Laminin peptide YIGSR induces collagen synthesis in Hs27 human dermal fibroblasts.

Abstract

The dermal ECM is synthesized from fibroblasts and is primarily compromised of fibrillar collagen and elastic fibers, which support the mechanical strength and resiliency of skin, respectively. Laminin, a major glycoprotein located in the basement membrane, promotes cell adhesion, cell growth, differentiation, and migration. The laminin tyrosine-isoleucine-glycine-serine-arginine (YIGSR) peptide, corresponding to the 929-933 sequence of the β1 chain, is known to be a functional motif with effects on the inhibition of tumor metastasis, the regulation of sensory axonal response and the inhibition of angiogenesis through high affinity to the 67kDa laminin receptor. In this study, we identified a novel function of the YIGSR peptide to enhance collagen synthesis in human dermal fibroblasts. To elucidate this novel function regarding collagen synthesis, we treated human dermal fibroblasts with YIGSR peptide in both a time- and dose-dependent manner. According to subsequent experiments, we found that the YIGSR peptide strongly enhanced collagen type 1 synthesis without changing cell proliferation or cellular MMP-1 level. This YIGSR peptide-mediated collagen type 1 synthesis was modulated by FAK inhibitor and MEK inhibitor. This study clearly reveals that YIGSR peptide plays a novel function on the collagen type 1 synthesis of dermal fibroblasts and also suggests that YIGSR is a strong candidate peptide for the treatment of skin aging and wrinkles.

• Authors: Jong Hyuk Yoon, Jaeyoon Kim, Hyeongjoo Lee, So Young Kim, Hwan-Hee Jang, Sung Ho Ryu, Beom Joon Kim, Taehoon G Lee
• Journal: Biochemical and biophysical research communications (Biochem Biophys Res Commun) Vol. 428 Issue 3 Pg. 416-21 (Nov 23 2012) ISSN: 1090-2104 [Electronic] United States
• PMID: 23111328 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
• Copyright: Copyright © 2012 Elsevier Inc. All rights reserved.

Chemical References

• Collagen Type I
• Laminin
• Oligopeptides
• tyrosyl-isoleucyl-glycyl-seryl-arginine
• Focal Adhesion Kinase 1
• Focal Adhesion Kinase 2
• PTK2 protein, human
• Extracellular Signal-Regulated MAP Kinases
• Matrix Metalloproteinase 1

Topics

• Cell Line
• Collagen Type I (biosynthesis, genetics)
• Extracellular Signal-Regulated MAP Kinases (metabolism)
• Fibroblasts (drug effects, metabolism)
• Focal Adhesion Kinase 1 (metabolism)
• Focal Adhesion Kinase 2 (metabolism)
• Humans
• Laminin (pharmacology)
• Matrix Metalloproteinase 1 (metabolism)
• Oligopeptides (pharmacology)
• Phosphorylation
• Protein Biosynthesis
• Skin (drug effects, metabolism)