Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.4.21.7 (plasmin)
 9,023 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Neuropeptide Y and calcitonin gene-related peptide are abundant neuropeptides in the mammalian central and peripheral nervous systems. Their enzymatic degradation by cultivated neurons, astrocytes, and microglia, as well as by purified urokinase-type plasminogen activator, plasmin, thrombin, and trypsin, was investigated in an in vitro approach to elucidate the role of matrix-degrading serine proteinases for inactivation of neuropeptides, especially those of higher amino acid chain length, in the brain. Astrocytes were almost unable to catabolize the peptides. Cultivated neurons and microglia digested neuropeptide Y through cleavage after Arg19, Arg25, Arg33, and Arg35, calcitonin gene-related peptide was cleaved after Arg11 and Arg18. The same cleavage pattern was observed, when neuropeptide Y and calcitonin gene-related peptide were degraded by purified urokinase-type plasminogen activator, plasmin, thrombin, and trypsin. For further characterization of the neuropeptide-degrading serine proteinase activities from cell cultures, urokinase-type plasminogen activator was identified on microglia by immunostaining, whereas tissue-type plasminogen activator mRNA occurred in neurons and astrocytes, but not in microglia. The data are consistent with the possibility that the neuropeptide-degrading serine proteinase activity on neurons and microglia is due to a mixture of plasmin and plasminogen activator activities.
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PMID:Metabolism of neuropeptide Y and calcitonin gene-related peptide by cultivated neurons and glial cells. 873 50

Neuropeptide Y (NPY) is one of the most abundant neuropeptides in the mammalian central nervous system. Like other neuropeptides, NPY is inactivated by specialized neuropeptidases. To trace the degradation of NPY, an assay was established using biotinylated NPY. Biotinyl-NPY was radiolabeled with Na125l by the chloramine-T method and bound to a streptavidin-agarose matrix. The amount of radiolabeling was analyzed by reverse-phase HPLC. The assay was carried out with five peptidases and inhibitors to demonstrate different specific activity. Measurable amounts of radioactivity were released by treatment with endopeptidase-24.18, plasmin, and trypsin, whereas dipeptidylpeptidase IV (DPPIV) and angiotensin-converting enzyme (ACE) showed no activity in this assay. In the case of DPPIV this is due to a resistance of the assay to aminopeptidase attack. The assay is useful to study the specific degradation of NPY particularly by endopeptidases in all kinds of biological samples.
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PMID:A radioactive assay for the degradation of neuropeptide Y. 878 65