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

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

Cited 39 times inthomson ciCited 41 times inthomson ci
Title
Reciprocal regulation of mammalian nitric oxide synthase and calcineurin by plant calmodulin isoforms
Author
Cho, Moo JeVaghy, PLKondo, RLee, SHDavis, JPRehl, RHeo, WDJohnson, JD
Keywords
LIGHT-CHAIN KINASE; DEPENDENT ENZYMES; CELLS; ACTIVATION; EXPRESSION; PURIFICATION; CALCIUM; GROWTH; WHEAT
Issue Date
199811
Publisher
AMER CHEMICAL SOC
Citation
BIOCHEMISTRY, v.37, no.45, pp.15593 - 15597
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.
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DOI
http://dx.doi.org/10.1021/bi981497g
ISSN
0006-2960
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