Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C1519176 (PSA)
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Idiopathic (autoimmune) thrombocytopenic purpura (ITP, AITP) represents a relatively frequent impairment. It involves a syndrome of various diseases with a shortened thrombocytes survival caused by anti-platelet antibodies. The majority of cases are of secondary character. Spleenectomy often evokes a complete remission of thrombocytopenia. The study describes morphologic findings in spleens of 30 patients with the clinical diagnosis of ITP/AITP. The findings were gained by light microscopy from formol-paraffin blocks and histochemical findings from cryostat sections of non-fixed tissue. The alcaline and acidic phosphatases, nonspecific esterase, chloracetate esterase, and dipeptydilpeptidase IV were investigated enzymohistochemically. Immunoglobulins were examined immunohistochemically and T lymphocytes by means of monoclonal antibodies. The affinity HPA--Helix pomatia agglutinin, PHA--phytohemagglutinin from Phaseolus vulgaris, SBA--soy-bean agglutinin from Glycine max. and PSA--peas bean agglutinin from Pisum sativum were investigated by means of specific antilectin antibodies. The human spleen during idiopathic thrombocytopenic purpura accumulates neutrophilic polymorphonuclear granulocytes; platelets-stagnate and are destroyed. These processes can be identified in histologic sections e.g. also by means of anti-fibrinogen antibodies. The red pulp contains foam cells to various extent. Besides generally known processes, the white pulp also displays alterations in composition of cellular compartment of the periarterial lymphatic sheaths. Human spleen distinguishes modified blood platelets as alien corpuscles, and thus eliminates them from the blood circulation system by its immunologic and other mechanisms, the details of which still remain to be clarified. (Fig. 6, Ref. 44.)
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PMID:[The human spleen in idiopathic thrombocytopenic purpura]. 788 65

To assess the analytic quality of laboratory testing in the United States, we obtained proficiency testing survey results from several national programs that comply with Clinical Laboratory Improvement Amendments (CLIA) regulations. We studied regulated tests (cholesterol, glucose, calcium, fibrinogen, and prothrombin time) and nonregulated tests (international normalized ratio [INR], glycohemoglobin, and prostate-specific antigen [PSA]). Quality was assessed on the sigma scale with a benchmark for minimum process performance of 3 sigma and a goal for world-class quality of 6 sigma. Based on the CLIA criteria for acceptable performance in proficiency testing (allowable total errors [TEa]), the national quality of cholesterol testing (TEa = 10%) estimated sigma values as 2.9 to 3.0; glucose (TEa = 10%), 2.9 to 3.3; calcium (TEa = 1.0 mg/dL), 2.8 to 3.0; prothrombin time (TEa = 15%), 1.8; INR (TEa = 20%), 2.4 to 3.5; fibrinogen (TEa = 20%), 1.8 to 3.2; glycohemoglobin (TEa = 10%), 1.9 to 2.6; and PSA (TEa = 10%), 1.2 to 1.8. The analytic quality of laboratory tests requires improvement in measurement performance and more intensive quality control monitoring than the CLIA minimum of 2 levels per day.
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PMID:The quality of laboratory testing today: an assessment of sigma metrics for analytic quality using performance data from proficiency testing surveys and the CLIA criteria for acceptable performance. 1661 37

PfbA (Plasmin(ogen) and Fibronectin Binding protein A) is an adhesin present on the surface of Streptococcus pneumoniae. Initial studies characterized PfbA as plasmin(ogen) and fibronectin binding protein and later it was found that it binds with many other proteins of the extracellular matrix such as fibrinogen, collagen and laminin. It also binds to blood protein human serum albumin (HSA). Interestingly, PfbA exhibits no binding with serum albumins of bovine (BSA), rabbit (RSA) and porcine (PSA) which are sequentially and structurally homologous to HSA. This suggests that PfbA is likely involved in host specificity. Therefore, to get more insights into this aspect, a detailed analysis, which includes the interaction of rPfbA with HSA/BSA/RSA/PSA at different pHs by bio-layer interferometry, comparison of sequences and surface electrostatic potential of HSA/BSA/RSA/PSA, lysine modification of HSA by succinylation and subsequent interaction analysis of succinylated HSA with rPfbA and the secondary structural content estimation by FT-IR spectroscopy was carried out. Since large protrusions are another important geometric feature of protein surfaces, the property was also analyzed for HSA/BSA/RSA/PSA. The results of the above studies clearly suggest that the rPfbA exhibits host specificity by selectively binding only to HSA and not with its homologous BSA/RSA/PSA. Since the three dimensional structures of these albumins are highly similar, it is likely that rPfbA utilizes the differences in the surface electrostatic charge in combination with surface protrusions of HSA/BSA/RSA/PSA for the selective molecular recognition process and this feature may be important in the pathogenesis of pneumococcal infection.
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PMID:Streptococcus pneumoniae Surface Adhesin PfbA Exhibits Host Specificity by Binding to Human Serum Albumin but Not Bovine, Rabbit and Porcine Serum Albumins. 3174 Nov 70