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Differences in the Plasma Transport and Tissue Concentrations of Tocopherols and Tocotrienols: Observations in Humans and Hamsters
The transport, tissue concentration, and relative biologic function of tocopherol and tocotrienol appear somewhat disparate and possibly unrelated.
Use of m1-toxin as a selective antagonist of m1 muscarinic receptors.
- S. I. Max, J. Liang, H. H. Valentine, L. Potter
- Biology, ChemistryThe Journal of pharmacology and experimental…
- 1 October 1993
m1-Toxin is the only ligand which is known to bind specifically to the extracellular face of genetically defined m1 muscarinic receptors; it binds pseudoirreversibly. A variety of studies were…
Anti-muscarinic toxins from Dendroaspis angusticeps.
Amino terminal region of acute phase, but not constitutive, serum amyloid A (apoSAA) specifically binds and transports cholesterol into aortic smooth muscle and HepG2 cells.
It is suggested that apoSAA modulates the local flux of cholesterol between cells and lipoproteins during inflammation and atherosclerosis.
Stable allosteric binding of m1-toxin to m1 muscarinic receptors.
It is demonstrated that m1-toxin binds allosterically and pseudoirreversibly to m1 receptors, and that the toxin can stabilize the outward-facing pocket of m 1 receptors which contains and binds competitive antagonists.
Plasma lipoproteins, biliary lipids and bile acid profile differ in various strains of Syrian hamsters Mesocricetus auratus.
A unique amyloidogenic apolipoprotein serum amyloid A (apoSAA) isoform expressed by the amyloid resistant CE/J mouse strain exhibits higher affinity for macrophages than apoSAA1 and apoSAA2 expressed…
The acute phase response in apolipoprotein A-1 knockout mice: apolipoprotein serum amyloid A and lipid distribution in plasma high density lipoproteins.
Recombinant human serum amyloid A (apoSAAp) binds cholesterol and modulates cholesterol flux.
Results suggest that apoSAA can potentially serve as a transient cholesterol-binding protein, and unlike peritoneal exudate cells, human HepG2 hepatoma cells do not secrete an enzyme that degrades ApoSAAp.
The fibril forming region of the beta-amyloid precursor differs from that of the amyloid A precursor in its interaction with lipids.
The results indicate that AbetaPP but not Abeta peptide can be retained in solution in the presence of C and PC and suggest that this failure to interact with lipids may account for the greater insolubility of Abeta fibrils than AA fibril forming region.