Study summary · research use only
Kisspeptin-10 increases collagen content in the myocardium by focal adhesion kinase activity
Plain-language summary
Paraphrased from the published abstract below — not a verdict on whether anything works.
This study combined human cardiac fibroblast cell culture with mouse serum measurements to examine kisspeptin-10 (KiSS-10) and its role in regulating collagen content in cardiac fibroblasts. The authors report that kisspeptin-10 increased intracellular collagen content in the myocardium and elevated phosphorylated focal adhesion kinase (FAK) levels in human cardiac fibroblasts, with FAK inhibition blocking KiSS-10's stimulatory effect on collagen deposition in vitro. These changes were associated with increased levels of procollagen type I (PICP) and III (PIIICP) propeptides in fibroblast culture medium and mouse PIIICP in serum. KiSS-10 also inhibited release of metalloproteinases (MMP-1,-2,-9) and increased secretion of their tissue inhibitors (TIMP-1,-2,-4), and enhanced expression of procollagen type I and III α1 chains in vitro. The profibrotic activity of KiSS-10 was mediated by FAK, independent of TGF-β1.
Abstract
The aim of the study was to evaluate the role of kisspeptin-10 (KiSS-10) in the regulation of collagen content in cardiac fibroblasts. An attempt was also made to describe the mechanism of the effect of KiSS-10 on collagen metabolism. The studies indicate that kisspeptin-10 significantly increases the content of intracellular collagen in the myocardium. KiSS-10 also elevates the level of phosphorylated focal adhesion kinase (FAK) in human cardiac fibroblasts. The inhibition of FAK negates the stimulatory effect of KiSS-10 on collagen deposition in vitro. These changes correlate with an increase in the level of propeptides of procollagen type I (PICP) and III (PIIICP) in fibroblast culture medium and mouse PIIICP in serum. Moreover, this hormone inhibits the release of metalloproteinases (MMP-1,-2,-9) and elevates the secretion of their tissue inhibitors (TIMP-1,-2,-4). KiSS-10 also enhances the expression of α1 chains of procollagen type I and III in vitro. Thus, KiSS-10 is involved in the regulation of collagen metabolism and cardiac fibrosis. Augmentation of collagen deposition by KiSS-10 is dependent on the protein synthesis elevation, inhibition of MMPs activity (increase of TIMPs release) or decrease of MMPs concentration. The profibrotic activity of KiSS-10 is mediated by FAK and is not dependent on TGF-β1.
pepmg summarizes the peer-reviewed literature and links to every source — it sells nothing, ships nothing, and gives no medical, dosing, or human-use guidance. Don't just trust this summary: follow the citation to its source and read it yourself. Research use only.