The affinities of procolipase and colipase for interfaces are regulated by lipids

Biophysical Journal
G D SchmitH L Brockman

Abstract

It has been suggested that at physiological pH, the trypsin-catalyzed activation of the lipase cofactor, procolipase, to colipase has no consequence for intestinal lipolysis and serves primarily to release the N-terminal pentapeptide, enterostatin, a satiety factor (Larsson, A., and C. Erlanson-Albertsson 1991. The effect of pancreatic procolipase and colipase on pancreatic lipase activation. Biochim. Biophys. Acta 1083:283-288). This hypothesis was tested by measuring the adsorption of [14C]colipase to monolayers of 1-stearoyl-2-oleoyl-sn-3-glycerophosphocholine and 13, 16-cis, cis-docosadienoic acid in the presence and absence of procolipase. With saturating [14C]colipase in the subphase, the surface excess of [14C]colipase is 29% higher than that of procolipase, indicating that colipase packs more tightly in the interface. With [14C]colipase-procolipase mixtures, the proteins compete equally for occupancy of the argon-buffer interface. However, if a monolayer of either or both lipids is present, [14C]colipase dominates the adsorption process, even if bile salt is present in the subphase. If [14C]colipase and procolipase are premixed for > 12 h at pH approximately 8, this dominance is partial. If they are not premixed, procol...Continue Reading

Citations

Jun 22, 2014·Current Cardiology Reports·Alan A HennessyCatherine Stanton
Sep 29, 2005·Analytical Biochemistry·W E MomsenH L Brockman
Sep 3, 2003·Journal of Lipid Research·Takahiro TsujitaHoward L Brockman
Mar 8, 2011·Advances in Colloid and Interface Science·P J Wilde, B S Chu

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