PMID- 24043621
OWN - NLM
STAT- MEDLINE
DCOM- 20131231
LR  - 20220311
IS  - 1083-351X (Electronic)
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 288
IP  - 44
DP  - 2013 Nov 1
TI  - An additional function of the rough endoplasmic reticulum protein complex prolyl 
      3-hydroxylase 1.cartilage-associated protein.cyclophilin B: the CXXXC motif 
      reveals disulfide isomerase activity in vitro.
PG  - 31437-46
LID - 10.1074/jbc.M113.498063 [doi]
AB  - Collagen biosynthesis occurs in the rough endoplasmic reticulum, and many 
      molecular chaperones and folding enzymes are involved in this process. The 
      folding mechanism of type I procollagen has been well characterized, and protein 
      disulfide isomerase (PDI) has been suggested as a key player in the formation of 
      the correct disulfide bonds in the noncollagenous carboxyl-terminal and 
      amino-terminal propeptides. Prolyl 3-hydroxylase 1 (P3H1) forms a hetero-trimeric 
      complex with cartilage-associated protein and cyclophilin B (CypB). This complex 
      is a multifunctional complex acting as a prolyl 3-hydroxylase, a peptidyl prolyl 
      cis-trans isomerase, and a molecular chaperone. Two major domains are predicted 
      from the primary sequence of P3H1: an amino-terminal domain and a 
      carboxyl-terminal domain corresponding to the 2-oxoglutarate- and iron-dependent 
      dioxygenase domains similar to the alpha-subunit of prolyl 4-hydroxylase and lysyl 
      hydroxylases. The amino-terminal domain contains four CXXXC sequence repeats. The 
      primary sequence of cartilage-associated protein is homologous to the 
      amino-terminal domain of P3H1 and also contains four CXXXC sequence repeats. 
      However, the function of the CXXXC sequence repeats is not known. Several 
      publications have reported that short peptides containing a CXC or a CXXC 
      sequence show oxido-reductase activity similar to PDI in vitro. We hypothesize 
      that CXXXC motifs have oxido-reductase activity similar to the CXXC motif in PDI. 
      We have tested the enzyme activities on model substrates in vitro using a GCRALCG 
      peptide and the P3H1 complex. Our results suggest that this complex could 
      function as a disulfide isomerase in the rough endoplasmic reticulum.
FAU - Ishikawa, Yoshihiro
AU  - Ishikawa Y
AD  - From the Department of Biochemistry and Molecular Biology, Oregon Health and 
      Science University and Shriners Hospital for Children, Research Department, 
      Portland, Oregon 97239.
FAU - Bachinger, Hans Peter
AU  - Bachinger HP
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20130916
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (CRTAP protein, human)
RN  - 0 (Crtap protein, mouse)
RN  - 0 (Extracellular Matrix Proteins)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Molecular Chaperones)
RN  - 0 (Multiprotein Complexes)
RN  - 0 (Peptides)
RN  - 0 (Proteins)
RN  - 0 (Proteoglycans)
RN  - 137497-17-7 (cyclophilin B)
RN  - EC 1.14.11.- (Prolyl Hydroxylases)
RN  - EC 1.14.11.7 (P3H1 protein, human)
RN  - EC 5.2.1.- (Cyclophilins)
RN  - EC 5.3.4.1 (Protein Disulfide-Isomerases)
SB  - IM
MH  - Amino Acid Motifs
MH  - Animals
MH  - Chickens
MH  - Cyclophilins/*chemistry/genetics/metabolism
MH  - Endoplasmic Reticulum, Rough/*chemistry/genetics/metabolism
MH  - Extracellular Matrix Proteins/*chemistry/genetics/metabolism
MH  - Humans
MH  - Membrane Glycoproteins/*chemistry/genetics/metabolism
MH  - Mice
MH  - Molecular Chaperones
MH  - Multiprotein Complexes/*chemistry/genetics/metabolism
MH  - Peptides/chemistry/genetics/metabolism
MH  - Prolyl Hydroxylases
MH  - Protein Disulfide-Isomerases/*chemistry/genetics/metabolism
MH  - Protein Structure, Quaternary
MH  - Protein Structure, Tertiary
MH  - Proteins/*chemistry/genetics/metabolism
MH  - Proteoglycans/*chemistry/genetics/metabolism
PMC - PMC3814740
OTO - NOTNLM
OT  - Collagen
OT  - Collagen Biosynthesis
OT  - Disulfide
OT  - Endoplasmic Reticulum (ER)
OT  - Oxidation-Reduction
OT  - Prolyl 3-Hydroxylase
OT  - Protein Isomerase
EDAT- 2013/09/18 06:00
MHDA- 2014/01/01 06:00
PMCR- 2014/11/01
CRDT- 2013/09/18 06:00
PHST- 2013/09/18 06:00 [entrez]
PHST- 2013/09/18 06:00 [pubmed]
PHST- 2014/01/01 06:00 [medline]
PHST- 2014/11/01 00:00 [pmc-release]
AID - S0021-9258(20)48618-1 [pii]
AID - M113.498063 [pii]
AID - 10.1074/jbc.M113.498063 [doi]
PST - ppublish
SO  - J Biol Chem. 2013 Nov 1;288(44):31437-46. doi: 10.1074/jbc.M113.498063. Epub 2013 
      Sep 16.