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Titolo:
PURIFICATION AND CHARACTERIZATION OF AN ARGININE-SPECIFIC PEPTIDASE FROM RAGWEED (AMBROSIA-ARTEMISIIFOLIA) POLLEN
Autore:
BAGAROZZI DA; POTEMPA J; TRAVIS J;
Indirizzi:
UNIV GEORGIA,DEPT BIOCHEM & MOL BIOL ATHENS GA 30605 UNIV GEORGIA,DEPT BIOCHEM & MOL BIOL ATHENS GA 30605 JAGIELLONIAN UNIV,DEPT IMMUNOL & MICROBIOL,INST MOL BIOL KRAKOW POLAND
Titolo Testata:
American journal of respiratory cell and molecular biology
fascicolo: 3, volume: 18, anno: 1998,
pagine: 363 - 369
SICI:
1044-1549(1998)18:3<363:PACOAA>2.0.ZU;2-0
Fonte:
ISI
Lingua:
ENG
Soggetto:
ALPHA-1-PROTEINASE INHIBITOR; MAST-CELLS; HAY-FEVER; IMMUNOTHERAPY; INACTIVATION; PROTEINASE; MEDIATORS; ASTHMA;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
30
Recensione:
Indirizzi per estratti:
Citazione:
D.A. Bagarozzi et al., "PURIFICATION AND CHARACTERIZATION OF AN ARGININE-SPECIFIC PEPTIDASE FROM RAGWEED (AMBROSIA-ARTEMISIIFOLIA) POLLEN", American journal of respiratory cell and molecular biology, 18(3), 1998, pp. 363-369

Abstract

Ragweed (Ambrosia artemisiifolia) is clinically the most important source of seasonal aeroallergens, as it is responsible for the majority and most severe cases of hay fever (allergic rhinitis). Extracts from pollen grains have been shown to contain numerous proteins with various functions, including a novel serine proteolytic enzyme with chymotrypsin-like specificity that has been previously described (J. Biol. Chem. 1996; 271:26227-26232). We now report the isolation and properties of a second, trypsin-like enzyme with a molecular mass near 80 kD, from ragweed pollen extracts. This enzyme has a blocked N-terminus, a pH optimum near 9.0, and requires Ca2+ for stability and activity, but not reducing agents. The enzyme is inhibited by diisopropyl fluorophosphate, a general serine class proteinase inhibitor, and more specifically by N-p-tosyl-L-lysine chloromethyl ketone. Activity toward protein substrates was not detected, but various synthetic substrates and smallbiologically active peptides were efficiently cleaved, with a strong preference for Arg in the P-1 position and either Arg or Gly in the P-2 position. This specificity was confirmed through inhibition studies with both peptidyl chloromethyl ketone and organophosphate inhibitors. Significantly, atrial natriuretic peptide and angiotensin 2, whose degradation would amplify kinin activity and influence inflammatory diseases of the respiratory tract and nasal passages, were also rapidly hydrolyzed. Thus, the ragweed pollen endopeptidase may be involved in the inactivation of regulatory neuropeptides during pollen-initiated allergic reactions.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 18/09/20 alle ore 17:19:39