Lipoprotein lipase hydrolysis of retinyl ester: possible implications for retinoid uptake by cells

• Published in: The Journal of biological chemistry Vol. 269; no. 24; pp. 16559 - 16565
• Main Authors: Blaner, W.S, Obunike, J.C, Kurlandsky, S.B, Al-Haideri, M, Piantedos, R, Deckelbaum, R.F, Goldberg, I.J
• Format: Journal Article
• Language: English
• Published: Bethesda, MD American Society for Biochemistry and Molecular Biology 17.06.1994
• Subjects: ACTIVIDAD ENZIMATICA; ACTIVITE ENZYMATIQUE; Adipocytes - metabolism; Adipose Tissue - metabolism; Analytical, structural and metabolic biochemistry; Animals; Biological and medical sciences; Biological Transport; Cattle; Cell Line; CELLULE; CELULAS; Chylomicrons - metabolism; Esters - metabolism; Female; Fundamental and applied biological sciences. Psychology; Heterocyclic compounds, pigments; HIDROLISIS; Humans; HYDROLYSE; Hydrolysis; Lipoprotein Lipase - metabolism; LIPOPROTEINA LIPASA; LIPOPROTEINE LIPASE; Lipoproteins, LDL - metabolism; Liver - metabolism; Male; Milk - enzymology; Miscellaneous; Other biological molecules; RAT; RATA; Rats; Retinoids - metabolism; RETINOL; Substrate Specificity; TEJIDO ADIPOSO; TISSU ADIPEUX; Vitamin A - blood; Vitamin A - metabolism; Lipoprotein LDL; Adipose tissue; Enzymatic activity; Enzyme; Membrane transport; Hydrolases; Esterases; Lipoprotein lipase; Retinoids; Triglyceride; Carboxylic ester hydrolases; Retinol
• ISSN: 0021-9258; 1083-351X
• DOI: 10.1016/s0021-9258(19)89425-5

Adipose tissue contains substantial stores of retinoid (retinol + retinyl ester) that, quantitatively, are second only to retinoid stores in the liver. Our studies show that retinoid levels in adipose tissue are markedly influenced by dietary retinoid intake. Because lipoprotein lipase (LPL) increases the uptake of lipoproteins and lipid emulsion particles by many cell types including adipocytes, we investigated whether LPL also increases retinoid uptake by adipocytes from lipid-containing particles. Addition of LPL (10 microgram/ml) to BFC-1 beta adipocytes produced a 2-fold increase in cellular uptake of [3H]retinoid from a lipid emulsion containing [3H]retinyl ester. Heparin, which displaces LPL from binding sites on cell surface proteoglycans, increased [3H]retinoid uptake by an additional 2-fold. High performance liquid chromatography analyses showed that greater than 75% of the media and 85% of the cellular radioactivity was present as retinol. The conversion of retinyl ester to retinol by LPL was then assessed using model retinyl ester containing lipid emulsions. Although triglyceride appears to be the preferred substrate for LPL, after greater than 25% of the triglyceride was hydrolyzed, significant amounts of retinyl ester were hydrolyzed by LPL. Retinyl ester hydrolysis was increased approximately 20-fold in the presence of a source of apolipoprotein C-II. The physiologically significant palmitate, stearate, oleate, and linoleate esters of retinol were all hydrolyzed by LPL. When LPL was incubated with [3H]retinyl ester containing rabbit mesenteric chylomicrons and in the presence of heparin and apolipoprotein C-II, the LPL was able to completely hydrolyze the retinyl ester to retinol. Thus, LPL is able to catalyze the hydrolysis of retinyl esters and, through the process of hydrolysis, may facilitate uptake of retinoid by adipocytes