Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0002962 (angina)
 21,142 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The determination of microalbuminuria is a valuable method in the diagnosis of renal and vascular diabetes or hypertension complications. Recently, microalbuminuria appeared to be the predictor of coronary heart diseases (CHD). The presented study comprised 26 patients with stable angina pectoris (AP) and 27 healthy volunteers. We simultaneously evaluated microproteinuria during the first morning and afternoon miction and the 24-h blood pressure. Amongst patients with AP all urine protein concentrations were increased (results in g/mol creatinine): alpha-1-microglobulin (1.04 + 0.13 vs. 0.47 + 0.05, p < 0.001) albumin (0.95 + 0.15 vs. 0.61 + 0.05, p < 0.05) and IgG (1.00 + 0.17 vs. 0.55 + 0.05, p < 0.01) were higher, in comparison to control group values. Indices for diurnal blood pressure rhythm were significantly lower in the AP group for both systolic (1.07 + 0.01 vs. 1.14 + 0.01 p < 0.001) and diastolic (1.09 + 0.02; vs. 1.21 + 0.03 p < 0.01) pressures. A physiological increase of albumin from the afternoon sample was only observed in the control group. Thus, our AP patients demonstrated signs of subclinical nephropathy in both the proximal tubuli and glomeruli.
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PMID:Particular fractions of microproteinuria in patients with stabile angina pectoris and without a clinical nephropathy. 1120 91

Factor XII Tenri (Y34C), a rare cross-reacting material (CRM)-negative factor XII deficiency, was identified in a 71-yr-old Japanese woman with angina pectoris. In the patient's plasma, factor XII activity and antigen levels were only 1.6% and 5.0%, respectively, of those seen in a normal subject. Immunoblot analysis showed that the secreted factor XII Tenri existed not only as a monomer (76 kDa), but also in complexes with apparent molecular weights of approximately 115, 140, 190, 215, and 225 kDa. After reduction with 2-mercaptoethanol, the factor XII Tenri contained in the complexes was completely converted to monomeric form on immunoblot patterns. It appeared that some of the secreted factor XII Tenri formed several types of disulfide-linked complexes, including a factor XII-alpha1-microglobulin complex, through a newly generated Cys residue. The monomeric form of factor XII Tenri, like normal factor XII, was degraded into 2 major fragments with molecular weights of approximately 45 kDa and 30 kDa following mixing with activated partial-thromboplastin-time measuring reagent (cephalin and ellagic acid), whereas the factor XII Tenri that formed the complexes was not. This indicates that the factor XII Tenri present in disulfide-linked complexes with other proteins (and itself) is not converted to active forms, suggesting that attached proteins obstruct or delay the activation of factor XII via an inhibition of its binding to a negatively charged surface in vitro.
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PMID:Characterization of factor XII Tenri, a rare CRM-negative factor XII deficiency. 1522 38