Nutrient transporter function studied in heterologous expression systems.
Although a large number of plasma cell nutrient transport proteins has been cloned in the last couple of years, much remains to be learned about their structure-function relationships, membrane topology, posttranslational regulation, and bioenergetics of transport. Major progress in the study of the human and animal transporters has come from heterologous expression systems, which offer the benefits of ease of genetic selection and manipulation, short generation time of the organisms in which transporters are expressed, and comparatively high levels of expression of the recombinant proteins. Because our main focus is mammalian peptide transporters, the intestinal peptide transporter, PEPT1, and its renal counterpart, PEPT2, will serve here as models for the analysis of their structure and function when they are heterologously expressed in different cell systems.
Daniel
H
H
Institute of Nutritional Sciences, Technical University of Munich, Hochfeldweg 2, 85350 Freising-Weihenstephan, Germany. daniel@weihenstephan.de
D000818:Animals; D002352:Carrier Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D015870:Gene Expression / Q000502:physiology; D006801:Humans; D007413:Intestinal Mucosa / Q000378:metabolism*; D007668:Kidney / Q000378:metabolism; D000074011:Peptide Transporter 1; D013329:Structure-Activity Relationship; D027981:Symporters
D002352:Carrier Proteins; D000074011:Peptide Transporter 1; C082186:SLC15A1 protein, human; D027981:Symporters; C093694:hydrogen-coupled oligopeptide transporter PepT2