C‐terminal amidation of neuropeptides

FEBS Letters - Tập 167 - Trang 160-164 - 1984
Sophie Gomez1, Carlo di Bello2, Lam Than Hung3, Roger Genet3, Jean-Louis Morgat3, Pierre Fromageot3, Paul Cohen1
1Groupe de Neurobiochimie Cellulaire et Moléculaire Université Pierre et Marie Curie, 96 boulevard Raspail, 75006 Paris, France
2Istituto di Chimica Biologica, Università di Padova, 35100 Padova, Italy
3Service de Biochimie, Departement de Biologie, CEN Saclay, 91191 Gif-sur-Yvette, France

Tóm tắt

Biosynthesis of the C‐terminal carboxamide group of peptide hormones was studied using comparatively pGlu‐His‐Pro‐Gly and Glu‐His‐Pro‐Gly‐Lys‐Arg as putative precursors of the tripeptide, thyroliberin (TRH). Rat hypothalamus granules were found to contain an amide group forming activity which converts both peptide substrates into TRH. Comparison of the rate of conversion of the two substrates indicated that the C‐terminal dibasic extension favored a 10‐fold increase in the production of amidated peptide. It is suggested that this type of structure may be present in the putative biosynthetic precursor of TRH and that it may provide a better substrate for the enzyme(s) involved in C‐terminal amidation.

Tài liệu tham khảo

10.1073/pnas.74.3.975 10.1038/278423a0 10.1073/pnas.77.8.4444 10.1038/295299a0 10.1038/298686a0 10.1016/0006-291X(83)91473-0 10.1073/pnas.80.16.5144 10.1016/0014-5793(83)80395-0 10.1016/0006-291X(79)90689-2 10.1016/0014-5793(72)80208-4 10.1111/j.1432-1033.1977.tb11745.x 10.1111/j.1432-1033.1982.tb06916.x 10.1016/0014-5793(83)81065-5 10.1038/301537a0
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FEBS Letters

Tập 167

160-164

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