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Titolo:
Cloning and expression of bovine p47-phox and p67-phox: comparison with the human and murine homologs
Autore:
Bunger, PL; Swain, SD; Clements, MK; Siemsen, DW; Davis, AR; Gauss, KA; Quinn, MT;
Indirizzi:
Montana State Univ, Dept Vet Mol Biol, Bozeman, MT 59717 USA Montana StateUniv Bozeman MT USA 59717 t Mol Biol, Bozeman, MT 59717 USA
Titolo Testata:
JOURNAL OF LEUKOCYTE BIOLOGY
fascicolo: 1, volume: 67, anno: 2000,
pagine: 63 - 72
SICI:
0741-5400(200001)67:1<63:CAEOBP>2.0.ZU;2-D
Fonte:
ISI
Lingua:
ENG
Soggetto:
RESPIRATORY BURST OXIDASE; PHAGOCYTE NADPH OXIDASE; CHRONIC GRANULOMATOUS-DISEASE; PROTEIN-KINASE-C; DOMAIN-MEDIATED INTERACTIONS; CELL-FREE SYSTEM; SH3 DOMAIN; HUMAN-NEUTROPHILS; BINDING-SITE; SUPEROXIDE PRODUCTION;
Keywords:
NADPH oxidase; neutrophil; superoxide anion; host defense;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
90
Recensione:
Indirizzi per estratti:
Indirizzo: Quinn, MT Montana State Univ, Dept Vet Mol Biol, Bozeman, MT 59717 USA Montana State Univ Bozeman MT USA 59717 , Bozeman, MT 59717 USA
Citazione:
P.L. Bunger et al., "Cloning and expression of bovine p47-phox and p67-phox: comparison with the human and murine homologs", J LEUK BIOL, 67(1), 2000, pp. 63-72

Abstract

Neutrophils play an essential role in bovine cellular host defense, and compromised leukocyte function has been linked to the development of respiratory and mucosal infections, During the host defense process, neutrophils migrate into infected tissues where they become activated, resulting in the assembly of neutrophil membrane and cytosolic proteins to form a superoxide anion-generating complex known as the NADPH oxidase, Two of the essential cytosolic components of the NADPH oxidase are p47-phox and p67-phox, Currently, only the human and murine homologs of these proteins have been sequenced. Because of the important role neutrophils play in bovine host defense, we carried out studies to clone, sequence, and express bovine p47-phox and p67-phox, Using polymerase chain reaction (PCR) cloning techniques and a bovine bone marrow cDNA library, we have cloned both of these bovine NADPH oxidase cytosolic components. Comparison of the bovine sequences with those ofthe human and murine homologs showed that they were highly conserved, but also revealed important information regarding key structural features of p47-phox and p67-phox, including location of putative phosphorylation sites. Functional expression of bovine p47-phox and p67-phox showed that these proteins could substitute for the human proteins in reconstituting NADPH oxidase activity in a cell-free assay system, again demonstrating the high degree of conservation between human and bovine homologs, This study greatly contributes to our understanding of the potential structural/functional regions of p47-phox and p67-phox as well as providing information that can be used to study the role of neutrophils in bovine inflammatory diseases.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 14/07/20 alle ore 13:18:54