Molecular cloning and characterization of grancalcin, a novel EF-hand calcium-binding protein abundant in neutrophils and monocytes
Boyhan, Angela and Casimir, Colin M. and French, John K. and Teahan, Carmel G. and Segal, Anthony W. (1992) Molecular cloning and characterization of grancalcin, a novel EF-hand calcium-binding protein abundant in neutrophils and monocytes. The Journal of Biological Chemistry, 267 (5). pp. 2928-2933. ISSN 0021-9258
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A novel EF-hand Ca(2+)-binding protein we have called grancalcin has been identified and characterized. This protein is particularly abundant in neutrophils and monocytes, with relatively small amounts in lymphocytes. The cDNA for this protein has been cloned and sequenced. The sequence predicts that the protein is composed of 217 amino acids, with a molecular mass of 24,010 daltons. It contains four EF-hand calcium-binding motifs and exhibits strong homology to sorcin, one of two proteins overexpressed in multidrug-resistant cells whose function is unknown. There are potentially one phosphorylation and two glycosylation sites. The 1.65-kilobase mRNA is detected in bone marrow and is present in neutrophils, monocytes, macrophages, B and T lymphocytes, and the promyelocytic cell line HL60s. The protein displays a Ca(2+)-dependent translocation to the granules and plasma membrane of neutrophils, suggesting that it might play an effector role in the specialized functions of these cells.
|Research Areas:||A. > School of Science and Technology > Natural Sciences
A. > School of Science and Technology > Natural Sciences > Molecular Biology group
|Depositing User:||Dr Colin Casimir|
|Date Deposited:||02 Dec 2009 10:39|
|Last Modified:||10 Mar 2015 10:18|
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