Dynorphin A Processing Enzyme: Tissue Distribution, Isolation, and Characterization.

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概要

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• Limited proteolysis of the dynorphin precursor (prodynorphin) at dibasic and monobasic processing sites results in the generation of bioactive dynorphins. In the brain and neurointermediate lobe of the pituitary, prodynorphin is processed to produce α and β neo endorphins, dynorphins (Dyn) A-17 and Dyn A-8, Dyn B-13, and leucine-enkephalin. The formation of Dyn A-8 from Dyn A-17 requires a monobasic cleavage between Ile and Arg. We have identified an enzymatic activity capable of processing at this monobasic site in the rat brain and neurointermediate lobe of the bovine pituitary; this enzyme is designated "dynorphin A-17 processing enzyme." In the rat brain and neurointermediate lobe, a majority of the Dyn A processing enzyme activity is membrane-associated and can be released by treatment with 1% Triton X-100. This enzyme has been purified to apparent homogeneity from the membrane extract of the neurointermediate lobe using preparative iso-electrofocussing in a granulated gel pH 3.5 to 10, FPLC using anion exchange chromatography, and non-denaturing electrophoresis. The Dyn A processing enzyme exhibits a pI of about 5.8 and a molecular mass of about 65 kDa under reducing conditions. The Dyn A processing enzyme is a metalloprotease and has a neutral pH optimum. It exhibits substantial sensitivity to metal chelating agents and thiol agents suggesting that this enzyme is a thiol-sensitive metalloprotease. Specific inhibitors of other metallopeptidases such as enkephalinase [EC 3. 4. 24. 11], the enkephalin generating neutral endopeptidase [EC 3. 4. 24. 15], or NRD convertase do not inhibit the Dyn A processing enzyme activity. In contrast, specific inhibitors of angiotensin converting enzyme inhibit the activity. The purified enzyme is able to process a number of neuropeptides at both monobasic and dibasic sites. These characteristics are consistent with a role for the Dyn A processing enzyme in the processing of Dyn A-17 and other neuropeptides in the brain.

• 社団法人 日本生化学会の論文

著者

• Wood David

  Department Of Civil Engineering Glasgow University

• Devi Lakshmi

  Department Of Pharmacology Kaplan Comprehensive Cancer Center And New York University School Of Medi

• Berman Yemiliya

  Department Of Pharmacology Kaplan Comprehensive Cancer Center And New York University School Of Medi

• Veksler Boris

  Department Of Pharmacology Kaplan Comprehensive Cancer Center And New York University School Of Medi

• Ageyeva Lyudmila

  Department Of Pharmacology Kaplan Comprehensive Cancer Center And New York University School Of Medi

• Wood David

  Departments of Pathology Kaplan Comprehensive Cancer Center and New York University School of Medicine

• Veksler Boris

  Departments of Pharmacology Kaplan Comprehensive Cancer Center and New York University School of Medicine

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