Abstract
Two immunoreactive neurotensin-related peptides generated by the action of endogenous protease(s) on protein substrates during acid extraction of avian tissues have been isolated from extracts of turkey skin and proventriculus. One was identified as the pentadecapeptide, H-Phe-Glu-Arg-Phe-Gln-Gly-Met-Arg-Thy-Arg-Gly-Pro-Tyr-Phe-Leu-OH and the other was its C-terminal octapeptide fragment. Each peptide showed partial homology to the C-terminal, biologically active region of avian neurotensin, and isolated preparations displayed pharmacologic activity at submicromolar concentrations. Synthetic preparations were shown to be indistinguishable from the native peptides during high pressure liquid chromatography (HPLC) and bioassay. Analysis by HPLC indicated that similar peptides could be generated in extracts of proventriculus, pancreas, small intestine, skin, heart, lung, and skeletal muscle. These results, establishing the presence of a neurotensin-related sequence which can be liberated from protein(s) by the action of tissue enzyme(s), suggest that peptide(s) similar to neurotensin may be rapidly formed in order to promote physiologic regulation in multiple tissue(s).
Highlights
Two immunoreactive neurotensin-related peptides Here we reportthatthisgeneration of immunoreactive generated by the action of endogenous protease(s) on neurotensincan occur inextracts of many avian tissues protein substrates during acid extraction of avian tis- includingheart, liver, andskin, where neurotensinisnot sadsiTtuhnehseocdysawC-ppheA-redatropevgvrtpe-iemadnGbreitlent,rieyaianc-llHuP-iohlsruPcoootshmla.-aepoOtT-eelyGnodprlget-fyuirwdP-otehaAomserft-griehad-LxegePetmnrhuCate-ei-cf-OnattieGenHtsr.dldmonEfta-ihanstGeucatlhrohly,kte-hbepMepyieoreeplstnwotki-tgdaiaAines--rg-dfarfoooceiturmdemnsnoedesnqdiusniintenrfnaaictmtaeiscnsiilgadyc.tteohixvfefteiortrarhmcseti.smmIoniaflajaotrduiritdrmykitmeitoyounsnk,vowiarneeraaidonceutditsveperrpmoevipenctneioitdnrmteihtcspheuoelnaumensn,eituns-o cally active region of avian neurotensin, and isolated preparations displayed pharmacologic activity at sub
AnaIysisby HPLC indicated that strated that the levels of immunoreactiveneurotensininsimilar peptides could begenerated in extracts of proventriculus, pancreas, small intestine, skin, heart, lung, and skeletal muscle
Creased more than 100-fold within seconds of extracting gastric tissue in0.1 N HC1 and that thiswas due to the actioonf acid protease(s) on protein substrates [8].The resultsshown in Fig. 1,A-C indicate that thisprocess can occur in extracts of many avian tissues, iist most rapid in extracts of the forestomach
Summary
Two immunoreactive neurotensin-related peptides Here we reportthatthisgeneration of immunoreactive generated by the action of endogenous protease(s) on neurotensincan occur inextracts of many avian tissues protein substrates during acid extraction of avian tis- includingheart, liver, andskin, where neurotensinisnot sadsiTtuhnehseocdysawC-ppheA-redatropevgvrtpe-iemadnGbreitlent,rieyaianc-llHuP-iohlsruPcoootshmla.-aepoOtT-eelyGnodprlget-fyuirwdP-otehaAomserft-griehad-LxegePetmnrhuCate-ei-cf-OnattieGenHtsr.dldmonEfta-ihanstGeucatlhrohly,kte-hbepMepyieoreeplstnwotki-tgdaiaAines--rg-dfarfoooceiturmdemnsnoedesnqdiusniintenrfnaaictmtaeiscnsiilgadyc.tteohixvfefteiortrarhmcseti.smmIoniaflajaotrduiritdrmykitmeitoyounsnk,vowiarneeraaidonceutditsveperrpmoevipenctneioitdnrmteihtcspheuoelnaumensn,eituns-o cally active region of avian neurotensin, and isolated preparations displayed pharmacologic activity at sub-. Synthetic preparations were shown tobe indistinguishable from the native peptides during high pressure liquid chromatography Tissue Dependence of Generation-Previously, we demon- AnaIysisby HPLC indicated that strated that the levels of immunoreactiveneurotensininsimilar peptides could begenerated in extracts of proventriculus, pancreas, small intestine, skin, heart, lung, and skeletal muscle.
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