Complexing of serum pre-β- and β-lipoproteins and acid mucopolysaccharides

Srinivasan, Sathanur R.; Lopez-S, Alfredo; Radhakrishnamurthy, B.; Berenson, Gerald S.

doi:10.1016/0021-9150(70)90036-5

Cited by 143 publications

(21 citation statements)

References 18 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…35 Several investigators have proposed that the role of calcium in the formation of insoluble PG-LDL complexes involves electrostatic bridging between the sulfate groups of the PG and the phospholipids of the LDL. 36 - 38 Changes within choline species were the only differences in LDL phospholipid distribution during fish-oil compared with lard feeding for the animals in the present study, 20 and whether polar head group-induced electrostatic differences are responsible for the different interactions with PG remains to be defined. A more likely probability is that phospholipid changes may alter the conformation of apo B on the LDL particles, and this may affect the exposure of PG binding sites.…”

Section: Resultsmentioning

confidence: 67%

Reduced proteoglycan binding of low density lipoproteins from monkeys (Macaca fascicularis) fed a fish oil versus lard diet.

Edwards

Gebre

Parks

1991

Arterioscler Thromb

View full text Add to dashboard Cite

Section: Resultsmentioning

confidence: 67%

Reduced proteoglycan binding of low density lipoproteins from monkeys (Macaca fascicularis) fed a fish oil versus lard diet.

Edwards

Gebre

Parks

1991

Arterioscler Thromb

View full text Add to dashboard Cite

“…(10,20, and 80 nM) from an agarosearterial PG, column (0.5 ml bed volume). The curves contain all the information required for calculation of the binding parameters Kd (dissociation constant) and Bt (maximal binding) using the procedure of Kasai et al 27 or Scatchard plots.…”

Section: Llpoprotelnsmentioning

confidence: 99%

Identification of Apo B-100 segments mediating the interaction of low density lipoproteins with arterial proteoglycans.

et al. 1988

View full text Add to dashboard Cite

The Interactions of low density llpoproteln (LDL) and apollpoproteln (apo) B-100 segments with chondroltin-6-S0 4 rich aortic proteoglycans aggregate (CSPG) were studied by using quantitative frontal elutlon affinity chromatography. The affinity of the agarose-CSPG was higher for LDL than for very low density llpoproteln, and high density llpoproteln was not bound. LDL from different Individuals had dissociation coefficients (Kd) from 28 to 179 nM. Experiments with tryptlc hydrolysates of apo B suggested that the capacity of LDL to bind with CSPG resides in the protein. Nine apo B-100 hydrophlllc peptldes, 12 to 26 amlno acids long, were selected, and three were found to Interact with the agarose-bound CSPG: apo B P-1 (LRKHKUDVISMY-RELLKDLSKEA, residues 4230 to 4254), apo B P-2 (RLTRKRGLKLATALSLSNK, residues 3359 to 3377), and apo B P-11 (RQVSHAKEKLTALTKK, residues 2106 to 2121). These peptides competed with LDL for binding to the agarose-bound and soluble CSPG; apo B P-2 was the most effective. This correlates with Kd values: 63, 86, and 82 /iM for apo B P-2, P-1, and P-11, respectively. The peptldes shared an excess of positive-charged side chains. Apo B P-2 belongs to the lys-and arg-rich, LDL-receptor domain. Apo E also binds to the agarose-proteoglycan. The results suggest that apo B regions with sequences and charge distributions analogous to those of residues 3359 to 3377, 4230 to 4254, and 2106 to 2121 are among those responsible for the Interaction of LDL with Intlma-media CSPG. (Arteriosclerosis 8:368-377, July/August 1988)

show abstract

“…Of all the glycosaminoglycans, heparin has the most potent ability to form complexes with apo B-containing lipoproteins in vitro. 42 The presence of heparin in aortic tissue has been previously described. 43 However, it is also likely that the fibrous plaque complexes might have acquired mast cell-derived heparin with the progression of the lesions.…”

mentioning

confidence: 99%

Lipoprotein-proteoglycan complexes from atherosclerotic lesions promote cholesteryl ester accumulation in human monocytes/macrophages.

Vijayagopal

Srinivasan

Radhakrishnamurthy

et al. 1992

Arterioscler Thromb

View full text Add to dashboard Cite

Lipoprotein-proteoglycan complexes from human atherosclerotic lesions were studied to determine their ability to stimulate cholesteryl ester accumulation in human monocytes/macrophages. Complexes containing apolipoprotein (apo) B lipoproteins and proteoglycans were extracted from fatty streaks and fibrous plaque lesions of human aortas by extraction with 0.15 M NaCl. Fractionation of the complex with Bio-Gel A-50m yielded a single fraction from fatty streaks and two fractions from fibrous plaques. The complexes were further purified by antl-apo B affinity chromatography and analyzed for apolipoproteins, lipids, and glycosaminoglycans. Apo B was the only apolipoprotein present in the complexes. Although the complexes from fatty streaks and fibrous plaques contained varying proportions of hyaluronic acid, chondroitin 6-sulfate, and dermatan sulfate, heparin was present in only the fibrous plaque complexes. All three lipoprotein-proteogtycan complexes increased the rate of incorporation of [ M C]oleate into cholesteryl [ 14 C]oleate and stimulated cholesteryl ester accumulation in monocytes/macrophages. However, the complexes from fibrous plaques were more potent than those from fatty streaks in this regard. Cholesteryl ester synthesis that is mediated by the uptake of the complexes was dose dependent and showed apparent saturation, suggesting that cell surface binding may be required. Chloroquine, a lysosomotropic agent, inhibited cholesteryl ester synthesis that is induced by the complexes, indicating that lysosomal hydrolysis was essential. Cholesteryl ester synthesis that is mediated by the complexes was inhibited 70-79% by polyinosinic acid. Furthermore, excess unlabeled fibrous plaque complexes significantly inhibited the binding and interaalization of in vitro In vitro, low density lipoprotein (LDL) does not induce cholesteryl ester accumulation in macrophages from different sources, including human

show abstract

Complexing of serum pre-β- and β-lipoproteins and acid mucopolysaccharides

Cited by 143 publications

References 18 publications

Reduced proteoglycan binding of low density lipoproteins from monkeys (Macaca fascicularis) fed a fish oil versus lard diet.

Reduced proteoglycan binding of low density lipoproteins from monkeys (Macaca fascicularis) fed a fish oil versus lard diet.

Identification of Apo B-100 segments mediating the interaction of low density lipoproteins with arterial proteoglycans.

Lipoprotein-proteoglycan complexes from atherosclerotic lesions promote cholesteryl ester accumulation in human monocytes/macrophages.

Contact Info

Product

Resources

About