Abstract
Cholecalcin (1) or calbindin (2), is a vitamin D-induced calcium-binding protein (CaBP) which belongs to the group of intracellular proteins that bind calcium with affinity constant Ka = 106M-1(3,4,5). Each calcium-binding site is organized into a structure of 28 amino acid residues called the “EF hand” which consists of a loop flanked by a helices (4,5). Two classes of vitamin D-dependent proteins, which differ in their calcium-binding sites, have been identified in mammals. A 28,000 Mr molecule (28K CaBP) found in kidney and cerebellum has four calcium-binding sites, whereas a 9,000 Mr protein (9K CaBP) mainly located in the duodenum possesses two calcium-binding domains (3,4,6). The chicken, however appears to pro duce only a single 28,000 Mr vitamin D-dependent CaBP with four calcium-binding sites which has been found in high concentration in intestine, kidney, and cerebellum (3). Chick CaBP and 28,000 Mr CaBP have some immunological features in common (6). In contrast, antibodies raised against rat intestinal CaBP do not recognize either the other mammalian and human intestinal CaBPs or the mammalian and avian 28K CaBPs (6,7).
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© 1987 Martinus Nijhoff Publishing, Boston
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Thomasset, M., Warembourg, M., Desplan, C., Perret, C. (1987). Vitamin D-Dependent Calcium-Binding Protein Gene: cDNA Cloning, mRNA Distribution and Regulation in the Rat. In: Spelsberg, T.C., Kumar, R. (eds) Steroid and Sterol Hormone Action. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-2073-9_19
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DOI: https://doi.org/10.1007/978-1-4613-2073-9_19
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