Metabolism of apolipoprotein A-I of chylomicrons in rats and humans

1981 ◽  
Vol 59 (8) ◽  
pp. 613-618 ◽  
Author(s):  
Jean-Louis Vigne ◽  
Richard J. Havel

After intravenous injection of a large amount of small chylomicrons into intact rats, the concentration of apolipoprotein (apo) A-I was increased by about 40% and remained at this elevated level as most of the chylomicron triglycerides were removed from plasma during the ensuing hour. This apo A-I rapidly left the chylomicrons and was transferred to lipoproteins of higher density. Such transfer of apo A-I did not occur when chylomicrons were incubated at comparably high concentrations with rat serum. In normolipidemic humans, the concentration of apo A-I and apo A-II, as well as phospholipids, increased in the light subfraction of high density lipoproteins (HDL2) 4 to 7 h after ingestion of a meal containing 1.5 g cream fat per kilogram body weight. The concentration of these components increased in the heavy subfraction of high density lipoproteins (HDL3) after 12 to 24 h. The concentration of apo E in plasma was unaffected by fat ingestion, but the concentration of this protein increased in lipoproteins of density less than 1.006 g∙mL−1 and fell in lipoproteins of higher density. It is concluded that apo A-I in rat chylomicrons is transferred quantitatively to HDL as chylomicron remnants are formed. Chylomicron apo A-I and apo A-II appear to be transferred similarly to HDL in humans, whereas apo E is transferred from HDL to chylomicrons after chylomicrons enter the blood.

1985 ◽  
Vol 226 (3) ◽  
pp. 715-721 ◽  
Author(s):  
F M Van't Hooft ◽  
A Van Tol

O-(4-Diazo-3-[125I]iodobenzoyl)sucrose ([125I]DIBS), a novel labelling compound specifically designed to study the catabolic sites of serum proteins [De Jong, Bouma, & Gruber (1981) Biochem. J. 198, 45-51], was applied to study the tissue sites of degradation of serum lipoproteins. [125I]DIBS-labelled apolipoproteins (apo) E and A-I, added in tracer amounts to rat serum, associate with high-density lipoproteins (HDL) just like conventionally iodinated apo E and A-I. No difference is observed between the serum decays of chromatographically isolated [125I]DIBS-labelled and conventionally iodinated HDL labelled specifically in either apo E or apo A-I. When these specifically labelled HDLs are injected into fasted rats, a substantial [125I]DIBS-dependent 125I accumulation occurs in the kidneys and in the liver. No [125I]DIBS-dependent accumulation is observed in the kidneys after injection of labelled asialofetuin or human low-density lipoprotein. It is concluded that the kidneys and the liver are important sites of catabolism of rat HDL apo E and A-I.


Medicines ◽  
2021 ◽  
Vol 8 (7) ◽  
pp. 38
Author(s):  
Kyung-Hyun Cho

The composition and properties of apolipoprotein (apo) A-I and apoA-II in high-density lipoproteins (HDL) might be critical to SARS-CoV-2 infection via SR-BI and antiviral activity against COVID-19. HDL containing native apoA-I showed potent antiviral activity, while HDL containing glycated apoA-I or other apolipoproteins did not. However, there has been no report to elucidate the putative role of apoA-II in the antiviral activity of HDL.


1992 ◽  
Vol 267 (30) ◽  
pp. 21630-21636 ◽  
Author(s):  
J.R. Schultz ◽  
E.L. Gong ◽  
M.R. McCall ◽  
A.V. Nichols ◽  
S.M. Clift ◽  
...  

1999 ◽  
Vol 40 (9) ◽  
pp. 1695-1700 ◽  
Author(s):  
Wanda Vélez-Carrasco ◽  
Alice H. Lichtenstein ◽  
P. Hugh R. Barrett ◽  
Zhiyong Sun ◽  
Gregory G. Dolnikowski ◽  
...  

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