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Titolo:
Development from actions of bacterial phospholipases C on eucaryotic plasma membranes to molecular biology of GPI-anchored proteins
Autore:
Ikezawa, H;
Indirizzi:
Nagoya City Univ, Fac Pharmaceut Sci, Mizuho Ku, Aichi 4678603, Japan Nagoya City Univ Aichi Japan 4678603 ci, Mizuho Ku, Aichi 4678603, Japan
Titolo Testata:
YAKUGAKU ZASSHI-JOURNAL OF THE PHARMACEUTICAL SOCIETY OF JAPAN
fascicolo: 7, volume: 119, anno: 1999,
pagine: 472 - 494
SICI:
0031-6903(199907)119:7<472:DFAOBP>2.0.ZU;2-K
Fonte:
ISI
Lingua:
JPN
Soggetto:
BOVINE LIVER 5'-NUCLEOTIDASE; BACILLUS-CEREUS SPHINGOMYELINASE; VARIANT SURFACE GLYCOPROTEIN; ERYTHROCYTE-MEMBRANES; BOMBYX-MORI; ALKALINE-PHOSPHATASE; AMINOPEPTIDASE-N; GLYCOSYLPHOSPHATIDYLINOSITOL ANCHOR; NUCLEOTIDE-SEQUENCE; MUTATIONAL ANALYSIS;
Keywords:
bacterial phospholipase C; hemolysis; GPI-anchored protein; plasma membrane;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
81
Recensione:
Indirizzi per estratti:
Indirizzo: Ikezawa, H Nagoya City Univ, Fac Pharmaceut Sci, Mizuho Ku, 3-1 Tanabe Dori, Aichi 4678603, Japan Nagoya City Univ 3-1 Tanabe Dori Aichi Japan 4678603 03, Japan
Citazione:
H. Ikezawa, "Development from actions of bacterial phospholipases C on eucaryotic plasma membranes to molecular biology of GPI-anchored proteins", YAKUGAKU ZA, 119(7), 1999, pp. 472-494

Abstract

Bacterial phospholipases C are known to act on biomembranes, since they can cleave the phosphodiester linkage between the polar head and the hydrophobic moiety of each phospholipid in these membranes. These enzymes have beenclassified into three groups; phosphatidylcholine (PC)-, sphingomyelin (SM)and phosphatidylinositol (PI)-degrading phospholipases C. Enzymatic properties and toxicities of these phospholipases C are reviewed, in relation to author's research. Studies on the hemolytic phospholipases of Clostridium sp., Bacillus cereus etc., revealed that hydrolysis of choline-containing phospholipids such as PC and SM was responsible for the hemolysis of mammalian erythrocytes by these enzymes in the presence of Ca2+ and/or Mg2+. Also, the studies on a structure-activity correlation of SM-hydrolyzing phospholipase C from B. cereus disclosed the similarity of active sites between thisenzyme and bovine pancreatic DNase I. By action of PI-degrading phospholipases C, several membrane proteins such as alkaline phosphatase, 5'-nucleotidase, VSG (protozoal surface glycoprotein) etc., were shown to be released from the plasma membranes of eucaryotic cells. From structural analysis, these proteins have been revealed to be glycosylphosphatidylinositol (GPI)-anchored proteins bound to the plasma membranes with carboxyl terminal-attached glycolipid. Biochemistry and molecular biology of GPI-anchored proteins,including the structures and biosynthetic routes of GPI glycolipids as well as the process of GPI attachment to proteins, requirements of C-terminal signal peptide for the protein modification by GPI, and distribution of GPI-anchored proteins in living world, are described in relation to our studies.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/03/20 alle ore 10:32:20