Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.14.11.2 (prolyl hydroxylase)
 1,814 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The chick chorioallantoic membrane model (CAM) has previously been used to demonstrate cell proliferation, characteristic of both angiogenesis and fibrogenesis, after exposure to fibrin degradation products. This model has now been adapted for quantitative in vivo assay of collagen polypeptide synthesis and prolyl hydroxylase activity. The CAM exhibits oscillations in the level of labelled collagen, a pattern attributable to rapid intracellular degradation and proline recycling following a brief labelling period. Both collagen synthesis and prolyl hydroxylase activity are stimulated by fibrin degradation products (less than 50 000 MW). Such stimulation occurs by 3 h and precedes the rise in general protein synthesis. Extracts of healing mouse skin wounds, rich in proteases, inhibited collagen synthesis, as did pure plasmin. Conversely, stimulation was achieved when proteolytic activity was neutralized by soybean trypsin inhibitor. These findings help to explain the observation that fibroblasts and endothelial cells proliferate and migrate centrally in an inflammatory lesion without depositing collagen, whilst in a milieu of high proteolytic activity. More peripherally, where proteases are inactivated by antiproteases in inflammatory exudate, such cell movement ceases and collagen deposition is observed.
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PMID:The control of fibrogenesis: stimulation and suppression of collagen synthesis in the chick chorioallantoic membrane with fibrin degradation products, wound extracts and proteases. 300 65

Protein disulphide isomerase (PDI) is a highly abundant and ubiquitous eukaryotic protein that is essential for viability in yeast. Although PDI is thought to catalyse disulphide bond formation and isomerization during protein biosynthesis, PDI has been found previously to have only moderate effects (approximately 25-fold) on the rate of oxidative folding of proteins in vitro. In addition, PDI has been implicated in several apparently unrelated cellular functions. For example, PDI is the beta-subunit of prolyl 4-hydroxylase and is part of the triglyceride transfer complex. The oxidative folding of bovine pancreatic trypsin inhibitor (BPTI) is slow and inefficient in vitro. Here we report that PDI increases by a factor of 3,000-6,000 the rates of folding of kinetically trapped BPTI folding intermediates, in which native structure impedes disulphide bond formation. By contrast, PDI has only small effects on the rate of disulphide bond formation in intermediates that are oxidized readily in the absence of PDI. These results suggest that an important function of PDI is to catalyse disulphide bond formation and rearrangements within kinetically trapped, structured folding intermediates.
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PMID:Efficient catalysis of disulphide bond rearrangements by protein disulphide isomerase. 769 Apr 63