Biomedical subjects

G Assmann

Publications and source records attributed to G Assmann.

At least 451 records · Page 25Linked to original sources

PubMed1975

Swine lipoproteins and atherosclerosis. Changes in the plasma lipoproteins and apoproteins induced by cholesterol feeding.

Cholesterol feeding in miniature swine resulted in a hypercholesterolemia with a distinctive hyperlipoproteinemia and the subsequent development of atherosclerosis. Alterations in the type and distribution of plasma lipoproteins induced by cholesterol feeding were as follows: (a) the occurrence of beta-migrating lipoproteins (B-VLDL) as well as very low density lipoproteins in the d less than 1.006 ultracentrifugal fraction; (b) an increased prominence of the intermediate lipoproteins (d = 1.006-1.02); (c) an increased prominence of low density lipoproteins; and (d) the occurrence of a distinctive lipoprotein with alpha mobility which was referred to as HDLc (cholesterol induced). Characterization of the various plasma lipoproteins included chemical composition, size by electron microscopy, and apoprotein content. The B-VLDL resembled the beta-migrating lipoproteins of human Type III hyperlipoproteinemia and contained a prominent protein equivalent to the arginine-rich apoprotein in addition to the B apoprotein, apo-A-I, and the fast-migrating apoproteins (apo-C). The HDLc were rich in cholesterol, ranged in size from 100 to 240 A in diameter, and contained the arginine-rich apoprotein and apo-A0I but lacked the B apoprotein. The arginine-rich apoproteins isolated from B-VLDL and HDLc by gel chromatography were similar in amino acid analyses, with glutamic acid as their amino-terminal residue. The occurrence of a spectrum of cholesterol-rich lipoproteins which contained the arginine-rich apoprotein with the occurrence of accelerated atherosclerosis suggested an interesting, although speculative, association.

Amino Acids↗

PubMed1975

Accumulation of oxygenated steryl esters in Wolman's disease.

7alpha- and 7beta-hydroxycholesteryl esters, 7-ketocholesteryl esters, and 5,6alpha- and 5,6beta-epoxycholesteryl esters have been identified in tissues of patients affected by Wolman's disease. Their structural identities were determined by mass spectroscopy and nuclear magnetic resonance spectroscopy and confirmed by chemical synthesis. It is postulated that cholesteryl ester hydrolase deficiency in Wolman's disease might lead to accumulation of oxygenated steryl esters in vivo and impairment of bile acid formation.

Adrenal Glands↗

PubMed1974

31P nuclear magnetic resonance spectroscopy of native and recombined lipoproteins.

Native and recombined lipoproteins have been studied by (31)P nuclear magnetic resonance spectroscopy. Very low-, low-, and high-density lipoproteins exhibited characteristic spectra. The main resonances were assigned to phosphatidylcholine and sphingomyelin. Relaxation times for these phospholipids were separately measured in low-density lipoproteins and high-density lipoproteins. The effect of paramagnetic ions (Eu(+++)) on the nuclear magnetic resonance spectrum of high-density lipoproteins is reported.

Europium↗

PubMed1974

Lipid-protein interactions in high density lipoproteins.

Delipidated high density lipoprotein (apo-HDL), isolated apolipoproteins apoA-I and apoA-II, S-carboxymethylated apoA-II, apoC-III, the NH(2)- and COOH-terminal CNBr peptides of apoA-II, and the COOH-terminal CNBr peptide of apoA-I were recombined in vitro with [N-C(3)H(3)-choline]phosphatidylcholine (PC) and [N-(14)CH(3)-choline]sphingomyelin (SPM). The lipid-protein complexes were analyzed by ultracentrifugal flotation, agarose gel chromatography and circular dichroism. ApoHDL, apoA-II, and S-carboxymethylated apoA-II readily recombined with PC or SPM to form particles that were similar in size to native HDL. The COOH- but not the NH(2)-terminal CNBr peptide of apoA-II recombined with lipid. ApoA-I and the COOH-terminal CNBr peptide of apoA-I, however, recombined with PC or SPM to only a limited extent, suggesting that protein-protein interactions between apoA-I and apoA-II are important in the integration of apoA-I into recombined lipoprotein particles. Analysis of the recombined lipid-protein complexes by circular dichroism indicated that there was an increase in helical structure concomitant with lipid-protein binding. The reconstituted particles had many of the physical and chemical properties of the native lipoprotein.

Chromatography↗

PubMed1974

A molecular model of high density lipoproteins.

Based on the analysis of recombined lipidapoprotein complexes by C-13 and P-31 nuclear magnetic resonance spectroscopy and circular dichroism [Assmann, G., Sokoloski, E. A. & Brewer, H. B., Jr. (1974) Proc. Nat. Acad. Sci. USA 71, 549-553; Assmann, G., Highet, R. J., Sokoloski, E. A. & Brewer, H. B., Jr. (1974) Proc. Nat. Acad. Sci. USA 71, in press; Assmann, G. & Brewer, H. B., Jr. (1974) Proc. Nat. Acad. Sci. USA 71, 989-993] and the identification of conformational amphipathic regions in apoproteins, a new model for human high density lipoproteins is proposed. This model is analogous to membrane models proposed by Singer, in that protein "icebergs" are embedded in a "sea" of lipid.

Amino Acid Sequence↗

PubMed1974

13C nuclear magnetic resonance spectroscopy of native and recombined lipoproteins.

(13)C nuclear magnetic resonance data on native and recombined lipoproteins are reported. [Methyl-(13)C]phosphatidylcholine, [methyl-(13)C]sphingomyelin, 1,2-[dioleoyl-1-(13)C]-sn-phosphatidylcholine and cholesteryl-[1-(13)C]oleate were enriched with 90% carbon-13 in respective molecules by chemical synthesis and used for recombination experiments with high density lipoprotein apoproteins. Relaxation times for these specifically enriched lipids in organic solvents, (2)H(2)O, and lipid-protein complexes isolated by ultracentrifugal flotation, were measured. The results show that both the phosphatidylcholine and sphingomyelin polar headgroups have the same hydrophilic environment in either sonicated lipid particles or reassembled lipoproteins, and suggest that ionic interaction of lipid and apolipoproteins is of minor importance in the formation of plasma lipoprotein complexes. Our experiments indicate that (13)C nuclear magnetic resonance spectroscopy will contribute to the understanding of lipidprotein interaction in lipoproteins and membranes.

Apoproteins↗

PubMed1974