a Ca(2+)-dependent conformational change in this protein [2].
• So far as the obtained 65-amino acid sequence is concerned, calgizzarin has approximately a 50% sequence homology with S-100 alpha, 47% with S-100 beta, and 39% with pEL-98 protein [2].
• The partial amino acid sequence (65 amino acid residues) of calgizzarin was seen to be SLLAVFQRYAGREGDNLKLSKKEFRTFMNTELASFTKNQKDPAVVDRMMKRLDINSDGQLDFQEF, and two putative Ca(2+)-binding sites (GREGDNLKLSKKE and D INSDGQLDFQE) were detected [2].
• We purified a new EF-hand type calcium binding protein from chicken gizzard smooth muscle, tentatively named calgizzarin (Todoroki, H., et al [3].

Biological context of S100A11

• S100A11 is a member of a multigenic family of Ca(2+)-modulated proteins of the EF-hand type [4].
• We studied the subcellular localization of S100A11 in developing and adult avian skeletal muscle cells by confocal laser scanning microscopy and immunogold cytochemistry to get information about possible functional roles of this protein [4].
• Molecular cloning and sequencing of a cDNA clone encoding a new calcium binding protein, named calgizzarin, from rabbit lung [3].
• Based on the internal peptide sequence of calgizzarin, we isolated and sequenced a cDNA clone coding for calgizzarin from a rabbit lung cDNA library [3].

Anatomical context of S100A11

• We now report the full-length coding sequence of avian smooth muscle S100A11 [1].
• Low levels of S100A11 were found in skeletal muscle cells at embryonic day (E) 8 [4].
• At E12, S100A11 was found in myotubes in the form of fine dots located between Z-discs, and on the sarcolemma and its invaginations [4].
• No evidence for association of S100A11 with the contractile elements of the sarcomeres was obtained [4].
• At E15, S100A11 was found on the sarcolemma and internal membranes, likely longitudinal tubules, where the protein was co-localized in part with S100A1 and S100B [4].

Associations of S100A11 with chemical compounds

• Our data suggests that, like S100A1 and S100B, S100A11 might have a role in the regulation of membrane activities, probably in relation to Ca(2+) fluxes in skeletal muscle cells [4].

Other interactions of S100A11

• Computer aided homology analysis revealed that calgizzarin exhibits a 43.2% homology to S-100 alpha, 38.6% to S-100 beta and 40.0% to annexin II light chain, p10 [3].

Analytical, diagnostic and therapeutic context of S100A11

• Application of W-7-Sepharose affinity chromatography to various tissues revealed that calgizzarin-like proteins were abundant in bovine aorta and rabbit lung [2].
• Calgizzarin has a Mr of 13,000 as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and approximately 30,000 as determined by gel filtration on a TSK G 3000SW high performance liquid chromatography column, suggesting that calgizzarin seems to be a rodlike protein [2].
• Molecular cloning and expression of avian smooth muscle S100A11 (calgizzarin, S100C) [1].
• Finally, the distribution of calgizzarin among chicken tissues was examined by immunoblotting: calgizzarin was expressed at its highest levels in lung tissue, followed by smooth muscle tissues (oesophagus, large intestine, trachea, and gizzard), kidney, liver, brain, and heart; it was not detected in small intestine or skeletal muscle [5].

References