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Titolo:
Naegleria fowleri amoebae express a membrane-associated calcium-independent phospholipase A(2)
Autore:
Barbour, SE; Marciano-Cabral, F;
Indirizzi:
Virginia Commonwealth Univ, Dept Microbiol & Immunol, Richmond, VA 23298 USA Virginia Commonwealth Univ Richmond VA USA 23298 , Richmond, VA 23298 USA
Titolo Testata:
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR AND CELL BIOLOGY OF LIPIDS
fascicolo: 2-3, volume: 1530, anno: 2001,
pagine: 123 - 133
SICI:
1388-1981(20010226)1530:2-3<123:NFAEAM>2.0.ZU;2-Q
Fonte:
ISI
Lingua:
ENG
Soggetto:
ARACHIDONOYL-HYDROLYZING PHOSPHOLIPASE-A2; CA2+-SENSITIVE CYTOSOLIC PHOSPHOLIPASE-A2; STIMULATED HUMAN PLATELETS; MACROPHAGE CELL-LINE; P388D(1) MACROPHAGES; ACANTHAMOEBA-CASTELLANII; SIGNAL-TRANSDUCTION; ACID; PHOSPHORYLATION; ENZYMES;
Keywords:
amoeba; phospholipase A(2); pathogenesis; cPLA(2); phospholipid; Naegleria fowleri;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
48
Recensione:
Indirizzi per estratti:
Indirizzo: Barbour, SE Virginia Commonwealth Univ, Dept Microbiol & Immunol, Box 980678, Richmond, VA 23298 USA Virginia Commonwealth Univ Box 980678 Richmond VA USA 23298 SA
Citazione:
S.E. Barbour e F. Marciano-Cabral, "Naegleria fowleri amoebae express a membrane-associated calcium-independent phospholipase A(2)", BBA-MOL C B, 1530(2-3), 2001, pp. 123-133

Abstract

Naegleria fowleri, a free-living amoeba, is the causative agent of primaryamoebic meningoencephalitis. Previous reports have demonstrated that N. fowleri expresses one or more forms of phospholipase A(2) (PLA(2)) and that asecreted form of this enzyme is involved in pathogenesis. However, the molecular nature of these phospholipases remains largely unknown. This study was initiated to determine whether N. fowleri expresses analogs of the well-characterized PLA(2)s that are expressed by mammalian macrophages. Amoeba cell homogenates contain a PLA(2) activity that hydrolyzes the substrate that is preferred by the 85 kDa calcium-dependent cytosolic PLA(2), cPLA(2). However, unlike the cPLA(2) enzyme in macrophages, this activity is largely calcium-independent, is constitutively associated with membranes and shows only a modest preference for phospholipids that contain arachidonate. The amoeba PLA(2) activity is sensitive to inhibitors that block the activities of cPLA(2)-alpha and the 80 kDa calcium-independent PLA(2), iPLA(2) that are expressed by mammalian cells. One of these compounds, methylarachidonyl fluorophosphonate, partially inhibits the constitutive release of [H-3]arachidonic acid from pre-labeled amoebae. Together, these data suggest that N. fowleri expresses a constitutively active calcium-independent PLA(2) that may play a role in the basal phospholipid metabolism of these cells. (C) 2001 Elsevier Science B.V. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 26/01/20 alle ore 00:55:41