A Chaperone Complex Formed by HSP47, FKBP65, and BiP Modulates Telopeptide Lysyl Hydroxylation of Type I Procollagen-Reference-Cited by-同舟云学术

A Chaperone Complex Formed by HSP47, FKBP65, and BiP Modulates Telopeptide Lysyl Hydroxylation of Type I Procollagen

Published:2017-04-06 Issue:6 Volume:32 Page:1309-1319
ISSN:0884-0431
Container-title:Journal of Bone and Mineral Research
language:en
Short-container-title:J Bone Miner Res

Author:

Duran Ivan¹²,Martin Jorge H¹,Weis Mary Ann³,Krejci Pavel⁴,Konik Peter⁵,Li Bing⁶,Alanay Yasemin⁷,Lietman Caressa⁸,Lee Brendan⁸⁹,Eyre David³,Cohn Daniel H¹⁶,Krakow Deborah¹⁰¹¹

Affiliation:

1. Department of Orthopaedic Surgery; David Geffen School of Medicine; University of California at Los Angeles; Los Angeles CA USA

2. Networking Research Center on Bioengineering; Biomaterials, and Nanomedicine (CIBER-BBN); University of Malaga; Malaga Spain

3. Department of Orthopaedics and Sports Medicine; University of Washington; Seattle WA USA

4. Department of Biology, Faculty of Medicine; Masaryk University; International Clinical Research Center; St. Anne's University Hospital; Brno Czech Republic

5. Faculty of Science; University of South Bohemia; Ceske Budejovice Czech Republic

6. Department of Molecular, Cell, and Developmental Biology; University of California at Los Angeles; Los Angeles CA USA

7. Pediatric Genetics Unit, Department of Pediatrics; Acibadem University School of Medicine; Istanbul Turkey

8. Department of Molecular and Human Genetics; Baylor College of Medicine; Houston TX USA

9. Howard Hughes Medical Institute; Chevy Chase MD USA

10. Department of Human Genetics, David Geffen School of Medicine; University of California at Los Angeles; Los Angeles CA USA

11. Department of Obstetrics and Gynecology; David Geffen School of Medicine; University of California at Los Angeles; Los Angeles CA USA

Funder

National Institutes of Health

Orthopaedic Institute for Children

March of Dimes Foundation

Baylor College of Medicine

Rolanette and Berdon Lawrence Bone Disease Program of Texas

Publisher

Wiley

Subject

Orthopedics and Sports Medicine,Endocrinology, Diabetes and Metabolism

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1002/jbmr.3095/fullpdf

Reference40 articles.

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3. Missense mutations that cause Bruck syndrome affect enzymatic activity, folding, and oligomerization of lysyl hydroxylase 2;Hyry;J Biol Chem,2009

4. Increased formation of pyridinoline cross-links due to higher telopeptide lysyl hydroxylase levels is a general fibrotic phenomenon;van der Slot;Matrix Biol,2004

5. Osteoarthritis-related fibrosis is associated with both elevated pyridinoline cross-link formation and lysyl hydroxylase 2b expression;Remst;Osteoarthr Cartil,2013

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