Premium
Regulation of lysyl oxidase and cyclooxygenase expression in human lung fibroblasts: interactions among TGF‐β, IL‐1β, and prostaglandin E
Author(s) -
Roy Rupa,
Polgar Peter,
Wang YuYing,
Goldstein Ronald H.,
Taylor Linda,
Kagan Herbert M.
Publication year - 1996
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/(sici)1097-4644(199609)62:3<411::aid-jcb11>3.0.co;2-l
Subject(s) - lysyl oxidase , cyclooxygenase , prostaglandin e2 , chemistry , autocrine signalling , prostaglandin , prostaglandin e , transforming growth factor , medicine , microbiology and biotechnology , endocrinology , biology , biochemistry , enzyme , receptor
Prostaglandin E 2 , transforming growth factor‐β and interleukin‐1β variably regulate the expression of cyclooxygenase 1, cyclooxygenase 2, and lysyl oxidase in IMR90, human embryo lung fibroblasts. Prostaglandin E 2 at 100 nM upregulates cyclooxygenase 1 mRNA by approximately three‐fold while it downregulates lysyl oxidase mRNA levels. Notably, prostaglandin E 2 suppresses the enhancing effect of TGF‐β on basal levels of lysyl oxidase mRNA. These changes in steady state mRNA levels reflect transcriptional level control, at least in part. Corresponding changes are seen in the protein levels of lysyl oxidase, cyclooxygenase 1 and cyclooxygenase 2 and in catalytic activities of these enzymes, including net prostaglandin E 2 synthesis. Cyclooxygenase 2 mRNA(t 1 2 , 30 min) is considerably less stable than that of cyclooxygenase 1 (t 1 2 , 4h) while lysyl oxidase mRNA is unusually stable (t 1 2 > 14h). Taken together with the differing kinetics with which these genes respond to perturbation by these cytokines, the present results suggest a coordinated, autocrine‐like mechanism of regulation of cyclooxygenase 1 and cyclooxygenase 2 and further point to the potential of their metabolic product, prostaglandin E 2 , to suppress the expression of lysyl oxidase in the inflammatory response to injury. © 1996 Wiley‐Liss, Inc.