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Titolo:
Role of hippocalcin in Ca2+-induced activation of phospholipase D
Autore:
Hyun, JK; Yon, C; Kim, YS; Noh, DY; Lee, KH; Han, JS;
Indirizzi:
Hanyang Univ, Coll Med, Inst Biomed Sci, Seoul 133791, South Korea HanyangUniv Seoul South Korea 133791 med Sci, Seoul 133791, South Korea Hanyang Univ, Coll Med, Dept Biochem, Seoul 133791, South Korea Hanyang Univ Seoul South Korea 133791 Biochem, Seoul 133791, South Korea Seoul Natl Univ, Coll Med, Dept Surg, Seoul 151742, South Korea Seoul NatlUniv Seoul South Korea 151742 Surg, Seoul 151742, South Korea Catholic Univ Korea, Coll Med, Dept Pharmacol, Seoul 137701, South Korea Catholic Univ Korea Seoul South Korea 137701 , Seoul 137701, South Korea
Titolo Testata:
MOLECULES AND CELLS
fascicolo: 6, volume: 10, anno: 2000,
pagine: 669 - 677
SICI:
1016-8478(200012)10:6<669:ROHICA>2.0.ZU;2-L
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROTEIN-KINASE-C; CALCIUM-BINDING PROTEIN; ADP-RIBOSYLATION FACTOR-1; PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE; POTENTIAL ROLE; HL-60 CELLS; BRAIN; PHOSPHORYLATION; PURIFICATION; RECOVERIN;
Keywords:
calcium; Cdc42; hippocalcin; phospholipase D; PKC; rat brain; Sf9 cell;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
41
Recensione:
Indirizzi per estratti:
Indirizzo: Han, JS Hanyang Univ, Coll Med, Inst Biomed Sci, Seoul 133791, South KoreaHanyang Univ Seoul South Korea 133791 Seoul 133791, South Korea
Citazione:
J.K. Hyun et al., "Role of hippocalcin in Ca2+-induced activation of phospholipase D", MOL CELLS, 10(6), 2000, pp. 669-677

Abstract

The role of hippocalcin as a novel mediator in the PKC-independent Ca2+-induced phospholipase D (PLD) activation pathway was investigated. Hippocalcin was expressed in the SO insect cell expression system because the myristoylation of this protein is essential for its function. PLD and Cdc42 proteins were prepared from a rat brain cell membrane and cytosol, respectively. The recombinant hippocalcin was expressed in the Sf9 cell using expression vector pVL1393. The hippocalcin expressed was purified as a single band on PAGE following the hydrophobic phenyl HPLC and TSKgel G3000SW gel filtration HPLC. The molecular size of the rat brain hippocalcin expressed in this system was estimated to be 22 kDa. Myristoylated hippocalcin migrated fasterthan the non-myristoylated form on SDS-PAGE. Less than 10% of the total hippocalcin expressed was myristoylated in this baculovirus expression system. PLD was extracted from rat brain membranes and chromatographically enriched 70-fold. From the rat brain cytosol, Cdc42 was purified to near homogeneity. While hippocalcin alone did not activate PLD, it increased PLD activity activated with Cdc42 1.8-fold in the presence of calcium (300 nM free calcium). In the absence of calcium in the reaction mixture, the effect of hippocalcin to facilitate Cdc42-activated PLD activity was abolished. This result suggests that hippocalcin might be one of the regulatory proteins in the PKC-independent Ca2+-mediated PLD activation pathway in conjunction with the Cdc42 protein.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/04/20 alle ore 00:34:09