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Molecular, mass spectral, and physiological characterization of a novel C‐type allatostatin peptide, SYWKQCAFNAVSCFamide, in crustaceans
Author(s) -
Ackerman Rachel J.,
Wiwatpanit Teerawat,
Stevens Jake S.,
Dickinson Patsy S.,
Stemmler Elizabeth A.,
Christie Andrew E.
Publication year - 2009
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.23.1_supplement.881.3
Subject(s) - crustacean , biology , homarus , juvenile hormone , expressed sequence tag , peptide , in silico , zoology , evolutionary biology , insect , ecology , genetics , biochemistry , gene , complementary dna
The allatostatins comprise three structurally distinct families of neuropeptides classified as A‐, B‐, and C‐type. Known to play a role in the regulation of juvenile hormone production by the insect corpora allata, members of the A‐ and B‐type allatostatin family are found in a wide variety of arthropods; however, members of the C‐type family have been only identified in insects. C‐type allatostatins typically possess a ‐PISCF motif. Here, we report on the characterization of the first C‐type allatostatin in crustaceans, SYWKQCAFNAVSCFamide, with bridged cysteines. Using in silico mining of extant express sequence tags (ESTs) from the lobster, Homarus americanus , transcripts encoding the prepro‐hormone sequence were used to predict the mature peptide. This peptide was subsequently detected in crustacean tissue samples from species representing five different decapod infraorders using MALDI‐FTMS, suggesting broad sequence conservation. In H. americanus , a synthetic form of the peptide has been tested and found to be bioactive. Support from: MDIBL; NSF (IBN 01140, MRI‐0116416); NIH P20 RR‐016463, NCRR; HHMI Undergrad Sci Prog.