Document Detail


L-proline transport by purified cell types of lobster hepatopancreas.
MedLine Citation:
PMID:  16823835     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The hepatopancreas of the American lobster, Homarus americanus, has four epithelial cell types that are anatomically distinguishable and can be separated for in vitro investigation of their individual biological roles in the intact organ using centrifugal elutriation. Previous studies employing this separation method have produced hepatopancreatic cell suspensions that have been used to examine the nature of copper transport, 2 Na+/1 H+ exchange, and D-glucose absorption by each cell type in isolation from the other cells comprising the tubular epithelium. The present investigation used this method to study amino acid transport by E-, F-, R-, and B-cells of the lobster hepatopancreas in order to characterize the absorption processes for protein digestion products by this organ and to identify which cell type was most likely the responsible agent for net transcellular transfer of these organic molecules from lumen to blood. Results indicated that heptopancreatic E- and F-cell types were the only cells exhibiting Na+-dependent 3H-L-proline transport. Further examination of 3H-L-proline influx by F-cell suspensions indicated that this cell type possessed plasma membrane Na+-dependent IMINO-like and B0-like transport mechanisms and Na+-independent L-like transport mechanisms. Using selective inhibitors of these separate transport systems (e.g., L-pipecolate, L-alanine, and L-leucine), the IMINO-like transporter appeared to predominate in L-proline influx into F-cells, while lesser amounts of amino acid transport took place by the B0-like and L-like systems. The results of this study suggest that the hepatopancreatic F-cell is the epithelial cell type responsible for the bulk of amino acid absorption by this organ and that the IMINO-like transporter is responsible for most of the L-proline transfer through this agent. It is further suggested that as digestion and absorption proceeds in the hepatopancreas and concentrations of luminal amino acids and sodium fall, Na+-dependent transport systems, like the IMINO-like and B0-like, increase their binding affinities for their substrates to maximize nutrient transfer across the epithelium.
Authors:
L Fiandra; P K Mandal; B Giordana; G A Ahearn
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, Non-P.H.S.    
Journal Detail:
Title:  Journal of experimental zoology. Part A, Comparative experimental biology     Volume:  305     ISSN:  1548-8969     ISO Abbreviation:  J. Exp. Zoolog. Part A Comp. Exp. Biol.     Publication Date:  2006 Oct 
Date Detail:
Created Date:  2006-09-25     Completed Date:  2006-10-31     Revised Date:  2009-10-05    
Medline Journal Info:
Nlm Unique ID:  101168223     Medline TA:  J Exp Zool A Comp Exp Biol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  851-61     Citation Subset:  IM    
Copyright Information:
2006 Wiley-Liss, Inc.
Affiliation:
Department of Biology, University of Milan, Milan 20133, Italy.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Transport Systems, Neutral / metabolism
Animals
Cell Separation
Epithelial Cells / cytology,  metabolism
Hepatopancreas / cytology*,  metabolism
Ion Transport*
Nephropidae / cytology,  metabolism*
Proline / metabolism*
Sodium / metabolism
Sodium-Hydrogen Antiporter / metabolism
Tritium / diagnostic use
Chemical
Reg. No./Substance:
0/Amino Acid Transport Systems, Neutral; 0/Sodium-Hydrogen Antiporter; 10028-17-8/Tritium; 147-85-3/Proline; 7440-23-5/Sodium

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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