Journal
JOURNAL OF CELLULAR BIOCHEMISTRY
Volume 85, Issue 4, Pages 775-784Publisher
WILEY-LISS
DOI: 10.1002/jcb.10181
Keywords
lysyl oxidase; smooth muscle cells; signal transduction; extracellular matrix
Categories
Funding
- NATIONAL HEART, LUNG, AND BLOOD INSTITUTE [P01HL013262] Funding Source: NIH RePORTER
- NHLBI NIH HHS [HL13262] Funding Source: Medline
Ask authors/readers for more resources
Lysyl oxidase (LO) plays a critical role in the stabilization and insolubilization of fibrous structural proteins of the extracellular matrix and has been implicated in the suppression of Ras-induced tumorigenesis. Several prior reports demonstrate that the expression of this catalyst is strongly influenced by a variety of effectors of cell function and is responsive to the growth state of fibrogenic cells. Using specific inhibitors of components of signal transduction pathways, the present study reveals that a PKC-MEK-MAPK-dependent pathway is critical to the enhanced expression of the LO gene in response to variations in the levels of the serum component of the growth medium and in response to platelet-derived growth factor (PDGF). PDGF is shown to be the major component of fetal bovine serum, which stimulates the activity of a LO promoter construct.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available