Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: UMLS:C0036474 (
scurvy
)
685
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
In cells, only properly folded procollagen trimers are secreted from the endoplasmic reticulum (ER), while improperly folded abnormal procollagens are retained within the ER. Ascorbic acid is a co-factor in procollagen hydroxylation, which in turn is required for trimer formation. We examined chaperone proteins which bound to procollagen in the absence of ascorbic acid, a model which mimics the human disease
scurvy
at the cellular level. We found that both prolyl 4-hydroxylase (P4-H)/protein disulfide isomerase (PDI) and
HSP47
bound to procollagen in the absence of ascorbic acid. However, the binding of PDI to procollagen decreased when
HSP47
was co-transfected, suggesting that
HSP47
and PDI compete for binding to procollagen. These data indicate that P4-H/PDI and
HSP47
have cooperative but distinct chaperone functions during procollagen biosynthesis.
...
PMID:Procollagen binds to both prolyl 4-hydroxylase/protein disulfide isomerase and HSP47 within the endoplasmic reticulum in the absence of ascorbate. 1064 4
