Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0019158 (hepatitis)
 30,205 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Sera from 82 patients with acute or chronic hepatitis and 40 chronic carriers of hepatitis B were examined by ELISA and immunoblotting for reactivity with the glycolytic enzyme aldolase. The results of the ELISA tests, expressed as a percentage of a positive control, were compared to those obtained with sera from 39 patients with rubella, 11 with cytomegalovirus infection and 74 healthy subjects. The ELISA reaction with sera, expressed as mean +/- standard deviation was, for 15 patients with hepatitis A, 58.3 +/- 20.5%; 15 with hepatitis B, 59.5 +/- 42.18; 23 with hepatitis non-A, non-B 51.1 +/- 34.4%; 11 with HBsAg positive chronic active hepatitis, 70.1 +/- 31.5%; and 17 with autoimmune chronic active hepatitis, 66.8 +/- 21.4%. All values were significantly (p less than 0.05-p - less than 0.001) higher than those obtained with sera from carriers of hepatitis B surface antigen, 25.6 +/- 27.2%; rubella, 21.1 +/- 20.0%; cytomegalovirus infection, 19.2 +/- 27.8%; or healthy subjects, 20.9 +/- 16.2%. In two randomly selected sera, reactivity with aldolase by ELISA was neutralized by absorption with the enzyme. Selected sera showing reactivity by ELISA reacted by immunoblotting with aldolase. The findings suggest that acute or chronic liver damage may provoke the production of autoantibodies to aldolase.
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PMID:Autoantibody to aldolase in acute and chronic hepatitis. 332 40

Serum autoantibodies to the glycolytic enzyme enolase have been reported in a diverse range of inflammatory, degenerative, and psychiatric disorders. Diseases in which these antibodies have been reported in high incidence include autoimmune polyglandular syndrome type 1 (80%, 35 of 44), primary (69%, 60 of 87), and secondary (58%, 14 of 24) membranous nephropathy, cancer-associated retinopathy (68.8%, 11 of 16), autoimmune hepatitis type 1 (60%, 12 of 20), mixed cryoglobulinemia with renal involvement (63.6%, seven of 11), cystoid macular edema (60%, six of 10), and endometriosis (50%, 21 of 41). In autoimmune polyglandular syndrome type 1 patients, all had chronic mucocutaneous candidiasis with demonstrated antibody reactivity to candida enolase, which is suggestive of cross reactivity or epitope mimicry. Formation of autoantibodies to enolase may be a normal process, with reported incidence in apparently healthy subjects ranging from 0% (zero of 91) to 11.7% (seven of 60). Nonetheless, we suggest that excessive production of these autoantibodies, which are generated as a consequence of uptake of enolase by antigen-presenting cells and subsequent B cell activation, can potentially initiate tissue injury as a result of immune complex deposition.
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PMID:Disease association, origin, and clinical relevance of autoantibodies to the glycolytic enzyme enolase. 1128 54

Nucleoside analogs used in antiviral therapies need to be phosphorylated to their tri-phospho counterparts in order to be active on their cellular target. Human phosphoglycerate kinase (hPGK) was recently reported to participate in the last step of phosphorylation of cytidine L-nucleotide derivatives [Krishnan PGE, Lam W, Dutschman GE, Grill SP, Cheng YC. Novel role of 3-phosphoglycerate kinase, a glycolytic enzyme, in the activation of L-nucleoside analogs, a new class of anticancer and antiviral agents. J Biol Chem 2003;278:36726-32]. In the present work, we extended the enzymatic study of human PGK specificity to purine and pyrimidine nucleotide derivatives in both D- and L-configuration. Human PGK demonstrated catalytic efficiencies in the 10(4)-10(5)M(-1)s(-1) range for purine ribo-, deoxyribo- and dideoxyribonucleotide derivatives, either in D- or L-configuration. In contrast, it was poorly active with natural pyrimidine D-nucleotides (less than 10(3)M(-1)s(-1)). Pyrimidine L-enantiomers, which are promising therapeutic analogs against B hepatitis, were 2-25 times better substrates than their D-counterparts. The broad specificity of substrate of human PGK suggests that this enzyme may be involved in the cellular activation of several antiviral nucleoside analogs including dideoxyinosine, acyclovir, L-2'-deoxycytosine and L-2'-deoxythymidine.
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PMID:Broad specificity of human phosphoglycerate kinase for antiviral nucleoside analogs. 1545 Sep 40

We identified the autoantibody against phosphoglycerate mutase 1 (PGAM1), which is a glycolytic enzyme, in sera from multiple sclerosis (MS) patients by proteomics-based analysis. We further searched this autoantibody in sera from patients with other neurological diseases. The prevalence of the anti-PGAM1 antibody is much higher in patients with MS and neuromyelitis optica (NMO) than in those with other neurological diseases and in healthy controls. It was reported that the anti-PGAM1 antibody is frequently detected in patients with autoimmune hepatitis (AIH). Results of our study suggest that the anti-PGAM1 antibody is not only a marker of AIH but also a nonspecific marker of central nervous system autoimmune diseases.
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PMID:High prevalence of autoantibodies against phosphoglycerate mutase 1 in patients with autoimmune central nervous system diseases. 1996 79