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NPY in invertebrates: molecular answers to altered functions during evolution.
de Jong-Brink, M; ter Maat, A; Tensen, C P.
Affiliation
  • de Jong-Brink M; Vrije Universiteit, Faculty of Biology, Department of Developmental Neurobiology, De Boelelaan 1087, 1081 HV, Amsterdam, The Netherlands. mdejong@bio.vu.nl
Peptides ; 22(3): 309-15, 2001 Mar.
Article in En | MEDLINE | ID: mdl-11287084
As in Lymnaea stagnalis NPY plays a key role in regulating energy flows but has no effect on food intake, two important questions arise: 1) How is the amount of food consumed related to energy storage? 2) Can we give a molecular explanation for this alteration in function of NPY during evolution? Recent data have shown that also in Lymnaea a leptin-like factor is produced by glycogen storing cells which inhibits food intake, a Lymnaea storage feedback factor (LySFF). So, food consumption seems in balance with the amount of energy stored in this animal. We suppose that NPY neurons in Lymnaea have receptors for LySFF so that their activity in regulating energy homeostasis reflects the amount of stored energy. By comparing the molecular structure of NPYs in invertebrates it became clear that only molluscan and arthropod NPY are synthesized from a prohormone similar to vertebrate NPYs and should be considered as real invertebrate homologs of NPY. Based on pharmacological data we suppose that the identified Lymnaea NPY receptor is a Y1 subtype. This might explain that LyNPY has no effect on food intake in Lymnaea as this function of NPY in mammals is regulated through the Y5 subtype receptor.
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Collection: 01-internacional Database: MEDLINE Main subject: Neuropeptide Y / Evolution, Molecular Type of study: Prognostic_studies Limits: Animals Language: En Journal: Peptides Year: 2001 Document type: Article Affiliation country: Netherlands Country of publication: United States
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Collection: 01-internacional Database: MEDLINE Main subject: Neuropeptide Y / Evolution, Molecular Type of study: Prognostic_studies Limits: Animals Language: En Journal: Peptides Year: 2001 Document type: Article Affiliation country: Netherlands Country of publication: United States