Crustacean peptide and peptide-like pheromones and kairomones.
Crustacean peptide pheromones, kairomones, and substituted amino sugar kairomones are reviewed from a historical perspective. These crustacean information molecules are secondary functions of structural polymers. They are partial hydrolysis products, generated usually by the action of trypsin-like enzymes on proteins, and glycosidase enzymes on glycoproteins and proteoglycans. Structure-function studies based upon synthetic mimics of peptide information molecules show neutral amino acids with a basic carboxyl terminal are active in modifying physiological and or behavioral responses. Behaviorally active substituted amino sugar mimics are disaccharide hydrolysis products of heparin and chondroitin sulfate. Similar molecules are also used as information molecules by a variety of other marine organisms indicating they are a common biological theme.
Rittschof
Dan
D
Duke University Marine Laboratory, Biology Department, Nicholas School of the Environment, Earth and Ocean Sciences, 135 Duke Marine Laboratory Road, Beaufort, NC 28516, USA. ritt@duke.edu
Cohen
Jonathan H
JH
D000818:Animals; D001920:Bradykinin / Q000737:chemistry; D002240:Carbohydrate Sequence; D002241:Carbohydrates / Q000737:chemistry; D002809:Chondroitin Sulfates / Q000737:chemistry; D003445:Crustacea; D006026:Glycoside Hydrolases / Q000737:chemistry; D006493:Heparin / Q000737:chemistry; D006868:Hydrolysis; D008956:Models, Chemical; D008969:Molecular Sequence Data; D009479:Neuropeptides / Q000494:pharmacology*; D010455:Peptides / Q000737:chemistry*; D010675:Pheromones / Q000737:chemistry*; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry; D013329:Structure-Activity Relationship; D014357:Trypsin / Q000737:chemistry
D002241:Carbohydrates; D009479:Neuropeptides; D010455:Peptides; D010675:Pheromones; D011506:Proteins; C058620:crustacean cardioactive peptide; D006493:Heparin; D002809:Chondroitin Sulfates; D006026:Glycoside Hydrolases; D014357:Trypsin; D001920:Bradykinin