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Start Over Descriptor "Protein Tyrosine Phosphatases" Language portuguese
2 results on '"Protein Tyrosine Phosphatases"'

1. Proteínas tirosina fosfatases: propriedades e funções biológicas

Author

Márcio André Miranda, Hiroshi Aoyama, Telma Maria Araújo Silva, and Carmen Veríssima Ferreira

Subjects
lcsh:Chemistry, Chemistry, lcsh:QD1-999, Biochemistry, General Chemistry, Protein tyrosine phosphatase, protein tyrosine phosphatases, QD1-999, signal transduction, biological function
Abstract

Protein phosphorylation-dephosphorylation catalyzed by the opposing and dynamic action of protein kinases and phosphatases probably, is the most crucial chemical reaction taking place in living organisms. Protein phosphatases are classified according to their substrate specificity and sensitivity to inhibitory or activator agents, into two families of protein phosphatases: serine/threonine phosphatases and tyrosine phosphatases (PTPs). PTPs can be divided into 3 groups: tyrosine specific phosphatases, dual and low molecular weight phosphatases. The role of tyrosine phosphorylation in mitogenic signaling is well documented, and one would predict that vanadate, pervanadate and other oxidant agents (protein tyrosine phosphatase inhibitors) may act as a growth stimulator.

Published
2003

2. [Contribution towards plague diagnosis].

Author

de Almeida AM, de Souza GT, Santos S, Silva SC, Petribú Mde M, Haver Pde O, Aragão AI, and Tavares C

Subjects
Animals, Enzyme-Linked Immunosorbent Assay, Hemagglutination Tests, Humans, Rabbits, Sensitivity and Specificity, Antibodies, Bacterial blood, Bacterial Outer Membrane Proteins, Bacterial Proteins, Plague diagnosis, Protein Tyrosine Phosphatases, Yersinia pestis immunology
Abstract

Despite the clinical-epidemiological features of plague, numerous suspected cases in Brazilian outbreaks have been discarded because of negative results from the hemagglutination test for antibodies against the Yersinia pestis F1 antigen. The transcendence of plague justifies studying whether such results are due to unresponsiveness to F1, and whether other Y. pestis proteins might be recognized in suspect serum. These would therefore be candidates to be alternative diagnostic targets to the F1 antigen. Thus, strains of Y. pestis and Y. pseudotuberculosis, a recombinant YopH protein and the F1 antigen were used to analyze serum from patients and immune serum from rabbits. F1 and YopH were not recognized by HA-negative human serum and no major protein common to all the human and rabbit serum samples was identified. This allows the conclusion that suspected cases must be subjected to more rigorous clinical-laboratory evaluation, with strengthening of epidemiological investigations in the search of other etiologies.

Published
2007
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