Complete amino acid sequence of porcine adrenomedullin and cloning of cDNA encoding its precursor
Open Access
- 7 February 1994
- journal article
- Published by Wiley in FEBS Letters
- Vol. 338 (3) , 306-310
- https://doi.org/10.1016/0014-5793(94)80289-0
Abstract
Porcine adrenomedullin was isolated from adrenal medulla extract and its amino acid sequence was determined. The peptide is identical to human adrenomedullin with a single replacement of Gly for Asn at position 40. The cDNA clone encoding the porcine adrenomedullin precursor was isolated and sequenced. The precursor for adrenomedullin (preproadrenomedullin) is 188 amino adds in length, including the adrenomedullin sequence, followed by a glycine (the amide donor). In addition to adrenomedullin, proadrenomedullin (proAM) contains a candidate for a unique 20‐residue peptide, proAM‐N20, whose carboxy‐terminus may be amidated. By RNA blot analysis, porcine adrenomedullin mRNA was found to be highly expressed in several porcine tissues including lung and kidney as well as adrenal medulla.Keywords
This publication has 13 references indexed in Scilit:
- Adrenomedullin: A Novel Hypotensive Peptide Isolated from Human PheochromocytomaBiochemical and Biophysical Research Communications, 1993
- Cloning and sequence analysis of a cDNA encoding a precursor for rat C‐type natriuretic peptide (CNP)FEBS Letters, 1990
- Regional distribution of immunoreactive endothelin in porcine tissue: Abundance in inner medulla of kidneyBiochemical and Biophysical Research Communications, 1989
- Constitutive and Regulated Secretion of ProteinsAnnual Review of Cell Biology, 1987
- Calcitonin gene-related peptide is a potent vasodilatorNature, 1985
- Purification and complete amino acid sequence of α-human atrial natriuretic polypeptide (α-hANP)Biochemical and Biophysical Research Communications, 1984
- A simple and very efficient method for generating cDNA librariesGene, 1983
- Patterns of Amino Acids near Signal‐Sequence Cleavage SitesEuropean Journal of Biochemistry, 1983
- Strategies for the biosynthesis of bioactive peptidesTrends in Neurosciences, 1983
- Purification of Biologically Active Globin Messenger RNA by Chromatography on Oligothymidylic acid-CelluloseProceedings of the National Academy of Sciences, 1972