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Titolo:
SERINE PROTEINASE-INHIBITORS INFLUENCE THE STABILITY OF TROPOELASTIN MESSENGER-RNA IN NEONATAL RAT LUNG FIBROBLAST-CULTURES
Autore:
MCGOWAN SE; LIU RG; HARVEY CS; JAECKEL EC;
Indirizzi:
UNIV IOWA HOSP & CLIN,DEPT INTERNAL MED,C33B-GH IOWA CITY IA 52242 DEPT VET AFFAIRS,RES SERV IOWA CITY IA 52242 UNIV IOWA,COLL MED IOWA CITY IA 52242
Titolo Testata:
American journal of physiology. Lung cellular and molecular physiology
fascicolo: 3, volume: 14, anno: 1996,
pagine: 376 - 385
SICI:
1040-0605(1996)14:3<376:SPITSO>2.0.ZU;2-G
Fonte:
ISI
Lingua:
ENG
Soggetto:
ELASTIN GENE-EXPRESSION; MUSCLE CELL-CULTURES; INCREASES ELASTIN; BETA; IDENTIFICATION; ELASTOGENESIS; DEGRADATION; MODEL;
Keywords:
ELASTIN; MESSENGER RIBONUCLEIC ACID STABILITY;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
24
Recensione:
Indirizzi per estratti:
Citazione:
S.E. Mcgowan et al., "SERINE PROTEINASE-INHIBITORS INFLUENCE THE STABILITY OF TROPOELASTIN MESSENGER-RNA IN NEONATAL RAT LUNG FIBROBLAST-CULTURES", American journal of physiology. Lung cellular and molecular physiology, 14(3), 1996, pp. 376-385

Abstract

Elastin, an elastic extracellular structural protein, is a polymer comprised of soluble tropoelastin (TE) monomers that are joined by covalent cross-links and become insoluble. In cultured vascular smooth muscle cells, the steady-state level of TE mRNA is influenced by soluble elastin moieties in the culture medium, either TE or its fragmentation products. We have hypothesized that an enzyme-mediated proteolytic event may modulate the quantities of TE and its fragmentation products inthe culture medium of mesenchymal cells, and thereby indirectly regulate the steady-state level of TE mRNA. Neonatal rat lung fibroblasts were cultured in the presence or absence of the serine proteinase inhibitor, aprotinin, and the quantities of soluble elastin and TE mRNA were analyzed. Exposures to aprotinin lasting up to 12 h increased the soluble elastin content of the culture medium. The increase in the soluble elastin content did not reflect an increase in TE mRNA, which diminished after exposures for 12 h or longer. The decrease in TE mRNA resulted from a decrease in its half-life, rather than a decrease in the rate of TE gene transcription. Aprotinin did not reduce TE mRNA in plasminogen-depleted cultures, but the effect of aprotinin was evident when purified plasminogen was added back to the cultures. Therefore, a serine proteinase, possibly plasmin, may participate in a feedback mechanism and modulate the quantity of TE in lung fibroblast cultures. Thismechanism may help ensure that intracellular TE synthesis occurs in tandem with extracellular elastin deposition and cross-linking.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 23/09/20 alle ore 22:07:37