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R K Ockner

Publications and source records attributed to R K Ockner.

64 records · Page 4Linked to original sources
PubMed1969

Very low density lipoproteins in intestinal lymph: origin, composition, and role in lipid transport in the fasting state.

The transport of endogenous lipids in the lipoproteins of mesenteric lymph was studied in fasting rats with mesenteric lymph fistulas. The lymph was found to contain, in addition to chylomicrons (S(f) >400), a significant amount of another, more dense, triglyceride-rich fraction, the very low density lipoproteins (VLDL), which showed a peak S(f) of 102. The VLDL differed from chylomicrons not only in flotation, but also in per cent lipid composition and electrophoretic mobility in agarose gel. The VLDL fraction was found to contain 47% of the triglyceride and 54% of the cholesterol of fasting lymph and, in the fasting state, was the major lipoprotein species present. When cholestyramine resin was administered intraduodenally, or bile flow was acutely diverted from the intestine, it was demonstrated that the lipids in lymph VLDL, like those in chylomicrons, were derived from the intestine and bile. These data indicate that the VLDL in intestinal lymph are not derived from the plasma but are of intestinal origin. Because certain properties of lymph VLDL were similar to those reported for plasma VLDL (per cent lipid composition, flotation coefficient, and continuing entry into plasma in the fasting state), additional comparisons between these fractions were made. Although lymph VLDL moved to the alpha(2) region in agarose gel, when they were mixed with VLDL-free serum immediately before electrophoresis they showed the alpha(2) mobility of rat serum VLDL. Furthermore, immunoelectrophoretic comparison of partially delipidated lymph and serum VLDL revealed that these fractions shared in common their major apoprotein, and possibly others as well. The fatty acid composition of lymph and serum triglycerides, as determined by gas-liquid chromatography, revealed that although they were generally similar, differences existed which most likely reflected the presence in serum of triglycerides of hepatic origin. These experiments demonstrate the importance of intestinal VLDL in the transport of endogenous lipids in mesenteric lymph in the fasting state. The similarities between intestinal lymph VLDL and plasma VLDL suggest that the latter may be derived in part from the former.

Animals↗
PubMed1969

Very low density lipoproteins in intestinal lymph: role in triglyceride and cholesterol transport during fat absorption.

The role of nonchylomicron very low density lipoproteins (VLDL, S(f) 20-400) in the transport of triglyceride and cholesterol was studied during lipid absorption. Various long chain fatty acids were infused intraduodenally in the form of mixed fatty acid-mono-olein-taurocholate micelles; control animals received saline or taurocholate. As compared with controls, all fatty acids (palmitic, oleic, linoleic) resulted in significant increases in chylomicron (S(f) > 400) triglyceride. In addition, palmitic acid resulted in a twofold increase in VLDL triglyceride, whereas with the absorption of oleic or linoleic acid VLDL triglyceride did not change significantly. Differences in triglyceride fatty acid composition between chylomicrons and VLDL were observed during lipid absorption. Although the absolute amount of endogenous cholesterol in intestinal lymph was not significantly affected by lipid absorption under these conditions, its lipoprotein distribution differed substantially among the lipid-infused groups. During palmitate absorption, VLDL cholesterol was similar to that in the taurocholate-infused controls, and was equal to chylomicron cholesterol. In contrast, during oleate and linoleate absorption the VLDL cholesterol fell markedly, and was less than half of the chylomicron cholesterol in these groups. The half-time of plasma survival of VLDL cholesterol-(14)C was found to be twice that of chylomicron cholesterol-(14)C. These studies demonstrate that dietary long chain fatty acids differ significantly in their effects upon the transport of triglyceride and cholesterol by lipoproteins of rat intestinal lymph. These findings, together with the observed differences in rates of removal of chylomicrons and VLDL from plasma, suggest that variations in lipoprotein production at the intestinal level may be reflected in differences in the subsequent metabolism of absorbed dietary and endogenous lipids.

Animals↗
PubMed1968

Very-low-density lipoprotein in intestinal lymph: evidence for presence of the A protein.

Rat mesenteric lymph very-low-density lipoproteins of intestinal origin contain components which are antigenically identical to plasma high-density lipoprotein. Because the antigenicity of the latter most likely resides in its apoprotein (the A protein), it is concluded that intestinal very-low-density lipoproteins contain the A protein. This and other evidence supports the concept that the intestine is a source of plasma very-low-density lipoprotein.

Animals↗
PubMed1967

Oral contraceptives.

Explore the source record for details and available documents.

Chemical and Drug Induced Liver Injury↗
PubMed1966

Biosynthesis of delta-7-cholesten-3-beta-ol, delta-5,7-cholestadien-3-beta-ol, and delta-5-cholesten-3-beta-ol by guinea pig intestinal mucosa in vitro.

Methods were developed for the separation and determination of the various 27-carbon sterols of intestinal mucosa by means of thin-layer chromatography. Scrapings of the mucosa of the small intestine of guinea pig and rat were shown to incorporate isotope from (14)C-labeled acetate and mevalonate into sterols in vitro. For each substrate this activity was lowest in mucosa from the proximal third of the small intestine and greatest in mucosa from the more distal regions of the small intestine. The total 27-carbon sterol content of guinea pig mucosa varied only slightly along the length of the small intestine, but the concentration of cholesterol was highest distally. More than 95% of the radioactivity incorporated from acetate-2-(14)C into 27-carbon sterols by guinea pig mucosa in 4 hr was recovered as lathosterol and 7-dehydrocholesterol; less than 5% was in cholesterol. The specific activities of the 27-carbon sterols were consistent with the concept that synthesis proceeds from lathosterol to 7-dehydrocholesterol to cholesterol.

Acetates↗
PubMedDate not supplied

Interaction of natural and synthetic albumin polymers with hepatocytes.

The hepatitis B virus binds avidly to albumin polymers which in turn may mediate the initial binding of viral particles to the liver cell. However, the interaction of albumin polymers with the liver remains poorly characterized, and the possibility that hepatic binding reflects an artifact of polymerization with glutaraldehyde has not been excluded. We therefore characterized the binding of 125I-labeled natural and synthetic albumin polymers to suspensions of rat hepatocytes. Saturable binding was demonstrated for all preparations of monomeric and polymeric albumin studied. Glutaraldehyde-polymerized albumin (mean polymerization number = 15) bound much more avidly than naturally occurring albumin polymers (mostly dimers and trimers) or monomeric albumin. Competition between monomer and synthetic polymer was not observed. Reduction of free aldehyde groups on the synthetic polymer decreased nonsaturable binding without affecting saturable binding. Autoradiography confirmed binding of polyalbumin to hepatic parenchymal cells. Glutaraldehyde-polymerized ovalbumin, a protein unrelated to serum albumin, also bound hepatocytes saturably. We conclude that hepatic binding of synthetic albumin polymers is not due to residual aldehyde groups on the polymer and is much more avid than for natural polymer. This difference may reflect the higher degree of polymerization or chemical modification of the synthetic polymer. The hepatic binding sites for synthetic polymer appear distinct from those previously described for monomeric albumin and may not be specific for albumin.

Animals↗
PubMedDate not supplied

Historic overview of studies on fatty acid-binding proteins.

Fatty acid-binding proteins (FABPs) were first identified in the cytosol of rat intestinal mucosa during studies on the regulation of intestinal fatty acid uptake. The subsequent finding of FABP activity in the cytosol of many other tissues initially was believed to reflect a single protein. However, the FABPs are now recognized as products of an ancient gene family comprised of at least 9 structurally related, solube intracellular members, a number of which exhibit high-affinity binding of long-chain fatty acids. Despite recent insights into regulation and tissue-specific expression suggesting FABPs to subserve diverse roles, their precise biological functions remain to be elucidated.

Animals↗