.png){kind=icon}
返回
Collagen Structure-Function Mapping Informs Applications for Regenerative Medicine
.png){kind=icon}
OA
AI
DOI：10.3390/bioengineering8010003.png)
.png){kind=icon}
.png){kind=icon}
分享.png){kind=icon}
收藏
摘要
En 中文
Type I collagen, the predominant protein of vertebrates, assembles into fibrils that orchestrate the form and function of bone, tendon, skin, and other tissues. Collagen plays roles in hemostasis, wound healing, angiogenesis, and biomineralization, and its dysfunction contributes to fibrosis, atherosclerosis, cancer metastasis, and brittle bone disease. To elucidate the type I collagen structure-function relationship, we constructed a type I collagen fibril interactome, including its functional sites and disease-associated mutations. When projected onto an X-ray diffraction model of the native collagen microfibril, data revealed a matrix interaction domain that assumes structural roles including collagen assembly, crosslinking, proteoglycan (PG) binding, and mineralization, and the cell interaction domain supporting dynamic aspects of collagen biology such as hemostasis, tissue remodeling, and cell adhesion. Our type III collagen interactome corroborates this model. We propose that in quiescent tissues, the fibril projects a structural face; however, tissue injury releases blood into the collagenous stroma, triggering exposure of the fibrils' cell and ligand binding sites crucial for tissue remodeling and regeneration. Applications of our research include discovery of anti-fibrotic antibodies and elucidating their interactions with collagen, and using insights from our angiogenesis studies and collagen structure-function model to inform the design of super-angiogenic collagens and collagen mimetics.
Keyword:
type I collagen
type III collagen
interactome
microfibril
ligand binding
extracellular matrix
connective tissue
fibrosis
angiogenesis
hemostasis
therapeutic antibodies
AI总结
对已上传原文的论文进行重点信息的提取，主要内容包括：简要概述、研究摘要、背景介绍、关键亮点、图文解析、展望与总结。
期刊
B
IF:
3.7
论文数:
5.9K
被引数:
1.3W
机构
引用论文
分享收藏Consortium for osteogeneslis imperfecta mutations in the helical domain of type I collagen:: Regions rich in lethal mutations align with collagen binding sites for integrins and proteoglycans.png)
HUMAN MUTATIONOAAI
HUMAN MUTATIONIF3.7
OAAI分享收藏分享收藏REstricted Fluid REsuscitation in Sepsis-associated Hypotension (REFRESH): study protocol for a pilot randomised controlled trialTrialsOAAI
TrialsIF0
OAAI分享收藏
查看更多内容