Huizhi Kou , Qingqiu Han , Chengzhi Xu , Lixia Liao , Yuanjing Hou , Haibo Wang , Juntao Zhang
{"title":"The fibrillogenesis influence the binding specificity of collagen to discoidin domain receptor 2 and cell behavior","authors":"Huizhi Kou , Qingqiu Han , Chengzhi Xu , Lixia Liao , Yuanjing Hou , Haibo Wang , Juntao Zhang","doi":"10.1016/j.colsurfb.2025.114554","DOIUrl":null,"url":null,"abstract":"<div><div>Collagen is one of the most important natural biopolymers, it plays its role as a load-bearing structure in tissues only after polymerizing into fibrils. DDR2 is a collagen-binding receptor tyrosine kinases, playing a role in the regulation of collagen-cell interactions. Here, we studied the recognition of collagen fibrils by DDR2 and the effect of fibrillogenesis on cell biological activity. Our results showed that for monomeric collagen, the binding affinity of DDR2 to mammalian porcine skin collagen is higher than that to fish collagen. When the assembly of collagen monomers into the collagen fibril, the binding affinity of DDR2 is enhanced. In contrast, the binding ability of the hybrid fibril is stronger than the corresponding black carp skin collagen fibrils, and slightly weaker than corresponding porcine skin collagen fibril. This indicates that the introduction of porcine skin collagen in the co-assembly system can regulate the binding of DDR2 to fish-sourced collagen. We also find that compared to monomers, the fibrillogenesis of collagen promotes cell interaction with the collagen substrate, and has an increased ability to induce cells spreading. Our results confirmed that the physical state of collagen impacts its binding with DDR2 and cell behavior. These findings provide new insights into cell-collagen interactions.</div></div>","PeriodicalId":279,"journal":{"name":"Colloids and Surfaces B: Biointerfaces","volume":"250 ","pages":"Article 114554"},"PeriodicalIF":5.4000,"publicationDate":"2025-02-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Colloids and Surfaces B: Biointerfaces","FirstCategoryId":"1","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S092777652500061X","RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"BIOPHYSICS","Score":null,"Total":0}
引用次数: 0
Abstract
Collagen is one of the most important natural biopolymers, it plays its role as a load-bearing structure in tissues only after polymerizing into fibrils. DDR2 is a collagen-binding receptor tyrosine kinases, playing a role in the regulation of collagen-cell interactions. Here, we studied the recognition of collagen fibrils by DDR2 and the effect of fibrillogenesis on cell biological activity. Our results showed that for monomeric collagen, the binding affinity of DDR2 to mammalian porcine skin collagen is higher than that to fish collagen. When the assembly of collagen monomers into the collagen fibril, the binding affinity of DDR2 is enhanced. In contrast, the binding ability of the hybrid fibril is stronger than the corresponding black carp skin collagen fibrils, and slightly weaker than corresponding porcine skin collagen fibril. This indicates that the introduction of porcine skin collagen in the co-assembly system can regulate the binding of DDR2 to fish-sourced collagen. We also find that compared to monomers, the fibrillogenesis of collagen promotes cell interaction with the collagen substrate, and has an increased ability to induce cells spreading. Our results confirmed that the physical state of collagen impacts its binding with DDR2 and cell behavior. These findings provide new insights into cell-collagen interactions.
期刊介绍:
Colloids and Surfaces B: Biointerfaces is an international journal devoted to fundamental and applied research on colloid and interfacial phenomena in relation to systems of biological origin, having particular relevance to the medical, pharmaceutical, biotechnological, food and cosmetic fields.
Submissions that: (1) deal solely with biological phenomena and do not describe the physico-chemical or colloid-chemical background and/or mechanism of the phenomena, and (2) deal solely with colloid/interfacial phenomena and do not have appropriate biological content or relevance, are outside the scope of the journal and will not be considered for publication.
The journal publishes regular research papers, reviews, short communications and invited perspective articles, called BioInterface Perspectives. The BioInterface Perspective provide researchers the opportunity to review their own work, as well as provide insight into the work of others that inspired and influenced the author. Regular articles should have a maximum total length of 6,000 words. In addition, a (combined) maximum of 8 normal-sized figures and/or tables is allowed (so for instance 3 tables and 5 figures). For multiple-panel figures each set of two panels equates to one figure. Short communications should not exceed half of the above. It is required to give on the article cover page a short statistical summary of the article listing the total number of words and tables/figures.