Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:1.16.3.1 (ceruloplasmin)
 5,074 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Metal-binding proteins (ceruloplasmin, transferrin, ferritin, and lactoferrin), proteinase inhibitors (alpha 1-antitrypsin, alpha 2-macroglobulin and inter-alpha-trypsin inhibitors), and albumin were assayed in synovial fluid obtained from 20 patients with rheumatoid arthritis (RA) and 15 with osteoarthritis (OA). The levels of proteinase inhibitors and metal-binding proteins, except transferrin, were significantly increased in synovial fluid from RA patients as compared with synovial fluid from OA patients. Metal-binding proteins significantly correlated with rheumatoid factor and immune complexes in synovial fluid from RA patients. Proteinase inhibitor levels also significantly correlated with C-reactive protein, and complement components. These results suggest that the raised level of metal-binding proteins and proteinase inhibitors in synovial fluid from RA patients reflect inflammatory activity, and hence may play an important role in the pathogenesis of inflammatory joint diseases.
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PMID:Correlation of metal-binding proteins and proteinase inhibitors with immunological parameters in rheumatoid synovial fluids. 170 87

This report compares the relative levels of messenger RNA species coding for plasma proteins in rat visceral yolk sac and fetal liver from 12.5 days to 21.5 days gestation. Transthyretin, retinol-binding protein, transferrin and alpha 1-fetoprotein mRNAs were detected in both tissues, although relative levels were much higher in the yolk sac compared to fetal liver, in early gestation. Messenger RNA coding for the positive acute phase proteins thiostatin, fibrinogen, alpha 2-macroglobulin and alpha 1-antitrypsin were detected at a low but significant level in yolk sac, while the levels in fetal liver steadily increased from 16.5 days gestation and, with the exception of alpha 1-antitrypsin, reached levels higher than those found in adult liver just prior to birth. Albumin, inter-alpha 1-trypsin inhibitor, alpha 1-acid glycoprotein, haptoglobin, vitamin D-binding protein and ceruloplasmin messenger RNA levels were either very low or undetectable in yolk sac and fetal liver. Secretion of proteins by yolk sac endoderm occurred largely across the basolateral surface, i.e. towards the fetal compartment. These data support the hypothesis that one function of the yolk sac in the rat is the synthesis and secretion of a select group of plasma proteins to maintain homeostasis in the fetal compartment in the period before the fetal liver has matured sufficiently to carry out this function.
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PMID:Plasma protein synthesis and secretion in the visceral yolk sac of the fetal rat: gene expression, protein synthesis and secretion. 170 70

It has been proposed that excessive and uncontrolled proteolytic activity is an important pathogenetic factor for chronic wounds. Identification of molecules that either control or reflect proteolysis in wounds may prove to be useful in determining wound healing activity. In this study wound fluid was sampled under a polyurethane dressing or on hydrophilic glass filters. Multiple chronic wound fluid components were identified; viz. the previously described alpha2-macroglobulin, alpha1-antitrypsin and fibronectin, as well as "novel" wound fluid molecules such as complement factor C3, inter-alpha-inhibitor, kininogen, IgG, IgA, C-reactive protein, tetranectin, orosomucoid and ceruloplasmin. There appeared to be a highly variable degradation of alpha1-antitrypsin in the wounds; furthermore, the activation of C3 appeared to correlate with the appearance of fibronectin breakdown products. In wound fluid, inter-alpha-inhibitor was degraded. The influence of the sampling procedures was studied. It was shown that contact phase activation must be taken into account in the study of molecules (such as kininogens) activated by hydrophilic charged surfaces.
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PMID:Degradation of antiproteinases, complement and fibronectin in chronic leg ulcers. 1095 7

It is critical to identify at-risk patients and minimize the deleterious effects of cardiopulmonary bypass (CPB) procedures in pediatric populations. The present study screened the plasma proteome of pediatric patients undergoing CPB procedures to identify potential clinical biomarkers related to tissue damage, inflammation, or other pathologies. Blood samples were collected at five different time points from 10 children undergoing a CPB procedure. Plasma was isolated and analyzed using two-dimensional differential in-gel electrophoresis and matrix-assisted laser desorption ionization time of flight mass spectrometry. Levels of differentially regulated proteins identified by two-dimensional differential in-gel electrophoresis, and related proteins were then measured in all time points and patients. As well, associated small molecules and ions were measured. The present study identified 13 proteins and protein isoforms altered in expression, including hemopexin, ceruloplasmin, inter-alpha inhibitor H4, and alpha-2-macroglobulin. Immunoblot analysis revealed significant decreases in each of these proteins during the CPB procedure. Significant changes in the levels of copper, iron, Hb, epinephrine, norepinephrine, and serotonin were observed. The potential markers of pathology (inflammation, oxidative stress) identified during this preliminary study may illuminate opportunities for preventative measures and/or treatments during and following CPB procedures in pediatric patients.
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PMID:Plasma biomarkers in pediatric patients undergoing cardiopulmonary bypass. 1831 39