Characterization of the plasma lipoproteins of the genetically obese hyperlipoproteinemic Zucker fatty rat
The plasma lipoproteins of the Zucker fatty rat were characterized with respect to lipid and apoprotein composition, and results were compared with those obtained from lean controls. Information on apoproteins was obtained from gel filtration experiments and electrophoresis on polyacrylamide gels. V...
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| Format: | Article |
| Language: | English |
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Elsevier
1974-09-01
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| Series: | Journal of Lipid Research |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S0022227520367651 |
| _version_ | 1818942554029162496 |
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| author | Gustav Schonfeld Cynthia Felski Mary Ann Howald |
| author_facet | Gustav Schonfeld Cynthia Felski Mary Ann Howald |
| author_sort | Gustav Schonfeld |
| collection | DOAJ |
| description | The plasma lipoproteins of the Zucker fatty rat were characterized with respect to lipid and apoprotein composition, and results were compared with those obtained from lean controls. Information on apoproteins was obtained from gel filtration experiments and electrophoresis on polyacrylamide gels. Very low density lipoproteins (VLDL) were increased severalfold in fatties, and 78% of their mass was triglycerides compared with 60% in the controls. Low density (LDL) and high density (HDL) lipoproteins were increased by a factor of 2, although their compositions were similar to those of the controls. Levels of apoVLDL, apoLDL, and apoHDL were five, two, and two times higher, respectively, in the fatties, and the two most rapidly moving subunit peptides on polyacrylamide gels were disproportionately elevated in the apoproteins. The slower of these two bands was present in relatively greater amounts than the faster one in fatties. If the slower peptide is an activator of lipoprotein lipase, analogous to the comparable subunit peptides of human apolipoproteins, plasmas of fatties could contain up to 10 times more lipase activator activity than control plasma. This finding, and the fact that adipose tissue lipoprotein lipase activity of fatties was about 150% of controls, suggests that fatties have increased capacities for VLDL catabolism. We have previously shown that hepatic VLDL secretory rates are higher than normal in these animals. The increased capacity for catabolism may be a response to the altered secretory rates. |
| first_indexed | 2024-12-20T07:13:16Z |
| format | Article |
| id | doaj.art-11c8fd9ca860433992b055e0582256e9 |
| institution | Directory Open Access Journal |
| issn | 0022-2275 |
| language | English |
| last_indexed | 2024-12-20T07:13:16Z |
| publishDate | 1974-09-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Journal of Lipid Research |
| spelling | doaj.art-11c8fd9ca860433992b055e0582256e92022-12-21T19:48:51ZengElsevierJournal of Lipid Research0022-22751974-09-01155457464Characterization of the plasma lipoproteins of the genetically obese hyperlipoproteinemic Zucker fatty ratGustav Schonfeld0Cynthia Felski1Mary Ann Howald2Lipid Research Center, Departments of Preventive Medicine and Medicine, Washington University School of Medicine, St. Louis, Missouri 63110Lipid Research Center, Departments of Preventive Medicine and Medicine, Washington University School of Medicine, St. Louis, Missouri 63110Lipid Research Center, Departments of Preventive Medicine and Medicine, Washington University School of Medicine, St. Louis, Missouri 63110The plasma lipoproteins of the Zucker fatty rat were characterized with respect to lipid and apoprotein composition, and results were compared with those obtained from lean controls. Information on apoproteins was obtained from gel filtration experiments and electrophoresis on polyacrylamide gels. Very low density lipoproteins (VLDL) were increased severalfold in fatties, and 78% of their mass was triglycerides compared with 60% in the controls. Low density (LDL) and high density (HDL) lipoproteins were increased by a factor of 2, although their compositions were similar to those of the controls. Levels of apoVLDL, apoLDL, and apoHDL were five, two, and two times higher, respectively, in the fatties, and the two most rapidly moving subunit peptides on polyacrylamide gels were disproportionately elevated in the apoproteins. The slower of these two bands was present in relatively greater amounts than the faster one in fatties. If the slower peptide is an activator of lipoprotein lipase, analogous to the comparable subunit peptides of human apolipoproteins, plasmas of fatties could contain up to 10 times more lipase activator activity than control plasma. This finding, and the fact that adipose tissue lipoprotein lipase activity of fatties was about 150% of controls, suggests that fatties have increased capacities for VLDL catabolism. We have previously shown that hepatic VLDL secretory rates are higher than normal in these animals. The increased capacity for catabolism may be a response to the altered secretory rates.http://www.sciencedirect.com/science/article/pii/S0022227520367651apolipoproteinslipoprotein lipase |
| spellingShingle | Gustav Schonfeld Cynthia Felski Mary Ann Howald Characterization of the plasma lipoproteins of the genetically obese hyperlipoproteinemic Zucker fatty rat Journal of Lipid Research apolipoproteins lipoprotein lipase |
| title | Characterization of the plasma lipoproteins of the genetically obese hyperlipoproteinemic Zucker fatty rat |
| title_full | Characterization of the plasma lipoproteins of the genetically obese hyperlipoproteinemic Zucker fatty rat |
| title_fullStr | Characterization of the plasma lipoproteins of the genetically obese hyperlipoproteinemic Zucker fatty rat |
| title_full_unstemmed | Characterization of the plasma lipoproteins of the genetically obese hyperlipoproteinemic Zucker fatty rat |
| title_short | Characterization of the plasma lipoproteins of the genetically obese hyperlipoproteinemic Zucker fatty rat |
| title_sort | characterization of the plasma lipoproteins of the genetically obese hyperlipoproteinemic zucker fatty rat |
| topic | apolipoproteins lipoprotein lipase |
| url | http://www.sciencedirect.com/science/article/pii/S0022227520367651 |
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