Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P02774 (Gc-globulin)
 196 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Twenty-seven independent polymorphic loci were detected by two-dimensional electrophoresis (2DE) of serum, erythrocytes, and fibroblasts in two large families and analyzed for linkage to classical genetic markers. We detected seven serum, four erythrocyte, and 17 fibroblast protein loci that exhibited charge variation in these two families and in a sample of unrelated individuals. The genetic basis of protein variants was confirmed by quantitative gene-dosage dependence and by conformance to Mendelian transmission in the two families, except for four rare variants for which transmission analysis was not possible. Linkage analysis demonstrated that each of the variants represent products of independent loci, with the exception of erythrocyte locus (RBC4), which we also detected in fibroblasts (NC27). Two allozyme polymorphisms, glyoxalase-1 (GLO1) and phosphoglucomutase-3 (PGM3) were specifically identified here based on genotypic concordance and molecular mass. Unknown fibroblast protein (NC22) may be linked to apolipoprotein E (lod score = 2.8 at theta m = theta f = 0), while a serum protein locus (SER1) may be linked to alpha-haptoglobin (lod score = 2.54 at theta m = .20, theta f = .01). Six of seven polymorphic serum loci were previously located on two-dimensional gels: alpha-1 antitrypsin (PI), Gc-globulin (GC), alpha-2 HS glycoprotein (HSGA), alpha-haptoglobin (HP), and two apolipoproteins (APOE and APOA4). Six of 17 polymorphisms detected in fibroblasts were positionally identical to polymorphic loci seen in lymphocytes. These studies indicate a minimum level of average protein charge heterozygosity of approximately 2.2% for the most predominant human cellular proteins and of 5.6% for the most predominant proteins of serum.
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PMID:Twenty-seven protein polymorphisms by two-dimensional electrophoresis of serum, erythrocytes, and fibroblasts in two pedigrees. 386 81

Two-dimensional (2-D) gel analysis was used to examine differences in the levels of 19 plasma proteins: before and after an acute inflammatory reaction (parenteral typhoid vaccination) in normal subjects, between rheumatoid arthritis (RA) patients and normals and in RA patients treated with tenidap (120 mg) and piroxicam (20 mg). Typhoid vaccination increased levels of SAA, haptoglobin alpha1, haptoglobin alpha2, haptoglobin beta and alpha1-anti-chymotrypsin but decreased transthyretin and apolipoprotein E. In RA patients, serum amyloid A (SAA), haptoglobin alpha2, haptoglobin beta, alpha1-antichymotrypsin and C3 proactivator levels were elevated while apolipoprotein A-I, apolipoprotein A-IV, transthyretin, Gc-globulin, alpha2-HS glycoprotein, alpha2-macroglobulin and alpha1-B glycoprotein levels were decreased, compared to normals. Compared to piroxicam, tenidap lowered levels of alpha1-antiprotease and SAA but raised the levels of transthyretin, Gc-globulin, alpha2-HS-glycoprotein and alpha2-macroglobulin in RA patients. C-reactive protein (CRP) could not be quantified on 2-D gels but, when measured by rate nephelometry, levels were reduced after treatment with tenidap compared to piroxicam. The general pattern of the acute phase protein response to an acute inflammatory response to typhoid vaccination is similar to that in the chronic inflammatory condition, RA. The impact of tenidap on both positive and negative acute-phase proteins in RA patients could clearly be distinguished from that of piroxicam.
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PMID:Analysis of changes in acute-phase plasma proteins in an acute inflammatory response and in rheumatoid arthritis using two-dimensional gel electrophoresis. 954 3

To search out novel biomarkers for monitoring diabetes prognosis, we examined the effect of hypoglycemic fungal exopolysaccharides (EPS) on the differential levels of plasma proteins in streptozotocin-induced diabetic rats. The orally administrated EPS exhibited an excellent hypoglycemic effect, lowering the average plasma glucose level, and increasing insulin secretion in diabetic rats. The 2-DE analysis of rat plasma demonstrated that about 500 visualized spots were differentially regulated, of which 20 spots were identified as principal diabetes-associated proteins. The distinct effect of diabetes induction on the pattern of rat plasma proteins includes the down-regulation of albumin, apolipoprotein E (Apo E), alpha1-inhibitor-3, fetuin beta, Gc-globulin, hemopexin, vitronectin, and transthyretin (TTR) monomer, and the up-regulation of Apo A-I, Apo A-IV, ceruloplasmin, alpha1-antitrypsin, serine protease inhibitor III, and transferrin. Those protein levels were interestingly restored to those of healthy rats by EPS treatment, although the order of magnitude of the changes differed widely. Two proteins of interest showed distinct differential expression with opposite trends: TTR tetramer was significantly down-regulated and immunoglobulin (Ig) kappa light chain was significantly up-regulated upon diabetes induction, both of which were also normalized to those of healthy groups after EPS treatment.
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PMID:Effect of fungal polysaccharides on the modulation of plasma proteins in streptozotocin-induced diabetic rats. 1694 19