Post-translational processing of preprotachykinins. Isolation of protachykinin-(1-37)-peptide from human adrenal-medullary phaeochromocytoma tissue.
The biosynthetic precursors of the mammalian tachykinins, alpha-, beta-and gamma-preprotachykinins, contain a common N-terminal region of 74 amino acids. A polyclonal antiserum was raised against a synthetic peptide representing N-tyrosylated beta-preprotachykinin-(48-56)-peptide as predicted from the nucleotide sequence of cloned DNA complementary to human beta-preprotachykinin mRNA. By using this antiserum in radioimmunoassay, a single immunoreactive peptide was identified in an extract of a human pheochromocytoma that produced substance P and neurokinin A. Partial microsequencing and determination of the amino acid composition of the peptide indicated identity with preprotachykinin-(20-56)-peptide. Thus the data demonstrate that the Ala19-Glu20 bond in preprotachykinin is the site of cleavage of the signal peptide.
Clinical Research Group for Gastrointestinal Endocrinology of the Max-Planck-Society, University of Göttingen, Federal Republic of Germany.
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R
Kage
L
L
Thim
W
W
Creutzfeldt
J M
JM
Conlon
D000310:Adrenal Gland Neoplasms / Q000378:metabolism*; D000328:Adult; D000595:Amino Acid Sequence; D002851:Chromatography, High Pressure Liquid; D005260:Female; D006801:Humans; D008969:Molecular Sequence Data; D009479:Neuropeptides / Q000378:metabolism*; D010446:Peptide Fragments / Q000302:isolation & purification*; D010673:Pheochromocytoma / Q000378:metabolism*; D014176:Protein Biosynthesis; D011498:Protein Precursors / Q000378:metabolism*; D011863:Radioimmunoassay; D015320:Tachykinins
D009479:Neuropeptides; D010446:Peptide Fragments; D011498:Protein Precursors; D015320:Tachykinins; C044206:preprotachykinin