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

J 2017

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

DURAN, Ivan, Jorge H. MARTIN, Mary Ann WEIS, Pavel KREJČÍ, Peter KONIK et. al.

Basic information

Original name

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

Authors

DURAN, Ivan (840 United States of America), Jorge H. MARTIN (840 United States of America), Mary Ann WEIS (840 United States of America), Pavel KREJČÍ (203 Czech Republic, guarantor, belonging to the institution), Peter KONIK (203 Czech Republic), Bing LI (840 United States of America), Yasemin ALANAY (792 Turkey), Caressa LIETMAN (840 United States of America), Brendan LEE (840 United States of America), David EYRE (840 United States of America), Daniel H. COHN (840 United States of America) and Deborah KRAKOW (840 United States of America)

Edition

Journal of Bone and Mineral Research, Hoboken, Wiley-Blackwell, 2017, 0884-0431

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

30202 Endocrinology and metabolism

Country of publisher

United States of America

Confidentiality degree

není předmětem státního či obchodního tajemství

Impact factor

Impact factor: 6.314

RIV identification code

RIV/00216224:14110/17:00096367

Organization unit

Faculty of Medicine

DOI

http://dx.doi.org/10.1002/jbmr.3095

UT WoS

000403220400021

Keywords in English

Lysine hydroxylation

Abstract

V originále

Lysine hydroxylation of type I collagen telopeptides varies from tissue to tissue and these distinct hydroxylation patterns modulate collagen crosslinking to generate a unique extracellular matrix. Abnormalities in these patterns contribute to pathologies that include osteogenesis imperfecta (OI), fibrosis and cancer. Telopeptide procollagen modifications are carried out by lysyl hydroxylase 2 (LH2), however, little is known regarding how this enzyme regulates hydroxylation patterns. We identified an ER complex of resident chaperones that includes HSP47, FKBP65 and BiP regulating the activity of LH2. Our findings show that FKBP65 and HSP47 modulate the activity of LH2 to either favor or repress its activity. BiP was also identified as a member of the complex, playing a role in enhancing the formation of the complex. This newly identified ER chaperone complex contributes to our understanding of how LH2 regulates lysyl hydroxylation of type I collagen C-telopeptides to affect the quality of connective tissues.

Citovat

DURAN, Ivan, Jorge H. MARTIN, Mary Ann WEIS, Pavel KREJČÍ, Peter KONIK, Bing LI, Yasemin ALANAY, Caressa LIETMAN, Brendan LEE, David EYRE, Daniel H. COHN and Deborah KRAKOW. A Chaperone Complex Formed by HSP47, FKBP65 and BiP Modulates Telopeptide Lysyl Hydroxylation of Type I Procollagen. Journal of Bone and Mineral Research. Hoboken: Wiley-Blackwell, 2017, vol. 32, No 6, p. 1309-1319. ISSN 0884-0431. Available from: https://dx.doi.org/10.1002/jbmr.3095.

@article{1376738,
   author = {Duran, Ivan and Martin, Jorge H. and Weis, Mary Ann and Krejčí, Pavel and Konik, Peter and Li, Bing and Alanay, Yasemin and Lietman, Caressa and Lee, Brendan and Eyre, David and Cohn, Daniel H. and Krakow, Deborah},
   article_location = {Hoboken},
   article_number = {6},
   doi = {http://dx.doi.org/10.1002/jbmr.3095},
   keywords = {Lysine hydroxylation},
   language = {eng},
   issn = {0884-0431},
   journal = {Journal of Bone and Mineral Research},
   title = {A Chaperone Complex Formed by HSP47, FKBP65 and BiP Modulates Telopeptide Lysyl Hydroxylation of Type I Procollagen},
   volume = {32},
   year = {2017}
}

TY  - JOUR
ID  - 1376738
AU  - Duran, Ivan - Martin, Jorge H. - Weis, Mary Ann - Krejčí, Pavel - Konik, Peter - Li, Bing - Alanay, Yasemin - Lietman, Caressa - Lee, Brendan - Eyre, David - Cohn, Daniel H. - Krakow, Deborah
PY  - 2017
TI  - A Chaperone Complex Formed by HSP47, FKBP65 and BiP Modulates Telopeptide Lysyl Hydroxylation of Type I Procollagen
JF  - Journal of Bone and Mineral Research
VL  - 32
IS  - 6
SP  - 1309-1319
EP  - 1309-1319
PB  - Wiley-Blackwell
SN  - 08840431
KW  - Lysine hydroxylation
N2  - Lysine hydroxylation of type I collagen telopeptides varies from tissue to tissue and these distinct hydroxylation patterns modulate collagen crosslinking to generate a unique extracellular matrix. Abnormalities in these patterns contribute to pathologies that include osteogenesis imperfecta (OI), fibrosis and cancer. Telopeptide procollagen modifications are carried out by lysyl hydroxylase 2 (LH2), however, little is known regarding how this enzyme regulates hydroxylation patterns. We identified an ER complex of resident chaperones that includes HSP47, FKBP65 and BiP regulating the activity of LH2. Our findings show that FKBP65 and HSP47 modulate the activity of LH2 to either favor or repress its activity. BiP was also identified as a member of the complex, playing a role in enhancing the formation of the complex. This newly identified ER chaperone complex contributes to our understanding of how LH2 regulates lysyl hydroxylation of type I collagen C-telopeptides to affect the quality of connective tissues.
ER  -

DURAN, Ivan, Jorge H. MARTIN, Mary Ann WEIS, Pavel KREJČÍ, Peter KONIK, Bing LI, Yasemin ALANAY, Caressa LIETMAN, Brendan LEE, David EYRE, Daniel H. COHN and Deborah KRAKOW. A Chaperone Complex Formed by HSP47, FKBP65 and BiP Modulates Telopeptide Lysyl Hydroxylation of Type I Procollagen. \textit{Journal of Bone and Mineral Research}. Hoboken: Wiley-Blackwell, 2017, vol.~32, No~6, p.~1309-1319. ISSN~0884-0431. Available from: https://dx.doi.org/10.1002/jbmr.3095.

Detailed Information on Publication Record