Release of lipoprotein lipase and hepatic triglyceride lipase in rats by heparin and other sulphated polysaccharides.
The ability of parenteral heparin to release the capillary-bound enzymes lipoprotein lipase (LPL) and hepatic triglyceride lipase (HTGL) into the circulation is shared by several other sulphated polysaccharides. The lipase-releasing activity in rats of two unfractionated heparins has been compared with that of characterised preparations of other glycosaminoglycans and of two partially synthetic polysaccharides. The results suggest that whilst both molecular weight and degree of sulphation are important in determining the potency, there is also some specific structural element associated with the heparin class. The clearance of lipases was also investigated. The half-lives of LPL (29 mins) and of HTGL (36 mins) did not appear to be affected by the nature of the releasing agent.
Williams
S P
SP
Dept Biochemistry, Charing Cross and Westminster Medical School, London, UK.
Johnson
E A
EA
D000818:Animals; D001780:Blood Coagulation Tests; D006207:Half-Life; D006493:Heparin / Q000494:pharmacology*; D008049:Lipase / Q000378:metabolism*; D008071:Lipoprotein Lipase / Q000378:metabolism*; D008099:Liver / Q000187:drug effects / Q000201:enzymology*; D008297:Male; D011134:Polysaccharides / Q000494:pharmacology*; D051381:Rats
D011134:Polysaccharides; D006493:Heparin; D008049:Lipase; D008071:Lipoprotein Lipase