Biochemical properties of pancreatic colipase from the common stingray Dasyatis pastinaca

Abstract

BackgroundPancreatic colipase is a required co-factor for pancreatic lipase, being necessary for its activity during hydrolysis of dietary triglycerides in the presence of bile salts. In the intestine, colipase is cleaved from a precursor molecule, procolipase, through the action of trypsin. This cleavage yields a peptide called enterostatin knoswn, being produced in equimolar proportions to colipase.ResultsIn this study, colipase from the common stingray Dasyatis pastinaca (CoSPL) was purified to homogeneity. The purified colipase is not glycosylated and has an apparent molecular mass of around 10 kDa. The NH2-terminal sequencing of purified CoSPL exhibits more than 55% identity with those of mammalian, bird or marine colipases. CoSPL was found to be less effective activator of bird and mammal pancreatic lipases than for the lipase from the same specie. The apparent dissociation constant (Kd) of the colipase/lipase complex and the apparent Vmax of the colipase-activated lipase values were deduced from the linear curves of the Scatchard plots. We concluded that Stingray Pancreatic Lipase (SPL) has higher ability to interact with colipase from the same species than with the mammal or bird ones.ConclusionThe fact that colipase is a universal lipase cofactor might thus be explained by a conservation of the colipase-lipase interaction site. The results obtained in the study may improve our knowledge of marine lipase/colipase.

Transcriptomic analysis of the lesser spotted catshark (Scyliorhinus canicula) pancreas, liver and brain reveals molecular level conservation of vertebrate pancreas function

“…It is likely therefore that the triacylglycerol lipase activity found previously is a result of the action of Carboxyl ester lipase (CEL or bile salt-stimulated lipase) [ 110 ]. We also find colipase , in agreement with earlier studies of a range of cartilaginous fish and other vertebrates [ 111 – 113 ] and Hepatic lipase and Hormone - sensitive lipase . Several lipid transporting apolipoproteins are also expressed by the catshark pancreas, including apolipoproteins A-IV, E, M and O .…”

A newly thermoactive and detergent‐stable lipase from annular sea bream (Diplodus annularis): Biochemical properties

“…In order to maintain full lipolytic activity in the presence of physiological concentrations of bile salts, pancreatic lipases need a cofactor, the colipase [51]. Colipase has been found in the pancreatic juice of all mammals, avian, and in many lower vertebrates such as common stingray (Dasyatis pastinaca) [52]. In order to check the presence of colipase in the annular seabream digestive glands, the homogenate was treated during 30 Min at pH 4 and/or at 60 • C to inactivate lipase and maintain only colipase activity.…”

“…In order to maintain full lipolytic activity in the presence of physiological concentrations of bile salts, pancreatic lipases need a cofactor, the colipase [51]. Colipase has been found in the pancreatic juice of all mammals, avian, and in many lower vertebrates such as common stingray (Dasyatis pastinaca) [52].…”

Biochemical characterization, cloning and molecular modeling of a digestive lipase from red seabream (Pagrus major): Structural explanation of the interaction deficiency with colipase and lipidic interface

“…It might also display unique structural features, different from classical colipases, making it specific to bony fish lipases. Cartilaginous fish (like common stingray, Dasyatis pastinaca and dogfish ( Squalus acanthius ) , however, possess the classical bile salts–colipase system and display high lipolytic activities, comparable to those described for mammals . We think that the presence of classical colipase effect and high activities of the cartilaginous fish lipolytic system are related to a high fat food content, as compared to that of bony fish .…”