Discovery and Functional Characterization of a Recombinant Fragment of Human Collagen Type XVII
文献类型： 外文期刊
作者： Piao, Lianhua 1 ; Li, Jiajia 2 ; Li, Xiaojing 5 ; Su, Yangyang 1 ; Yuan, Xiaofeng 6 ; Chang, Shan 1 ; Cheng, Xinyi 4 ; Fu, Shengwei 2 ; Kong, Ren 1 ;
作者机构： 1.Jiangsu Univ Technol, Inst Bioinformat & Med Engn, Changzhou 213001, Peoples R China
2.TRAUTEC Med Technol CO Ltd, Changzhou 213000, Peoples R China
3.Primary Biotechnol Co Ltd, Changzhou 213125, Peoples R China
4.Jiangsu Acad Agr Sci, Inst Plant Protect, Nanjing 210014, Peoples R China
5.Proya Cosmet Co Ltd, Hangzhou 310000, Peoples R China
6.Soochow Univ, Affiliated Hosp 3, Dept Orthopaed, Changzhou 213000, Jiangsu, Peoples R China
关键词： collagen; recombinant protein; integrins; laminin; PAR
期刊名称：JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY （ 影响因子：6.2； 五年影响因子：6.4 ）
ISSN： 0021-8561
年卷期： 2025 年 73 卷 11 期
页码：
收录情况： SCI
摘要： COL17A1 is predominantly expressed in skin epithelial cells and primarily localized within hemidesmosomes. It plays an essential role in epidermal-dermal attachment. Consequently, a recombinant human-like COL17A1 protein (rhCOL17) with low molecular weight and high biocompatibility presents a promising and competitive biomaterial. The aim of this study is to gain more insight into the biological functions and underlying molecular mechanisms of rhCOL17, which primarily consists of amino acid residues Gly659-Leu720. Using a combination of surface plasmon resonance (SPR) and liquid chromatography-tandem mass spectrometry (LC-MS/MS), we identified the interacting partner proteins of rhCOL17 in HaCaT cells. These included several collagens, integrins, and cell polarity proteins. Upon rhCOL17 treatment, the expression levels of laminin-332, integrin beta 1, and the cell polarity proteins PAR-3 and PAR-6B were upregulated, while the PRKCZ, AKT, and TGF-beta 1 signaling pathways were activated. Furthermore, rhCOL17 was found to promote cell proliferation and mitigate UV radiation-induced damage, partly by modulating these interacting proteins and their associated signaling pathways. Additional analyses using AlphaFold2 and molecular dynamics simulations revealed that the rhCOL17 peptide bound stably and tightly to the canonical ligand-binding site between the integrin alpha 3 and beta 1 subunits. These findings highlight the potential versatility and applications of rhCOL17 in the field of antiaging.
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