| LDR | | 00000nam u2200205 4500 |
| 001 | | 000000434165 |
| 005 | | 20200226141938 |
| 008 | | 200131s2019 ||||||||||||||||| ||eng d |
| 020 | |
▼a 9781392270783 |
| 035 | |
▼a (MiAaPQ)AAI13885370 |
| 035 | |
▼a (MiAaPQ)princeton:13021 |
| 040 | |
▼a MiAaPQ
▼c MiAaPQ
▼d 247004 |
| 082 | 0 |
▼a 574 |
| 100 | 1 |
▼a Saunders, Jared Tyler. |
| 245 | 10 |
▼a Fibronectin Matrix as a Scaffold for Procollagen Protease Binding and Collagen Processing. |
| 260 | |
▼a [S.l.]:
▼b Princeton University.,
▼c 2019. |
| 260 | 1 |
▼a Ann Arbor:
▼b ProQuest Dissertations & Theses,
▼c 2019. |
| 300 | |
▼a 100 p. |
| 500 | |
▼a Source: Dissertations Abstracts International, Volume: 80-12, Section: B. |
| 500 | |
▼a Publisher info.: Dissertation/Thesis. |
| 500 | |
▼a Advisor: Schwarzbauer, Jean E. |
| 502 | 1 |
▼a Thesis (Ph.D.)--Princeton University, 2019. |
| 506 | |
▼a This item must not be sold to any third party vendors. |
| 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. |
| 590 | |
▼a School code: 0181. |
| 650 | 4 |
▼a Molecular biology. |
| 650 | 4 |
▼a Cellular biology. |
| 690 | |
▼a 0307 |
| 690 | |
▼a 0379 |
| 710 | 20 |
▼a Princeton University.
▼b Molecular Biology. |
| 773 | 0 |
▼t Dissertations Abstracts International
▼g 80-12B. |
| 773 | |
▼t Dissertation Abstract International |
| 790 | |
▼a 0181 |
| 791 | |
▼a Ph.D. |
| 792 | |
▼a 2019 |
| 793 | |
▼a English |
| 856 | 40 |
▼u http://www.riss.kr/pdu/ddodLink.do?id=T15491436
▼n KERIS
▼z 이 자료의 원문은 한국교육학술정보원에서 제공합니다. |
| 980 | |
▼a 202002
▼f 2020 |
| 990 | |
▼a ***1816162 |
| 991 | |
▼a E-BOOK |