Evidence in vitro that hepatic lipase reduces the concentration of apolipoprotein A-I in rabbit high-density lipoproteins

1990 ◽  
Vol 1044 (1) ◽  
pp. 50-56 ◽  
Author(s):  
Moira A. Clay ◽  
Kerry-Anne Rye ◽  
Philip J. Barter
Keyword(s):  
Hepatic Lipase ◽  
High Density ◽  
High Density Lipoproteins ◽  
Apolipoprotein A

scholarly journals Neutrophil association and degradation of normal and acute-phase high-density lipoprotein 3

1987 ◽  
Vol 248 (3) ◽  
pp. 919-926 ◽  
Author(s):  
E G Shephard ◽  
F C de Beer ◽  
M C de Beer ◽  
M S Jeenah ◽  
G A Coetzee ◽  
...  
Keyword(s):  
Acute Phase ◽  
Density Lipoprotein ◽  
High Density ◽  
High Density Lipoproteins ◽  
Human Neutrophils ◽  
Amyloid A ◽  
Apolipoprotein A ◽  
Serum Amyloid A Protein ◽  
Alpha 1 Antitrypsin

The interaction of normal and acute-phase high-density lipoproteins of the subclass 3 (N-HDL3 and AP-HDL3) with human neutrophils and the accompanying degradation of HDL3 apolipoproteins have been studied in vitro. The chemical composition of normal and acute-phase HDL3 was similar except that serum amyloid A protein (apo-SAA) was a major apolipoprotein in AP-HDL3 (approx. 30% of total apolipoproteins). 125I-labelled AP-HDL3 was degraded 5-10 times faster than 125I-labelled N-HDL3 during incubation with neutrophils or neutrophil-conditioned medium. Apo-SAA, like apolipoprotein A-II (apo-A-II), was more susceptible than apolipoprotein A-I (apo-A-I) to the action of proteases released from the cells. The amounts of cell-associated AP-HDL3 apolipoproteins at saturation were up to 2.8 times greater than N-HDL3 apolipoproteins; while apo-A-I was the major cell-associated apolipoprotein when N-HDL3 was bound, apo-SAA constituted 80% of the apolipoproteins bound in the case of AP-HDL3. The associated intact apo-SAA was mostly surface-bound as it was accessible to the action of exogenous trypsin. alpha 1-Antitrypsin-resistant (alpha 1-AT-resistant) cellular degradation of AP-HDL3 apolipoproteins also occurred; experiments in which pulse-chase labelling was performed or lysosomotropic agents were used indicated that insignificant intracellular degradation occurred which points to the involvement of cell-surface proteases in this degradation.

The in vitro interaction of human apolipoprotein A-I and high density lipoproteins

1977 ◽  
Vol 489 (3) ◽  
pp. 486-501 ◽  
Author(s):  
James Shepherd ◽  
Antonio M. Gotto ◽  
O.David Taunton ◽  
Muriel J. Caslake ◽  
Elizabeth Farish
Keyword(s):  
High Density ◽  
High Density Lipoproteins ◽  
Human Apolipoprotein ◽  
Apolipoprotein A ◽  
In Vitro Interaction

scholarly journals Importance of Apolipoprotein A-I and A-II Composition in HDL and Its Potential for Studying COVID-19 and SARS-CoV-2

Medicines ◽  
2021 ◽  
Vol 8 (7) ◽  
pp. 38
Author(s):  
Kyung-Hyun Cho
Keyword(s):  
Antiviral Activity ◽  
High Density ◽  
High Density Lipoproteins ◽  
Potent Antiviral Activity ◽  
Apolipoprotein A ◽  
Putative Role

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.

scholarly journals Expression of human apolipoprotein A-II and its effect on high density lipoproteins in transgenic mice.

1992 ◽  
Vol 267 (30) ◽  
pp. 21630-21636 ◽  
Author(s):  
J.R. Schultz ◽  
E.L. Gong ◽  
M.R. McCall ◽  
A.V. Nichols ◽  
S.M. Clift ◽  
...  
Keyword(s):  
Transgenic Mice ◽  
High Density ◽  
High Density Lipoproteins ◽  
Human Apolipoprotein ◽  
Apolipoprotein A
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