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Titolo:
Direct interaction between endothelial nitric-oxide synthase and dynamin-2- Implications for nitric-oxide synthase function
Autore:
Cao, S; Yao, J; McCabe, TJ; Yao, Q; Katusic, ZS; Sessa, WC; Shah, V;
Indirizzi:
Mayo Clin & Mayo Fdn, GI Res Unit, Rochester, MN 55905 USA Mayo Clin & Mayo Fdn Rochester MN USA 55905 Unit, Rochester, MN 55905 USA Mayo Clin & Mayo Fdn, Dept Med, Rochester, MN 55905 USA Mayo Clin & Mayo Fdn Rochester MN USA 55905 Med, Rochester, MN 55905 USA Yale Univ, Dept Pharmacol, New Haven, CT 06520 USA Yale Univ New Haven CTUSA 06520 Dept Pharmacol, New Haven, CT 06520 USA
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 17, volume: 276, anno: 2001,
pagine: 14249 - 14256
SICI:
0021-9258(20010427)276:17<14249:DIBENS>2.0.ZU;2-W
Fonte:
ISI
Lingua:
ENG
Soggetto:
SRC HOMOLOGY-3 DOMAIN; SIGNAL-TRANSDUCTION; TRANSPORT VESICLES; CAVEOLIN BINDING; ESCHERICHIA-COLI; CELL CAVEOLAE; ENDOCYTOSIS; ASSOCIATION; CALMODULIN; RECEPTOR;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
35
Recensione:
Indirizzi per estratti:
Indirizzo: Shah, V Mayo Clin & Mayo Fdn, GI Res Unit, 200 1st St SW,Alfred 2-435, Rochester, MN 55905 USA Mayo Clin & Mayo Fdn 200 1st St SW,Alfred 2-435 Rochester MN USA 55905
Citazione:
S. Cao et al., "Direct interaction between endothelial nitric-oxide synthase and dynamin-2- Implications for nitric-oxide synthase function", J BIOL CHEM, 276(17), 2001, pp. 14249-14256

Abstract

Endothelial nitric-oxide synthase (eNOS) is regulated in part through specific protein interactions. Dynamin-2 is a large GTPase residing within similar membrane compartments as eNOS, Here we show that dynamin-2 binds directly with eNOS thereby augmenting eNOS activity, Double label confocal immunofluorescence demonstrates colocalization of eNOS and dynamin in both Clone 9 cells cotransfected with green fluorescent protein-dynamin and eNOS, as well as in bovine aortic endothelial cells (BAEC) expressing both proteins endogenously, predominantly in a Gels membrane distribution. Immunoprecipitation of eNOS from BAEC lysate coprecipitates dynamin and, conversely, immunoprecipitation of dynamin coprecipitates eNOS. Additionally, the calcium ionophore, A23187, a reagent that promotes nitric oxide release, enhances coprecipitation of dynamin with eNOS in BAEC, suggesting the interaction between the proteins can be regulated by intracellular signals. In vitro studiesdemonstrate that glutathione S-transferase (GST)-dynamin-2 quantitatively precipitates both purified recombinant eNOS protein as well as in vitro transcribed S-35-labeled eNOS from solution indicating a direct interaction between the proteins in vitro, Scatchard analysis of binding studies demonstrates an equilibrium dissociation constant (K-d) of 27.6 nM. Incubation of purified recombinant eNOS protein with GST-dynamin-2 significantly increaseseNOS activity as does overexpression of dynamin-2 in ECV 304 cells stably transfected with eNOS-green fluorescent protein. These studies demonstrate a direct protein-protein interaction between eNOS and dynamin-2, thereby identifying a new NOS-associated protein and providing a novel function for dynamin. These events may have relevance for eNOS regulation and traffickingwithin vascular endothelium.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 10/07/20 alle ore 19:15:55