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Fibronectin Matrix as a Scaffold for...

Saunders, Jared Tyler.

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Fibronectin Matrix as a Scaffold for Procollagen Protease Binding and Collagen Processing.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	Fibronectin Matrix as a Scaffold for Procollagen Protease Binding and Collagen Processing./
作者:	Saunders, Jared Tyler.
出版者:	Ann Arbor : ProQuest Dissertations & Theses, : 2019,
面頁冊數:	100 p.
附註:	Source: Dissertations Abstracts International, Volume: 80-12, Section: B.
Contained By:	Dissertations Abstracts International80-12B.
標題:	Molecular biology. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=13885370
ISBN:	9781392270783

Fibronectin Matrix as a Scaffold for Procollagen Protease Binding and Collagen Processing.
Saunders, Jared Tyler.

Fibronectin Matrix as a Scaffold for Procollagen Protease Binding and Collagen Processing. - Ann Arbor : ProQuest Dissertations & Theses, 2019 - 100 p.

Source: Dissertations Abstracts International, Volume: 80-12, Section: B.

Thesis (Ph.D.)--Princeton University, 2019.

This item must not be sold to any third party vendors.

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.

ISBN: 9781392270783Subjects--Topical Terms:

517296
Molecular biology.

Fibronectin Matrix as a Scaffold for Procollagen Protease Binding and Collagen Processing.
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520 $a 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.
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