Colipase, abbreviated CLPS, is a proteinco-enzyme that counteracts the inhibitory effect of intestinal bile acid on the enzymatic activity of pancreatic lipase. It is secreted by the pancreas in an inactive form, procolipase, which is activated in the intestinal lumen by trypsin.
Intestinal bile acids (which aid lipid digestion by facilitating micelle formation) adhere to the surface of emulsified fat droplets, displacing lipase (which is only active at the water-fat interface) from the droplet surface. Colipase acts as a bridging molecule, binding to both lipase and bile acids, thus anchoring lipase onto the droplet surface, preventing its displacement.[5]
In humans, the colipase protein is encoded by the CLPS gene.[6]
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^Koeppen, Bruce M.; Stanton, Bruce A.; Swiatecka-Urban, Agnieszka, eds. (2024). Berne & Levy Physiology (8th ed.). Philadelphia, PA: Elsevier. ISBN978-0-323-84790-2.
^Davis RC, Xia YR, Mohandas T, Schotz MC, Lusis AJ (May 1991). "Assignment of the human pancreatic colipase gene to chromosome 6p21.1 to pter". Genomics. 10 (1): 262–5. doi:10.1016/0888-7543(91)90509-D. PMID2045105.