Sökning: onr:"swepub:oai:lup.lub.lu.se:d5041bb6-8657-412a-9321-774ac2cb97b0" > Binding, interioriz...
Fältnamn | Indikatorer | Metadata |
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000 | 04145naa a2200313 4500 | |
001 | oai:lup.lub.lu.se:d5041bb6-8657-412a-9321-774ac2cb97b0 | |
003 | SwePub | |
008 | 190524s1977 | |||||||||||000 ||eng| | |
024 | 7 | a https://lup.lub.lu.se/record/d5041bb6-8657-412a-9321-774ac2cb97b02 URI |
024 | 7 | a https://doi.org/10.1042/bj16804832 DOI |
040 | a (SwePub)lu | |
041 | a engb eng | |
042 | 9 SwePub | |
072 | 7 | a art2 swepub-publicationtype |
072 | 7 | a ref2 swepub-contenttype |
100 | 1 | a Florén, Claes-Henriku Lund University,Lunds universitet,Medicin, Lund,Sektion II,Institutionen för kliniska vetenskaper, Lund,Medicinska fakulteten,Gastro,Forskargrupper vid Lunds universitet,Medicine, Lund,Section II,Department of Clinical Sciences, Lund,Faculty of Medicine,Lund University Research Groups4 aut0 (Swepub:lu)med-cfl |
245 | 1 0 | a Binding, interiorization and degradation of cholesteryl ester labelled chylomicron remnant particles by rat hepatocyte monolayers |
264 | 1 | b Portland Press Ltd.c 1977 |
300 | a 11 s. | |
520 | a 1. The cholesteryl ester of isolated chylomicron-remnant particles was efficiently degraded by hepatocyte monolayers. The degradation was sensitive to metabolic inhibitors. 2. With increasing amounts of remnant cholesteryl ester the rate of uptake approached saturation and conformed to a linear double-reciprocal plot. The V(max.) was determined as 80ng of cholesteryl ester/h per mg of protein and the apparent K(m) as 1.4mug of cholesteryl ester per mg of protein. The time course for the uptake and hydrolysis suggested that binding of particles to the cell surface preceded the degradation. 3. Cholesteryl esters of native chylomicrons were degraded to a much smaller extent and their presence had only a small inhibitory effect on the degradation of chylomicron remnants. Intestinal very-low-density lipoproteins were degraded somewhat faster than chylomicrons, and caused more inhibition of remnant degradation. Rat high-density lipoproteins inhibited the hydrolysis of remnant cholesteryl ester by up to 50%, but had less influence on the amount of cholesteryl ester that was bound to the cells. Serum decreased both the uptake and hydrolysis, whereas d=1.21 infranatant had no effect. 4. The cholesteryl ester hydrolysis after the uptake by the cells was inhibited by chloroquine and by colchicine. Only 28-36% of the unhydrolysed cholesteryl ester could be released from these cells by trypsin treatment, indicating that the major portion was truly intracellular. The particles that could be released from the cell surface by trypsin and those remaining in the medium had the same triacylglycerol/cholesteryl ester ratio as the added remnant particles. Significant amounts of denser particles were thus not formed during contact with the cell surface. 5. The presence of heparin, as well as preincubation of the cells with heparin, increased the uptake of chylomicron remnants. This effect was most marked in the presence of serum. A much smaller proportion of the other serum lipoproteins was taken up, and this proportion was not increased by heparin. | |
650 | 7 | a MEDICIN OCH HÄLSOVETENSKAPx Medicinska och farmaceutiska grundvetenskaperx Andra medicinska och farmaceutiska grundvetenskaper0 (SwePub)301992 hsv//swe |
650 | 7 | a MEDICAL AND HEALTH SCIENCESx Basic Medicinex Other Basic Medicine0 (SwePub)301992 hsv//eng |
700 | 1 | a Nilsson, Åkeu Lund University,Lunds universitet,Medicin, Lund,Sektion II,Institutionen för kliniska vetenskaper, Lund,Medicinska fakulteten,Gastro,Forskargrupper vid Lunds universitet,Medicine, Lund,Section II,Department of Clinical Sciences, Lund,Faculty of Medicine,Lund University Research Groups4 aut0 (Swepub:lu)med-ani |
710 | 2 | a Medicin, Lundb Sektion II4 org |
773 | 0 | t The Biochemical journald : Portland Press Ltd.g 168:3, s. 483-494q 168:3<483-494x 0264-6021 |
856 | 4 | u http://dx.doi.org/10.1042/bj1680483y FULLTEXT |
856 | 4 | u https://europepmc.org/articles/pmc1183796?pdf=render |
856 | 4 8 | u https://lup.lub.lu.se/record/d5041bb6-8657-412a-9321-774ac2cb97b0 |
856 | 4 8 | u https://doi.org/10.1042/bj1680483 |
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