Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Nitric oxide activates the beta(2) subunit of soluble guanylyl cyclase in the absence of a second subunit
Autore:
Koglin, M; Vehse, K; Budaeus, L; Scholz, H; Behrends, S;
Indirizzi:
Univ Hamburg, Inst Expt & Klin Pharmacol, D-20251 Hamburg, Germany Univ Hamburg Hamburg Germany D-20251 Pharmacol, D-20251 Hamburg, Germany
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 33, volume: 276, anno: 2001,
pagine: 30737 - 30743
SICI:
0021-9258(20010817)276:33<30737:NOATBS>2.0.ZU;2-6
Fonte:
ISI
Lingua:
ENG
Soggetto:
MOLECULAR-CLONING; ACTIVITY REQUIRES; ALPHA(2) SUBUNIT; ENZYME SUBUNITS; RAT-KIDNEY; EXPRESSION; ADENYLYL; CONTAINS; FORM;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
22
Recensione:
Indirizzi per estratti:
Indirizzo: Behrends, S Univ Hamburg, Inst Expt & Klin Pharmacol, Martinistr 52, D-20251 Hamburg, Germany Univ Hamburg Martinistr 52 Hamburg Germany D-20251 g, Germany
Citazione:
M. Koglin et al., "Nitric oxide activates the beta(2) subunit of soluble guanylyl cyclase in the absence of a second subunit", J BIOL CHEM, 276(33), 2001, pp. 30737-30743

Abstract

Previously characterized mammalian soluble guanylyl cyclases form alpha/beta heterodimers that can be activated by the gaseous messenger, nitric oxide, and the novel guanylyl cyclase modulator YC-1. Four mammalian subunits have been cloned named alpha (1), beta (1), alpha (2), and beta (2). The alpha (1)/beta (1) and alpha (2)/beta (1) heterodimeric enzyme isoforms have been rigorously characterized. The role of the beta (2) subunit has remainedelusive. Here we isolate a novel variant of this subunit and show that thebeta (2) subunit does not need to form heterodimers for catalytic activitybecause enzyme activity can be measured when it is expressed alone in Sf9 cells. In analogy to the beta (3) subunit recently isolated from the insectManduca sexta, activity was dependent on the presence of 4 mm free Mn2+. The EC50 values for the NO-donor diethylamine/NO were shifted to the left byI order of magnitude as compared with the alpha (1)/beta (1) heterodimericform. In the presence of the detergent Tween, NO sensitivity of beta (2) was abolished, but the enzyme could be activated by protoporphyrin IX, indicating removal of a prosthetic heme group and exchange for the heme precursor. We suggest that the beta (2) subunit is the first mammalian NO-sensitiveguanylyl cyclase lacking a heterodimeric structure.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 24/11/20 alle ore 14:31:36