Recommendations for pacing.
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Cardiac Pacing, Artificial↗
Biomedical subjects
K M Channon
Publications and source records attributed to K M Channon.
Investigation of lipid transfer in human serum leading to the development of an isotopic method for the determination of endogenous cholesterol esterification and transfer.
The rate at which radioactivity appeared in cholesteryl esters (CE) in whole serum and in very low density lipoproteins (VLDL) and low density lipoproteins (LDL) when radioactively labelled free cholesterol (FC) was incubated with serum was investigated. At 4 degrees C equilibration of radioactive FC with native FC occurred, but there was no conversion to CE. At 37 degrees C CE mass increased in parallel with radioactivity in CE both in whole serum and VLDL/LDL. Incubation at 37 degrees C with an inhibitor of lecithin cholesterol acyl transferase (LCAT) abolished the increase in the total CE radioactivity and mass in serum. Transfer of CE from high density lipoprotein (HDL) to VLDL/LDL, however, continued to occur. An assay for LCAT and for cholesteryl ester transfer protein (CETP) was developed, which employed the increases in radioactive CE in whole serum and VLDL/LDL during a single incubation as indices of LCAT and CETP activity, respectively. Determination of the initial serum FC concentration allowed the expression of these activities in nmol/ml per h. References ranges were established in 62 fasting normolipidaemic men and women and increases in both LCAT and CETP were found following a fatty meal. The experiments thus provided further information about the carrier-mediated transfer of CE from its site of esterification on HDL to VLDL/LDL and formed the basis of a relatively simple assay, which has advantages over previously published methods and which may be used in clinical and epidemiological studies to elucidate the role of CETP and LCAT in atherosclerosis.
Apolipoproteins↗
Isolation of a 25kDal, fibronectin-binding, mitogenic peptide from bovine plasma.
In addition to fibronectin-derived peptides, several immunologically distinct peptides have been found to co-purify with fibronectin on gelatin-sepharose affinity chromatography of bovine plasma. We have isolated a 25kdal peptide ("25K") which co-purifies with fibronectin and which is mitogenic for cultured fibroblasts. 25K migrated as a doublet of Mr 25kdal and 25-28kdal on SDS-PAGE and stimulated 3H-thymidine incorporation into quiescent 3T3 fibroblasts. At 8 micrograms/ml, its mitogenic activity was found to be equivalent to 25 ng/ml PDGF, or 50% that of 10% foetal calf serum. It is unlikely that 25K is a proteolytic fragment of fibronectin since no cross-reactivity was found by western blotting and immunological staining, using a polyclonal anti-fibronectin antibody. Using affinity chromatography, it was found that 25K bound only weakly to gelatin, but inhibited the binding of fibronectin to gelatin. 25K bound strongly to fibronectin, an interaction inhibited by the presence of free gelatin. It would therefore appear that 25K binds specifically to fibronectin through the collagen-binding site.
Animals↗