Identification of the protein responsible for hepatic system N amino acid transport activity
In the liver, glutamine utilization may be limited by the rate of transport across the plasma membrane by the System N carrier. System N-mediated transport activity has been solubilized from rat liver plasma membrane, partially purified, and then reconstituted into proteoliposomes. To identify the S...
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| Veröffentlicht in: | The Journal of biological chemistry 1992-02, Vol.267 (4), p.2370-2374 |
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| container_issue | 4 |
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| container_title | The Journal of biological chemistry |
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| creator | Tamarappoo, B K Handlogten, M E Laine, R O Serrano, M A Dugan, J Kilberg, M S |
| description | In the liver, glutamine utilization may be limited by the rate of transport across the plasma membrane by the System N carrier. System N-mediated transport activity has been solubilized from rat liver plasma membrane, partially purified, and then reconstituted into proteoliposomes. To identify the System N carrier protein, monoclonal antibodies were generated against the protein fraction enriched for System N activity. Two antibodies , 3E1-2 and 1E7-3, inhibited System N activity in hepatocytes. These antibodies also immunoprecipitated System N activity from a mixture of solubilized proteins and were specific for antigen recognition in that neither immunoprecipitated System A activity. The antibody recognized a single protein of molecular size 100 kDa by immunoblot analysis. Recognition of this protein by the antibody increased in parallel with the enrichment of System N activity in solubilized membrane fractions. These data suggest that a 100-kDa plasma membrane protein mediates System N transport activity in rat hepatocytes. |
| doi_str_mv | 10.1016/S0021-9258(18)45888-7 |
| format | Article |
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System N-mediated transport activity has been solubilized from rat liver plasma membrane, partially purified, and then reconstituted into proteoliposomes. To identify the System N carrier protein, monoclonal antibodies were generated against the protein fraction enriched for System N activity. Two antibodies , 3E1-2 and 1E7-3, inhibited System N activity in hepatocytes. These antibodies also immunoprecipitated System N activity from a mixture of solubilized proteins and were specific for antigen recognition in that neither immunoprecipitated System A activity. The antibody recognized a single protein of molecular size 100 kDa by immunoblot analysis. Recognition of this protein by the antibody increased in parallel with the enrichment of System N activity in solubilized membrane fractions. These data suggest that a 100-kDa plasma membrane protein mediates System N transport activity in rat hepatocytes.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(18)45888-7</identifier><identifier>PMID: 1733938</identifier><identifier>CODEN: JBCHA3</identifier><language>eng</language><publisher>Bethesda, MD: Elsevier Inc</publisher><subject>amino acids ; Amino Acids - metabolism ; Analytical, structural and metabolic biochemistry ; Animals ; Antibodies, Monoclonal ; Antibody Specificity ; Biological and medical sciences ; Biological Transport ; Blotting, Western ; Carrier Proteins - analysis ; Carrier Proteins - immunology ; Cell Membrane - metabolism ; Enzyme-Linked Immunosorbent Assay ; Enzymes and enzyme inhibitors ; Fundamental and applied biological sciences. 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System N-mediated transport activity has been solubilized from rat liver plasma membrane, partially purified, and then reconstituted into proteoliposomes. To identify the System N carrier protein, monoclonal antibodies were generated against the protein fraction enriched for System N activity. Two antibodies , 3E1-2 and 1E7-3, inhibited System N activity in hepatocytes. These antibodies also immunoprecipitated System N activity from a mixture of solubilized proteins and were specific for antigen recognition in that neither immunoprecipitated System A activity. The antibody recognized a single protein of molecular size 100 kDa by immunoblot analysis. Recognition of this protein by the antibody increased in parallel with the enrichment of System N activity in solubilized membrane fractions. These data suggest that a 100-kDa plasma membrane protein mediates System N transport activity in rat hepatocytes.</description><subject>amino acids</subject><subject>Amino Acids - metabolism</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Antibodies, Monoclonal</subject><subject>Antibody Specificity</subject><subject>Biological and medical sciences</subject><subject>Biological Transport</subject><subject>Blotting, Western</subject><subject>Carrier Proteins - analysis</subject><subject>Carrier Proteins - immunology</subject><subject>Cell Membrane - metabolism</subject><subject>Enzyme-Linked Immunosorbent Assay</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Fundamental and applied biological sciences. 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| ispartof | The Journal of biological chemistry, 1992-02, Vol.267 (4), p.2370-2374 |
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| language | eng |
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| subjects | amino acids Amino Acids - metabolism Analytical, structural and metabolic biochemistry Animals Antibodies, Monoclonal Antibody Specificity Biological and medical sciences Biological Transport Blotting, Western Carrier Proteins - analysis Carrier Proteins - immunology Cell Membrane - metabolism Enzyme-Linked Immunosorbent Assay Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Liver - chemistry Liver - metabolism membrane proteins Miscellaneous Precipitin Tests Rats |
| title | Identification of the protein responsible for hepatic system N amino acid transport activity |
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