gopubmed logo
find other proteinsAll proteins
GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

Colipase, pancreatic

colipase, CLPS
The protein encoded by this gene is a cofactor needed by pancreatic lipase for efficient dietary lipid hydrolysis. It binds to the C-terminal, non-catalytic domain of lipase, thereby stabilizing an active conformation and considerably increasing the overall hydrophobic binding site. The gene product allows lipase to anchor noncovalently to the surface of lipid micelles, counteracting the destabilizing influence of intestinal bile salts. This cofactor is only expressed in pancreatic acinar cells, suggesting regulation of expression by tissue-specific elements. Three transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Nov 2011] (from NCBI)
Top mentioned proteins: ACID, HAD, CAN, Trypsin, fibrillin-1
Papers on colipase
Structure of a putative ClpS N-end rule adaptor protein from the malaria pathogen Plasmodium falciparum.
Egea et al., Los Angeles, United States. In Protein Sci, Jan 2016
In bacteria, the ClpS adaptor binds and delivers N-end rule substrates for their degradation upon association with the ClpA/P chaperone/protease.
Characterization of ClpS2, an essential adaptor protein for the cyanobacterium Synechococcus elongatus.
Clarke et al., Göteborg, Sweden. In Febs Lett, Jan 2016
The adaptor protein ClpS associates to the Clp protease and promotes degradation of N-end rule substrates in eubacteria and in algal/plant chloroplasts.
A model for the structure and mechanism of action of pulmonary surfactant protein B.
Pérez-Gil et al., Madrid, Spain. In Faseb J, Oct 2015
A similar sequential assembly of dimers, supradimeric oligomers and phospholipid-loaded tubes could explain the activity of other saposins with colipase, cytolysin, or antibiotic activities, offering a common framework to understand the range of functions carried out by saposins.
A newly thermoactive and detergent-stable lipase from annular sea bream (Diplodus annularis): Biochemical properties.
Fendri et al., Sfax, Tunisia. In Biotechnol Appl Biochem, Oct 2015
No colipase was detected in the annular seabream pyloric caeca.
Effect of feeding strategies on weaning weight and milk production of Holstein × Zebu calves in dual purpose milk production systems.
de Duarte et al., Viçosa, Brazil. In Trop Anim Health Prod, Aug 2015
Calves in treatment 4 (CCPS) were supplemented with 1 kg of concentrate from 90 to 180 days of age and calves in treatment 5 (CLPS) were supplemented with 1 kg of concentrate from 90 to 270 days of age.
Genetic analysis and cAMP measurement: comparison between lean and obese anovulating mice.
da Silva et al., São Paulo, Brazil. In Rev Bras Ginecol Obstet, Apr 2015
RESULTS: The most downregulated genes in the Obesity Group included adenylate cyclase-activating polypeptide type 1, somatostatin, apolipoprotein A4, pancreatic colipase, and interleukin-1 beta.
The ClpS-like N-domain is essential for the functioning of Ubr11, an N-recognin in Schizosaccharomyces pombe.
Kitamura, Hiroshima, Japan. In Springerplus, 2013
The type 1 and type 2 residues bind to the UBR box and the ClpS/N-domain, respectively, in canonical Ubr ubiquitin ligases that act as N-recognins.
Interfacial & colloidal aspects of lipid digestion.
Chu et al., Norwich, United Kingdom. In Adv Colloid Interface Sci, 2011
Pancreatic lipase, which is responsible for the majority of lipid hydrolysis, also requires the action of bile salts and colipase to function effectively.
The mPlrp2 and mClps genes are involved in the hydrolysis of retinyl esters in the mouse liver.
Zhang et al., Nanjing, China. In J Lipid Res, 2011
Data suggest that the conditional expression of mPlrp2 and mClps is involved in the hydrolysis of retinyl esters in the mouse liver.
Physiological parameters governing the action of pancreatic lipase.
Pearson et al., Newcastle upon Tyne, United Kingdom. In Nutr Res Rev, 2010
Colipase-dependent pancreatic lipase is believed to be the major gastrointestinal enzyme involved in catalysis of lipid ester bonds.
The bacterial N-end rule pathway: expect the unexpected.
Zeth et al., Melbourne, Australia. In Mol Microbiol, 2010
In prokaryotes, the recognition component is a specialized adaptor protein, known as ClpS, which delivers target proteins directly to the ClpAP protease for degradation.
Enterostatin deficiency increases serum cholesterol but does not influence growth and food intake in mice.
Lowe et al., Pittsburgh, United States. In Am J Physiol Endocrinol Metab, 2009
colipase (-/-)mice develop diet-induced obesity, as do colipase (+/+) mice, and have normal responses to a two-macronutrient choice diet and to a switch from a high-fat to a low-fat diet
Controlled destruction: AAA+ ATPases in protein degradation from bacteria to eukaryotes.
Weber-Ban et al., Zürich, Switzerland. In Curr Opin Struct Biol, 2009
Crystal structures of the ubiquitin receptor Rpn13 as well as ClpS, the bacterial determinant of N-end rule degradation, in complex with their respective substrates demonstrate principles of substrate recognition by chaperone-proteases.
Genetic variability of procolipase associates with altered insulin secretion in non-diabetic Caucasians.
Häring et al., Tübingen, Germany. In Exp Clin Endocrinol Diabetes, 2009
CLPS genetic variability associates with insulin secretory function in non-diabetic humans and may represent a novel candidate gene for development of type 2 diabetes
Procolipase gene: no association with early-onset obesity or fat intake.
Hebebrand et al., Marburg an der Lahn, Germany. In Obes Facts, 2008
found no evidence for an association of pancreatic colipase(CLPS) single nucleotide polymorphisms rs2766597, rs41270082, rs3748050, and rs3748051 with obesity or percentage of dietary fat intake
The toxicogenomic multiverse: convergent recruitment of proteins into animal venoms.
de la Vega et al., Melbourne, Australia. In Annu Rev Genomics Hum Genet, 2008
The protein scaffolds utilized convergently have included AVIT/colipase/prokineticin, CAP, chitinase, cystatin, defensins, hyaluronidase, Kunitz, lectin, lipocalin, natriuretic peptide, peptidase S1, phospholipase A(2), sphingomyelinase D, and SPRY.
A polymorphism in the gene encoding procolipase produces a colipase, Arg92Cys, with decreased function against long-chain triglycerides.
Lowe et al., Pittsburgh, United States. In J Lipid Res, 2007
Our findings demonstrate that the Arg92Cys polymorphism decreases the function of Cys92 colipase. This change may contribute to the development of type 2 diabetes.
ClpS is an essential component of the N-end rule pathway in Escherichia coli.
Bukau et al., Heidelberg, Germany. In Nature, 2006
Here we report that the ClpAP-specific adaptor, ClpS, is essential for degradation of N-end rule substrates by ClpAP in bacteria.
Structure of the pancreatic lipase-procolipase complex.
Cambillau et al., Marseille, France. In Nature, 1992
In the presence of such amphiphiles, lipase binding to the interface requires a protein cofactor, colipase.
Watching fat digestion.
Carey et al., In Science, 1979
Under simulated physiological conditions, hydrolysis of emulsified fat droplets by human pancreatic lipase in the presence of colipase and bile salt micelles proceeds with the sequential formation of two visible product phases.
share on facebooktweetadd +1mail to friends