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Cho, Moo Je
Ulsan National Institute of Science and Technology
Research Interests
  • Calcium Signaling
  • Calmodulin
  • Plant Defense Mechanism


Reciprocal regulation of mammalian nitric oxide synthase and calcineurin by plant calmodulin isoforms

DC Field Value Language Cho, Moo Je ko Vaghy, PL ko Kondo, R ko Lee, SH ko Davis, JP ko Rehl, R ko Heo, WD ko Johnson, JD ko 2014-09-23T07:04:54Z - 2014-09-22 ko 1998-11 ko
dc.identifier.citation BIOCHEMISTRY, v.37, no.45, pp.15593 - 15597 ko
dc.identifier.issn 0006-2960 ko
dc.identifier.uri -
dc.description.abstract Calmodulin (CaM) is the primary mediator of Ca signal transduction processes in cells. Unlike animal cells, plant cells express multiple CaM isoforms. One cloned soybean CaM isoform (SCaM-4) half-maximally activated mammalian nitric oxide synthase (NOS) at 180 nM while another (SCaM-1) served as a competitive antagonist (K(i) ≃ 120 nM) of this activation. The reciprocal was true for the protein phosphatase calcineurin (CAN); SCaM-1 half-maximally activated mammalian CaN at ~12 nM, and SCaM-4 competitively antagonized (K(i) ≃ 70 nM) its activation. The reciprocal enzyme activation and competitive inhibition exhibited by these plant CaM isoforms suggest that their differential expression in cells could allow selective activation of some target enzymes and the selective inhibition of others. This may allow for a branching or bifurcation in the Ca2+-CaM signal transduction pathway and to alterations in cell function. ko
dc.description.statementofresponsibility close -
dc.language 영어 ko
dc.publisher AMER CHEMICAL SOC ko
dc.title Reciprocal regulation of mammalian nitric oxide synthase and calcineurin by plant calmodulin isoforms ko
dc.type ARTICLE ko
dc.identifier.scopusid 2-s2.0-0032506166 ko
dc.identifier.wosid 000077143600001 ko
dc.type.rims ART ko
dc.description.wostc 39 *
dc.description.scopustc 41 * 2015-05-06 * 2014-09-22 *
dc.identifier.doi 10.1021/bi981497g ko
dc.identifier.url ko
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