Assignment of the rat calcineurin inhibitor gene (Cain) to rat chromosome band 20p12 by fluorescence in situ hybridization.

H Kim, Y K Jung, D G Jo, S H Park
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Abstract

Calcineurin is a serine/threonine protein phosphatase activated by calcium and calmodulin (Klee et al., 1988). It mediates the immunosuppressive actions of drugs such as cyclosporin and FK506 (Liu et al., 1991; Friedman and Weissman, 1991), and has diverse roles in calcium sensitive pathways in the nervous system, including regulation of neurotransmitter release (Lieberman and Mody, 1994; Tong et al., 1995) and modulation of long-term changes in synaptic plasticity (Yakel, 1997). Cain (calcineurin inhibitor) is a most potent endogeneous inhibitor of calcineurin and in its physiological role is suspected to provide a docking site for calcineurin in its inactive form (Lai et al., 1998). Recently, full-length Cain cDNA has been cloned from rat brain cDNA library (Lai et al., 1998). In this paper, we localized the rat gene Cain to rat chromosome band 20p12 by fluorescence in situ hybridization. Fig. 1. Chromosomal localization of Cain to rat chromosome 20p12. (A) Fluorescent signals on chromosomes 20p12 as indicated by arrowheads. (B) Ideogram of rat chromosome 20 (Szpirer et al., 1996), showing the location of Cain.
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用荧光原位杂交技术将大鼠钙调磷酸酶抑制剂基因(Cain)定位到大鼠染色体20p12带。
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