Disease relevance of S100A6

• Using a procedure developed to purify calcyclin from mouse Ehrlich ascites tumor cells calcyclin was purified from smooth muscle of chicken gizzard [1].

High impact information on S100A6

• The distribution of calcyclin in some chicken tissues was studied by Western blotting using polyclonal antibodies raised against calcyclin purified from chicken gizzard [2].
• Immunohistochemical studies of chicken gizzard tissue revealed the presence of calcyclin only in muscle fibers [2].
• UV irradiation of mixtures of calcyclin and gizzard beta beta-tropomyosin labeled with benzophenone-iodoacetamide at Cys36, with or without actin, produced crosslinks between tropomyosin chains and calcyclin monomers only in the presence of Ca2+ [3].
• Western blotting of chicken tissues with anti-(gizzard calcyclin) indicated abundant expression of calcyclin in smooth muscle tissues, including esophagus, large intestine, and trachea, with lower levels in lung, heart, kidney, and brain, and none detectable in liver or skeletal muscle [4].
• Two isoforms of calcyclin (A and B), which differ with respect to the presence or absence of a C-terminal lysine, were identified and the native protein was shown to exist as noncovalently associated homodimers (AA and BB) and heterodimers (AB) [4].

Biological context of S100A6

• The deduced amino acid sequence contains 92 residues with 12 substitutions and a 2 amino acid C-terminal extension when compared with human calcyclin [4].

Anatomical context of S100A6

• Calcyclin was purified from chicken gizzard by Ca(2+)-dependent hydrophobic chromatography, heat treatment, and anion-exchange chromatography, N-terminal sequencing of two CNBr peptides confirmed its identity as calcyclin [4].

Associations of S100A6 with chemical compounds

• Chicken gizzard calcyclin bound 45Ca2+ on nitrocellulose filters and exhibited a shift in electrophoretic mobility on urea-PAGE depending on Ca2+ concentration [1].

Other interactions of S100A6

• Characterization of chicken gizzard calcyclin and examination of its interaction with caldesmon [1].

Analytical, diagnostic and therapeutic context of S100A6

• Molecular cloning of chicken calcyclin (S100A6) and identification of putative isoforms [4].
• Titrations of pyreneiodoacetamide-labeled tropomyosin alone or with actin showed binding of calcyclin to tropomyosin with muM dissociation constants when Ca2+ was present [3].

References