1. Effect of laminin tyrosine-isoleucine-glycine-serine-arginine peptide on the growth of human prostate cancer (PC-3) cells in vitro
Hai-ning Yu, Lan-cui Zhang, Jun-guo Yang, Undurti N Das, Sheng-rong Shen Eur J Pharmacol. 2009 Aug 15;616(1-3):251-5. doi: 10.1016/j.ejphar.2009.06.050. Epub 2009 Jul 2.
The laminin tyrosine-isoleucine-glycine-serine-arginine (YIGSR) peptide, corresponding to the 929-933 sequence of beta1 chain, is known to inhibit tumor growth and metastasis. In the present study, we observed that YIGSR not only inhibited the growth and migration of prostate cancer cells in a dose-dependent manner but also decreased mitochondrial membrane potential, inhibited ATP synthesis and increased caspase-9 activity. Investigation into the interaction of YIGSR with 67LR, the receptor for laminin and polyphenol (-) epigallocatechin-3-gallate (EGCG) employing MVD (Molegro Virtual Docker, an integrated platform for predicting protein ligand interactions), revealed that the binding site of YIGSR was the same as that of EGCG that explains as to why YIGSR is able to inhibit the cytotoxicity of EGCG against PC-3 cells.
2. Laminin peptide YIGSR induces collagen synthesis in Hs27 human dermal fibroblasts
Jong Hyuk Yoon, Jaeyoon Kim, Hyeongjoo Lee, So Young Kim, Hwan-Hee Jang, Sung Ho Ryu, Beom Joon Kim, Taehoon G Lee Biochem Biophys Res Commun. 2012 Nov 23;428(3):416-21. doi: 10.1016/j.bbrc.2012.10.070. Epub 2012 Oct 27.
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.
