| Evidence for conversion of N-Tyr-MIF-1 into MIF-1 by a specific brain aminopeptidase. | |
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MedLine Citation:
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PMID: 20488055 Owner: NLM Status: In-Data-Review |
Abstract/OtherAbstract:
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N-Tyr-MIF-1 (Tyr-Pro-Leu-Gly.NH(2)), an immunoreactive neuropeptide exhibiting saturable high affinity binding in rat brain was found to be converted into MIF-1 (Pro-Leu-Gly.NH(2)) by a specific brain aminopeptidase present in rat brain homogenates or cytosol, but with low activity associated with synaptosomal plasma membranes and microsomes. Conversion occurred at a rate of 16 ?mol per g w/wt per h and was unaffected by puromycin but inhibited by bestatin (I(50), 5 x 10(?5) M). Aminopeptidases purified from cytosolic fractions of rat brain (arylamidase), mouse brain (Mn(2+)-activated aminopeptidase) or porcine kidney (leucine aminopeptidase) were inactive towards N-Tyr-MIF-1 but degraded MIF-1 with release of Leu-Gly.NH(2) as detected by RP-HPLC procedures. Morphiceptin (Tyr-Pro-Phe-Pro.NH(2)), a ? opioid agonist, also acted as a substrate for the N-Tyr-MIF-1 converting enzyme with cleavage of the Tyr-Pro bond. These tetrapeptides, but not MIF-1 or its N-blocked analogs, were degraded in vitro by a metalloendopeptidase purified from kidney membranes. Since dipeptide products were not detected for crude extracts, a significant role for brain metalloendopeptidase on turnover can be excluded. Thus the results point to the presence of a specific (X-Pro-degrading) aminopeptidase in brain cytosol as an enzyme responsible for converting N-Tyr-MIF-1 and inactivating morphiceptin. |
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Authors:
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N Marks; M J Berg; A J Kastin; D H Coy |
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Publication Detail:
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Type: Journal Article |
Journal Detail:
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Title: Neurochemistry international Volume: 6 ISSN: 0197-0186 ISO Abbreviation: Neurochem. Int. Publication Date: 1984 |
Date Detail:
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Created Date: 2010-05-21 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 8006959 Medline TA: Neurochem Int Country: England |
Other Details:
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Languages: eng Pagination: 347-53 Citation Subset: - |
Affiliation:
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Center for Neurochemistry, Nathan S. Kline Institute for Psychiatric Research, Ward's Island, NY 10035, U.S.A. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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