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Titolo:
IDENTIFICATION OF MEMBRANE DIPEPTIDASE AS A MAJOR GLYCOSYL-PHOSPHATIDYLINOSITOL-ANCHORED PROTEIN OF THE PANCREATIC ZYMOGEN GRANULE MEMBRANE, AND EVIDENCE FOR ITS RELEASE BY PHOSPHOLIPASE-A
Autore:
HOOPER NM; COOK S; LAINE J; LEBEL D;
Indirizzi:
UNIV LEEDS,DEPT BIOCHEM & MOL BIOL LEEDS LS2 9JT W YORKSHIRE ENGLAND UNIV SHERBROOKE,DEPT BIOL SHERBROOKE PQ J1K 2R1 CANADA
Titolo Testata:
Biochemical journal
, volume: 324, anno: 1997,
parte:, 1
pagine: 151 - 157
SICI:
0264-6021(1997)324:<151:IOMDAA>2.0.ZU;2-L
Fonte:
ISI
Lingua:
ENG
Soggetto:
KIDNEY MICROVILLAR MEMBRANE; ANGIOTENSIN CONVERTING ENZYME; RENAL DIPEPTIDASE; ECTO-ENZYMES; CELLULAR SECRETION; TRYPANOSOMA-BRUCEI; PIG BRAIN; PURIFICATION; FORM; GP-2;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
56
Recensione:
Indirizzi per estratti:
Citazione:
N.M. Hooper et al., "IDENTIFICATION OF MEMBRANE DIPEPTIDASE AS A MAJOR GLYCOSYL-PHOSPHATIDYLINOSITOL-ANCHORED PROTEIN OF THE PANCREATIC ZYMOGEN GRANULE MEMBRANE, AND EVIDENCE FOR ITS RELEASE BY PHOSPHOLIPASE-A", Biochemical journal, 324, 1997, pp. 151-157

Abstract

Membrane dipeptidase (EC 3.4.13.19) enzyme activity that is inhibitedby cilastatin has been detected in pancreatic zymogen granule membranes of human, porcine and rat origin. Immunoelectrophoretic blot analysis of human and porcine pancreatic zymogen granule membranes with polyclonal antisera raised against the corresponding kidney membrane dipeptidase revealed that the enzyme is a disulphide-linked homodimer of subunit mass 61 kDa in the human and 45 kDa in the pig. Although membrane dipeptidase was, along with glycoprotein-2, one of the only two major components of carbonate high pH-washed membranes, no enzyme activityor immunoreactivity was detected in the zymogen granule contents, Digestion with bacterial phosphatidylinositol-specific phospholipase C (PI-PLC), and subsequent recognition by antibodies specific for the crossreacting determinant, revealed that membrane dipeptidase in human andporcine pancreatic zymogen granule membranes is glycosyl-phosphatidylinositol-anchored. Membrane dipeptidase was released from the pancreatic zymogen granule membranes by an endogenous hydrolase, and the released form migrated as a disulphide-linked dimer on SDS/PAGE under non-reducing conditions. Under reducing conditions it migrated with the same apparent molecular mass as the membrane-bound form, and was still a substrate for bacterial PI-PLC. Treatment of kidney microvillar membranes with phospholipase A(2) resulted in the release of membrane dipeptidase in a form that demonstrated electrophoretic and cilastatin-Sepharose binding properties identical to those of the endogenously released form of the enzyme from zymogen granule membranes. These results indicate that the glycosyl-phosphatidylinositol anchor on the pancreatic membrane dipeptidase is cleaved by an endogenous hydrolase, probably aphospholipase A, and that this cleavage may promote the release of the protein from the membrane.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/12/20 alle ore 01:07:44