Purification and characterization of lipoprotein lipase from the white adipose, skeletal muscle, cardiac muscle, mammary gland and lung tissues of the rat

Distinct immunoreactivities suggest the existence of potential tissue variants in rat lipoprotein lipase

“…The similarity of reactivity between the anti-peptide antibody and the enzyme from the five sources, together with the consistent pattern of differences seen when the other polyclonal and monoclonal antibodies raised and screened against the whole molecule were studied, further substantiated the possible existence of tissue-specific molecular variants of LPL, as postulated previously (Soteriou and Cryer, 1993).…”

“…In use against the five tissue LPL preparations, this antiserum revealed only minor variations between the tissue sources, compared with the hierarchy of reactivity observed when antibodies raised against the whole molecule were used. In combination with the outcome of previous studies on some of the physical properties of these preparations [Soteriou and Cryer (1993) Int. J. Biochem.…”

“…LPL is under tissue-specific control with respect to its synthesis and translocation to the endothelial site of action, and it has been suggested previously that tissue-specific variations of the enzyme may exist (Fielding, 1976;Ben-Zeev et al, 1983). Indeed, when LPL was purified from various tissues taken from a single species, variations in the specific activity, isoelectric point and in the patterns observed after two-dimensional electrophoresis were observed between the individual tissue LPL preparations (Soteriou and Cryer, 1993). These preliminary indications of putative tissue-specific LPL variants must, however, be contrasted with the existence of a single, highly conserved gene for LPL (Zechner et al, 1988;Enerback et al, 1988;Edwards et al, 1993), which makes it probable that, if variations do exist, they arise because of distinct post-transcriptional changes, as discussed by Soteriou and Cryer (1993).…”

Low-protein diet prevents tissue lipoprotein lipase activity increase in growing rats

“…They play key roles in vascular lipoprotein metabolism through an efficient transfer of energy in the form of lipids from the sites of synthesis to those of storage or utilisation. The major tissues in which lipoprotein lipase (LPL) activity has been found include adipose tissue, heart, muscles and several other tissues (Soteriou & Cryer, 1993). LPL, present at the luminal surface of the capillary endothelium, is synthesised predominantly by parenchymal cells and requires, for maximal activity, apolipoprotein (Apo) C-II, an activating cofactor which is found in plasma associated mainly with chylomicrons, VLDL and HDL (Goldberg et al 1990;Ikeda et al 1989).…”

Purification of Lipase

“…Investigators have examined the purification of lamb pre-gastric lipase [36], of dog gastric lipase [37], of diacylglycerol lipase from bovine aorta [38], of intestinal acid lipase from rat [39], purification and characterization of bovine pancreatic lipase [40], purification and characterization of rat phospholipase [41], and the purification of lipoprotein lipase from different rat tissues [42]. An important conclusion is that lipases from different tissues subjected to identical purification steps are purified to the same extent.…”