Molecular cloning of chicken calcyclin (S100A6) and identification of putative isoforms

Biochemistry and Cell Biology

Volumn 75, Issue 6, 1997, Pages 733-738

  Allen, Bruce G ^a  

^a UNIVERSITY OF CALGARY   (Canada)

Author keywords

Ca2+ binding proteins; Calcyclin; CDNA cloning; Isoforms; Smooth muscle

Indexed keywords

CALCIUM BINDING PROTEIN; CALCYCLIN PROTEIN, GALLUS GALLUS; CELL CYCLE PROTEIN; COMPLEMENTARY DNA; PROTEIN S 100; S100A6 PROTEIN, MOUSE; S100A6 PROTEIN, RAT;

AMINO ACID SEQUENCE; ANIMAL; ANTIBODY SPECIFICITY; ARTICLE; AVIAN STOMACH; CHEMISTRY; CHICKEN; DNA SEQUENCE; GENETICS; ISOLATION AND PURIFICATION; ISOMERISM; MOLECULAR CLONING; MOLECULAR GENETICS; MOUSE; NUCLEOTIDE SEQUENCE; RABBIT; RAT; SEQUENCE HOMOLOGY; SMOOTH MUSCLE;

AMINO ACID SEQUENCE; ANIMALS; BASE SEQUENCE; CALCIUM-BINDING PROTEINS; CELL CYCLE PROTEINS; CHICKENS; CLONING, MOLECULAR; DNA, COMPLEMENTARY; GIZZARD; ISOMERISM; MICE; MOLECULAR SEQUENCE DATA; MUSCLE, SMOOTH; ORGAN SPECIFICITY; RABBITS; RATS; S100 PROTEINS; SEQUENCE ANALYSIS, DNA; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 0031324996     PISSN: 08298211     EISSN: None     Source Type: Journal    
DOI: 10.1139/o97-068     Document Type: Article

References (5)

1. 2+-binding properties of calgizzarin (S100C) isolated from chicken gizzard smooth muscle. Biochem. Cell Biol. 74: 687-694.
2. Ando, Y., Watanabe, M., Akatsuka, H., Tokumitsu, H., and Hidaka, H. 1992. Site-directed mutation makes rabbit calcyclin dimer. FEBS Lett. 314: 109-113.
3. Barger, S.W., Wolchok, S.R., and Van Eldik, L.J. 1992. Disulfidelinked S100 beta dimers and signal transduction. Biochim. Biophys.Acta, 1160: 105-112.
4. Calabretta, B., Kaczmarek, L., Mars, W., Ochoa, D., Gibson, C.W., Hirschhorn, R.R., and Baserga, R. 1985. Cell-cycle-specific genes differentially expressed in human leukemias. Proc. Natl. Acad. Sci. U.S.A. 82: 4463-4467.
5. Calabretta, B., Battini, R., Kaczmarek, L., de Riel, J.K., and Baserga, R. 1986. Molecular cloning of the cDNA for a growth factorinducible gene with strong homology to S100, a calcium-binding protein. J. Biol. Chem. 261: 12 628 - 12 632.