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Proteolytic cleavage confers nitric oxide synthase inducing activity upon prolactin
Corbacho, A. M.; Nava, G.; Eiserich, J. P. et al.
2000In Journal of Biological Chemistry, 275 (18), p. 13183-6
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Keywords :
Animals; Cells, Cultured; Comparative Study; Enzyme Induction/drug effects; Fibroblasts/*metabolism; Nitric Oxide/*metabolism; Nitric Oxide Synthase/*metabolism; Nitric Oxide Synthase Type II; Peptide Fragments/metabolism/*pharmacology; Prolactin/metabolism/*pharmacology; Rats; Rats, Sprague-Dawley; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.
Abstract :
[en] Prolactin (PRL), originally associated with milk secretion, is now known to possess a wide variety of biological actions and diverse sites of production beyond the pituitary. Proteolytic cleavage is a common post-translational modification that can either activate precursor proteins or confer upon the peptide fragment unique biological actions not exerted by the parent molecule. Recent studies have demonstrated that the 16-kDa N-terminal proteolytic cleavage product of PRL (16K-PRL) acts as a potent inhibitor of angiogenesis. Despite previous demonstrations of 16K-PRL production in vivo, biological functions beyond its antiangiogenic actions remain unknown. Here we show that 16K-PRL, but not full-length PRL, acts to promote the expression of the inducible isoform of nitric oxide synthase (iNOS) and nitric oxide (*NO) production by pulmonary fibroblasts and alveolar type II cells with potency comparable with the proinflammatory cytokines interleukin-1beta, interferon gamma, and tumor necrosis factor alpha. The differential effect of 16K-PRL versus PRL occurs through a receptor distinct from known PRL receptors. Additionally, pulmonary fibroblasts express the PRL gene and endogenously produce 16K-PRL, suggesting that this pathway may serve both autocrine and paracrine roles in the regulation of *NO production. These results reveal that proteolytic cleavage of PRL confers upon this classical hormone potent iNOS inducing activity, suggesting its role in inflammatory/immune processes.
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Corbacho, A. M.
Nava, G.
Eiserich, J. P.
Noris, G.
Macotela, Y.
Struman, Ingrid  ;  Université de Liège - ULiège > Département des sciences de la vie > GIGA-R : Biologie et génétique moléculaire
Martinez De La Escalera, G.
Freeman, B. A.
Clapp, C.
Language :
English
Title :
Proteolytic cleavage confers nitric oxide synthase inducing activity upon prolactin
Publication date :
2000
Journal title :
Journal of Biological Chemistry
ISSN :
0021-9258
eISSN :
1083-351X
Publisher :
American Society for Biochemistry and Molecular Biology, United States - Maryland
Volume :
275
Issue :
18
Pages :
13183-6
Peer reviewed :
Peer Reviewed verified by ORBi
Available on ORBi :
since 06 May 2009

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