QUICK SEARCH:   [advanced] Author: Keyword(s):
Home     Help     Feedback     Subscriptions     Archive     Search     Table of Contents

First published online November 2, 2007
Journal of Experimental Biology 210, 3883-3896 (2007)
Published by The Company of Biologists 2007
doi: 10.1242/jeb.007898

This Article Figures Only Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Rønnestad, I. Articles by Cancela, M. L. Search for Related Content PubMed PubMed Citation Articles by Rønnestad, I. Articles by Cancela, M. L.

Oligopeptide transporter PepT1 in Atlantic cod (Gadus morhua L.): cloning, tissue expression and comparative aspects

Ivar Rønnestad^1,*, Paulo J. Gavaia², Carla S. B. Viegas², Tiziano Verri³, Alessandro Romano³, Tom Ole Nilsen¹, Ann-Elise O. Jordal¹, Yuko Kamisaka¹ and M. Leonor Cancela²

¹ University of Bergen, Department of Biology, N-5020 Bergen, Norway
² University of Algarve –CCMAR, Campus de Gambelas, 8005-139 Faro, Portugal
³ University of Salento (formerly University of Lecce), Department of Biological and Environmental Sciences and Technologies, I-73100 Lecce, Italy

^* Author for correspondence (e-mail: ivar.ronnestad{at}bio.uib.no)

Accepted 29 August 2007

A novel full-length cDNA that encodes for the Atlantic cod (Gadus morhua L.) PepT1-type oligopeptide transporter has been cloned. This cDNA (named codPepT1) was 2838 bp long, with an open reading frame of 2190 bp encoding a putative protein of 729 amino acids. Comparison of the predicted Atlantic cod PepT1 protein with zebrafish, bird and mammalian orthologs allowed detection of many structural features that are highly conserved among all the vertebrate proteins analysed, including (1) a larger than expected area of hydrophobic amino acids in close proximity to the N terminus; (2) a single highly conserved cAMP/cGMP-dependent protein kinase phosphorylation motif; (3) a large N-glycosylation-rich region within the large extracellular loop; and (4) a conserved and previously undescribed stretch of 8–12 amino acid residues within the large extracellular loop. Expression analysis at the mRNA level indicated that Atlantic cod PepT1 is mainly expressed at intestinal level, but that it is also present in kidney and spleen. Analysis of its regional distribution along the intestinal tract of the fish revealed that PepT1 is ubiquitously expressed in all segments beyond the stomach, including the pyloric caeca, and through the whole midgut. Only in the last segment, which included the hindgut, was there a lower expression. Atlantic cod PepT1, the second teleost fish PepT1-type transporter documented to date, will contribute to the elucidation of the evolutionary and functional relationships among vertebrate peptide transporters. Moreover, it can represent a useful tool for the study of gut functional regionalization, as well as a marker for the analysis of temporal and spatial expression during ontogeny.

Key words: oligopeptide transporter PepT1, comparative sequence analysis, tissue expression, peptide, teleost

This article has been cited by other articles:

				E. R. Gilbert, E. A. Wong, and K. E. Webb Jr. BOARD-INVITED REVIEW: Peptide absorption and utilization: Implications for animal nutrition and health J Anim Sci, September 1, 2008; 86(9): 2135 - 2155. [Abstract] [Full Text] [PDF]