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Locustatachykinin I and II, two novel insect neuropeptides with homology to peptides of the vertebrate tachykinin family
Author(s) -
Schoofs Liliane,
Holman G.Mark,
Hayes Timothy K.,
Nachman Ronald J.,
De Loof Arnold
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)80601-e
Subject(s) - vertebrate , neuropeptide , biology , locust , insect , homology (biology) , peptide , tachykinin receptor , substance p , peptide sequence , biochemistry , amino acid , receptor , botany , gene
Two myotropic peptides termed locustatachykinin I (Gly‐Pro‐Ser‐Gly‐Phe‐Tyr‐Gly‐Val‐Arg‐NH 2 ) and locustatachykinin II (Ala‐Pro‐Leu‐Ser‐Gly‐Phe‐Tyr‐Gly‐Val‐Arg‐NH 2 ) were isolated from brain‐corpora cardiaca‐corpora allata‐suboesophageal ganglion extracts of the locust, Locusta migratoria . Both peptides exhibit sequence homologies with the vertebrate tachykinins. Sequence homology is greater with the fish and amphibian tachykinins (up to 45%) than with the mammalian tachykinins. In addition, the intestinal myotropic activity of the locustatachykinins is analogous to that of vertebrate tachykinins. The peptides discovered in this study may just be the first in a whole series of substances from arthropod species to be identified as tachykinin family peptides. Moreover, both chemical and biological similarities of vertebrate and insect tachykinins substantiate the evidence for a long evolutionary history of the tachykinin peptide family.