Isolation and identification of a second diuretic hormone from Tenebrio molitor.
A diuretic hormone (DH) of unusual structure was isolated from extracts of heads of Tenebrio molitor. The hormone is a 47 amino acid peptide, Mr = 5,029.9, with the sequence AGALGESGASLSIVNSLDVLRNRLLLEIARKKAKEGANRNRQILLSL. This peptide increases cyclic AMP production in Malpighian tubules of T. molitor. We recently identified a smaller DH from T. molitor with 37 amino acids; these peptides have only 15 identical amino acids when aligned to maximize similarity to other members of the insect DH family. This family has sequence similarity to the corticotropin-releasing factor superfamily of vertebrate peptides.
Furuya
K
K
Department of Biochemistry, University of Nevada, Reno 89557, USA.
Schegg
K M
KM
Schooley
D A
DA
D000595:Amino Acid Sequence; D000818:Animals; D003346:Corticotropin-Releasing Hormone / Q000737:chemistry; D000242:Cyclic AMP / Q000378:metabolism; D004232:Diuretics / Q000737:chemistry* / Q000494:pharmacology; D006257:Head; D006728:Hormones / Q000737:chemistry* / Q000494:pharmacology; D019476:Insect Proteins / Q000737:chemistry* / Q000494:pharmacology; D008317:Malpighian Tubules / Q000187:drug effects; D008969:Molecular Sequence Data; D005810:Multigene Family; D017386:Sequence Homology, Amino Acid; D013712:Tenebrio / Q000737:chemistry*
D004232:Diuretics; D006728:Hormones; D019476:Insect Proteins; D003346:Corticotropin-Releasing Hormone; D000242:Cyclic AMP