Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.2.1.31 (beta-glucuronidase)
 7,680 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Neuronal and glial localization of brain peptidases was investigated by means of the kainic acid (KA) lesion technique. Activities of 6 different peptidases were measured in the rat caudate-putamen (CP) and substantia nigra (SN) 2, 7 and 21 days after unilateral intra-CP injection with 2.5 micrograms of KA. As an indicator of KA lesion in CP, substance P content in both CP and SN was also determined. In addition, activities of the same peptidases in the primary and secondary glial cell cultures of fetal rats were measured and compared to those in CP homogenate. After the KA injection, prolyl endopeptidase (Pro-EP) activity was decreased in the lesioned CP and, to a lesser extent, in the ipsilateral SN. The activity of angiotensin-converting enzyme (ACE) in the lesioned CP was decreased with a complex time course, whereas a slow and progressive reduction was observed in the SN. Alanyl and leucyl aminopeptidase (Ala-AP and Leu-AP respectively) activities gave only small changes after the lesion; Ala-AP was decreased and Leu-AP was increased in the lesioned CP, while both were decreased in the SN. Dipeptidyl aminopeptidase (DAP) and arginyl endopeptidase (Arg-EP) activities were increased 5-fold in the CP 7 days after the KA injection. Their increases paralleled that of beta-glucuronidase, the lysosomal marker enzyme. Cultured glial cells contained only a trace amount of ACE activity. Ala-AP and Pro-EP activities were considerably lower in the glial culture cells than in the CP homogenate. In contrast, DAP and Arg-EP as well as lysosomal marker enzymes showed much higher activity in the former than in the latter. These results suggest that (1) Ala-AP and Pro-EP have large neuronal components, (2) ACE is preferencially localized in neurons and (3) DAP and Arg-EP are associated with glial lysosomal function. It is, therefore, concluded that at least a part of the brain peptidases are differentially localized in neurons and glia, and may be involved in specific neuronal or glial function.
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PMID:Brain peptidases: their possible neuronal and glial localization. 608 24

Many enzyme activities in Alzheimer's disease (AD) are changed. Some of these enzyme activities are related to certain neurotransmitter systems. Enzymes in the brain can also be sensitive to antemortem hypoxia. In the present study it was determined if enzyme activities that are altered in AD are also subject to alteration by antemortem hypoxia. As an indicator of antemortem hypoxia brain lactate concentration was used. Enzyme activities measured were those of prolyl endopeptidase (PE), aminopeptidase (AP), phosphatidylinositol (PI) kinase, phosphatidylinositol phosphate kinase, alpha-ketoglutarate dehydrogenase (alpha-KGDH), choline acetyltransferase and beta-glucuronidase. All of these enzyme activities have been measured in AD patients before and several of them have been found to be decreased. In accordance with previous findings, PE, alpha-KGDH and ChAT activities were reduced in AD patients. PI kinase and beta-glucuronidase activities, however, were not reduced, contrary to previous findings. All enzyme activities, except that of beta-glucuronidase, correlated with brain lactate concentration, suggesting that antemortem hypoxia has a major influence on the activity of enzymes in the brain. PE, AP, alpha-KGDH and ChAT activities were still different between AD and control samples when these were matched for lactate concentration. The enzyme activities that were changed in AD were also significantly correlated with lactate concentration, an indicator of antemortem hypoxia, in brain specimens. This suggests that antemortem hypoxia and AD have some factor in common that may be responsible for changes in enzyme activities. Since both PE and alpha-KGDH are known to be sensitive to oxidative stress this factor could be oxidative stress.
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PMID:Affected enzyme activities in Alzheimer's disease are sensitive to antemortem hypoxia. 987 81