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 e...
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Veröffentlicht in: | Peptides (New York, N.Y. : 1980) N.Y. : 1980), 2004-09, Vol.25 (9), p.1503-1516 |
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description | 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. |
doi_str_mv | 10.1016/j.peptides.2003.10.024 |
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Similar molecules are also used as information molecules by a variety of other marine organisms indicating they are a common biological theme.</description><subject>Animals</subject><subject>Behavior</subject><subject>Bradykinin - chemistry</subject><subject>Carbohydrate Sequence</subject><subject>Carbohydrates - chemistry</subject><subject>Chondroitin Sulfates - chemistry</subject><subject>Crustacea</subject><subject>Crustacean</subject><subject>Glycoproteins</subject><subject>Glycoside Hydrolases - chemistry</subject><subject>Heparin - chemistry</subject><subject>Hydrolysis</subject><subject>Information molecules</subject><subject>Kairomone</subject><subject>Models, Chemical</subject><subject>Molecular Sequence Data</subject><subject>Neuropeptides - pharmacology</subject><subject>Peptides</subject><subject>Peptides - chemistry</subject><subject>Pheromone</subject><subject>Pheromones - chemistry</subject><subject>Protein Structure, Tertiary</subject><subject>Proteins - chemistry</subject><subject>Proteoglycans</subject><subject>Structure-Activity Relationship</subject><subject>Substituted amino sugars</subject><subject>Trypsin - chemistry</subject><issn>0196-9781</issn><issn>1873-5169</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkMlOwzAQhi0EoqXwClVP3BLsOF5yQAJVbFIlLr1btjMWbrNhJ0i8PSlNxZHTbP_8o_kQWhKcEkz43S7toOt9CTHNMKZjM8VZfobmRAqaMMKLczTHpOBJISSZoasYdxjjPC_kJZoRRkXOGZmj-3UYYq8t6GY1Oa50U57ypPJ7WHUfENq6bSD-zvbaT-U1unC6inAzxQXaPj9t16_J5v3lbf24SSzleZ9klDvHhSBSS-NIDtRxhrXT2IIxlkGppXBZAZwYg7mmmaUyZ8aSkhlh6QLdHm270H4OEHtV-2ihqnQD7RAV51JKwopRyI9CG9oYAzjVBV_r8K0IVgduaqdO3NSB26E_chsXl9OFwdRQ_q1NoEbBw1EA45tfHoKK1kNjofQBbK_K1v934wd_PINu</recordid><startdate>20040901</startdate><enddate>20040901</enddate><creator>Rittschof, Dan</creator><creator>Cohen, Jonathan H.</creator><general>Elsevier Inc</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>20040901</creationdate><title>Crustacean peptide and peptide-like pheromones and kairomones</title><author>Rittschof, Dan ; Cohen, Jonathan H.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c364t-236ff67718a8bf14e3f650afa0cebbc5eda87f29e61bb06a32c3845bc1d5b7c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Animals</topic><topic>Behavior</topic><topic>Bradykinin - chemistry</topic><topic>Carbohydrate Sequence</topic><topic>Carbohydrates - chemistry</topic><topic>Chondroitin Sulfates - chemistry</topic><topic>Crustacea</topic><topic>Crustacean</topic><topic>Glycoproteins</topic><topic>Glycoside Hydrolases - chemistry</topic><topic>Heparin - chemistry</topic><topic>Hydrolysis</topic><topic>Information molecules</topic><topic>Kairomone</topic><topic>Models, Chemical</topic><topic>Molecular Sequence Data</topic><topic>Neuropeptides - pharmacology</topic><topic>Peptides</topic><topic>Peptides - chemistry</topic><topic>Pheromone</topic><topic>Pheromones - chemistry</topic><topic>Protein Structure, Tertiary</topic><topic>Proteins - chemistry</topic><topic>Proteoglycans</topic><topic>Structure-Activity Relationship</topic><topic>Substituted amino sugars</topic><topic>Trypsin - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Rittschof, Dan</creatorcontrib><creatorcontrib>Cohen, Jonathan H.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Peptides (New York, N.Y. : 1980)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Rittschof, Dan</au><au>Cohen, Jonathan H.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Crustacean peptide and peptide-like pheromones and kairomones</atitle><jtitle>Peptides (New York, N.Y. : 1980)</jtitle><addtitle>Peptides</addtitle><date>2004-09-01</date><risdate>2004</risdate><volume>25</volume><issue>9</issue><spage>1503</spage><epage>1516</epage><pages>1503-1516</pages><issn>0196-9781</issn><eissn>1873-5169</eissn><abstract>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.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>15374651</pmid><doi>10.1016/j.peptides.2003.10.024</doi><tpages>14</tpages></addata></record> |
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subjects | Animals Behavior Bradykinin - chemistry Carbohydrate Sequence Carbohydrates - chemistry Chondroitin Sulfates - chemistry Crustacea Crustacean Glycoproteins Glycoside Hydrolases - chemistry Heparin - chemistry Hydrolysis Information molecules Kairomone Models, Chemical Molecular Sequence Data Neuropeptides - pharmacology Peptides Peptides - chemistry Pheromone Pheromones - chemistry Protein Structure, Tertiary Proteins - chemistry Proteoglycans Structure-Activity Relationship Substituted amino sugars Trypsin - chemistry |
title | Crustacean peptide and peptide-like pheromones and kairomones |
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