Reciprocal regulation of mammalian nitric oxide synthase and calcineurin by plant calmodulin isoforms
Cited 39 times inCited 41 times in
- Reciprocal regulation of mammalian nitric oxide synthase and calcineurin by plant calmodulin isoforms
- Cho, Moo Je; Vaghy, PL; Kondo, R; Lee, SH; Davis, JP; Rehl, R; Heo, WD; Johnson, JD
- Issue Date
- AMER CHEMICAL SOC
- BIOCHEMISTRY, v.37, no.45, pp.15593 - 15597
- 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.
- Appears in Collections:
- BIO_Journal Papers
- Files in This Item:
- There are no files associated with this item.
can give you direct access to the published full text of this article. (UNISTARs only)
Show full item record
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.