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Fibronectin Matrix as a Scaffold for Procollagen Protease Binding and Collagen Processing
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| 자료유형 | 학위논문 |
|---|---|
| 서명/저자사항 | Fibronectin Matrix as a Scaffold for Procollagen Protease Binding and Collagen Processing. |
| 개인저자 | Saunders, Jared Tyler. |
| 단체저자명 | Princeton University. Molecular Biology. |
| 발행사항 | [S.l.]: Princeton University., 2019. |
| 발행사항 | Ann Arbor: ProQuest Dissertations & Theses, 2019. |
| 형태사항 | 100 p. |
| 기본자료 저록 | Dissertations Abstracts International 80-12B. Dissertation Abstract International |
| ISBN | 9781392270783 |
| 학위논문주기 | Thesis (Ph.D.)--Princeton University, 2019. |
| 일반주기 |
Source: Dissertations Abstracts International, Volume: 80-12, Section: B.
Publisher info.: Dissertation/Thesis. Advisor: Schwarzbauer, Jean E. |
| 이용제한사항 | This item must not be sold to any third party vendors. |
| 요약 | The extracellular matrix (ECM) proteins fibronectin (FN) and type I collagen (collagen I) are co-distributed in many tissues and collagens have been shown to depend on a FN matrix for fibrillogenesis. Despite extensive understanding of supramolecular collagen fiber structure and matrix deposition, the molecular interactions of the proteolytic processing of collagen's biosynthetic precursor, type I procollagen (procollagen I), have not been elucidated, in particular the role of FN matrix in that process. Microscopic analysis of a fibroblast ECM showed co-localization of procollagen I with FN fibrils and inhibition of FN matrix assembly led to a significant reduction of proteolytic cleavage of procollagen to initiate fibril formation, and a concurrent enrichment of collagens containing one or both propeptides. We examined the role of FN matrix in procollagen processing by the C-propeptide proteinase BMP-1. We found that BMP-1, like procollagen, co-localizes with FN fibrils in the matrix microenvironment. Binding studies with FN fragments identified a binding site in FN's primary heparin binding domain. In solution, BMP-1-FN interactions and BMP-1 cleavage of procollagen I were both enhanced by the presence of heparin suggesting a role for heparin in complex formation during proteolysis. Indeed, addition of heparin enhanced the rate of procollagen cleavage by matrix-bound BMP-1. Our results show that matrix localization of this proteinase facilitates the initiation of collagen assembly and suggest a model in which FN matrix and associated heparan sulfate act as a scaffold to organize enzyme and substrate for procollagen processing. |
| 일반주제명 | Molecular biology. Cellular biology. |
| 언어 | 영어 |
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