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Gene Review

CEL  -  carboxyl ester lipase

Bos taurus

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Disease relevance of CEL

  • These viral component presentations were selected to obtain mAbs against specific BLV proteins: located on the cell surface (FOR and CEL), in free virus particles (PV) and intracellular viral proteins (SOC and LYS) [1].
  • Pneumonia in pigs caused by experimental infection with Mycoplasma hyopneumoniae resulted in a 25-fold increase in the B-cell population in BAL and lung parenchyma 28 days post infection [2].
  • Naive calves infected with Pasteurella multocida had a 5-fold increase in the B-cell blast population in lung parenchyma and BAL, and a greater than 60-fold increase in the draining lymph node at 9 days post infection [2].

High impact information on CEL


Chemical compound and disease context of CEL

  • The five antigen preparations for immunizing BALB/c mice were: live cells (CEL), sonicated and ultracentrifuged cells (SOC), cell lysates (LYS), semi-purified BLV (PV), and formalin-treated cells (FOR) from two cell lines permanently infected with BLV (FLK-BLV and BLV-bat2) [1].

Biological context of CEL

  • The high-resolution crystal structure of bovine pancreatic cholesterol esterase (Rcryst = 21.1%; Rfree = 25.0% to 1.6 A resolution) shows an alpha-beta hydrolase fold with an unusual active site environment around the catalytic triad [4].
  • Comparison of the N-terminal amino acid sequence of bp-BAL with the deduced amino acid sequence of the latter revealed that they are identical [5].
  • Conventional antibody against Nepsilon-(carboxymethyl)lysine (CML) shows cross-reaction to Nepsilon-(carboxyethyl)lysine (CEL): immunochemical quantification of CML with a specific antibody [6].
  • In the dark, IFA reversibly inhibited cholesteryl [14C]oleate hydrolysis by purified bovine pancreatic cholesterol esterase with an apparent Ki of 150 microM [7].
  • Taken together, these data suggest that pancreatic cholesterol esterase and possibly other proteoglycan-binding extracellular enzymes of neutral lipid metabolism may facilitate movement of neutral lipids into the plasma membrane and direct them into functional intracellular sites [8].

Anatomical context of CEL


Associations of CEL with chemical compounds

  • The structure of pancreatic cholesterol esterase, an enzyme that hydrolyzes a wide variety of dietary lipids, mediates the absorption of cholesterol esters, and is dependent on bile salts for optimal activity, is determined to 1.6 A resolution [4].
  • The amphipathic, helical lid found in other triglyceride lipases is truncated in the structure of cholesterol esterase and therefore is not a salient feature of activation of this lipase [4].
  • RESULTS: The crystal structures of bovine BAL and its complex with taurocholate have been determined at 2.8 A resolution [10].
  • Staining with various lectins showed that bp-BAL is a glycoprotein which contains fucose residues [5].
  • The lipase activity increased 42 times in the presence of 10 mM sodium taurocholate, which for the first time provides direct evidence that a bile salt-activated lipase (bp-BAL) was isolated from bovine pancreas [5].

Other interactions of CEL


Analytical, diagnostic and therapeutic context of CEL


  1. Production and characterization of monoclonal antibodies against bovine leukaemia virus using various crude antigen preparations: a comparative study. Llames, L., Gomez-Lucia, E., Domenech, A., De Avila, A., Suarez, G., Goyache, J. J. Vet. Med. B Infect. Dis. Vet. Public Health (2000) [Pubmed]
  2. Restricted B-cell responses to microbial challenge of the respiratory tract. Walker, J., Lee, R., Mathy, N., Doughty, S., Conlon, J. Vet. Immunol. Immunopathol. (1996) [Pubmed]
  3. p-Nitrophenyl and cholesteryl-N-alkyl carbamates as inhibitors of cholesterol esterase. Hosie, L., Sutton, L.D., Quinn, D.M. J. Biol. Chem. (1987) [Pubmed]
  4. Structure of bovine pancreatic cholesterol esterase at 1.6 A: novel structural features involved in lipase activation. Chen, J.C., Miercke, L.J., Krucinski, J., Starr, J.R., Saenz, G., Wang, X., Spilburg, C.A., Lange, L.G., Ellsworth, J.L., Stroud, R.M. Biochemistry (1998) [Pubmed]
  5. Purification and characterization of bovine pancreatic bile salt-activated lipase. Tanaka, H., Mierau, I., Ito, F. J. Biochem. (1999) [Pubmed]
  6. Conventional antibody against Nepsilon-(carboxymethyl)lysine (CML) shows cross-reaction to Nepsilon-(carboxyethyl)lysine (CEL): immunochemical quantification of CML with a specific antibody. Koito, W., Araki, T., Horiuchi, S., Nagai, R. J. Biochem. (2004) [Pubmed]
  7. 12-[(5-iodo-4-azido-2-hydroxybenzoyl)amino]dodecanoic acid: biological recognition by cholesterol esterase and acyl-CoA:cholesterol O-acyltransferase. Kinnunen, P.M., Klopf, F.H., Bastiani, C.A., Gelfman, C.M., Lange, L.G. Biochemistry (1990) [Pubmed]
  8. Cholesterol transport function of pancreatic cholesterol esterase: directed sterol uptake and esterification in enterocytes. Lopez-Candales, A., Bosner, M.S., Spilburg, C.A., Lange, L.G. Biochemistry (1993) [Pubmed]
  9. Cholesterol esterase bound to intestinal brush border membranes does not accelerate incorporation of micellar cholesterol into absorptive cells. Ikeda, I., Mitsui, K., Matsuoka, R., Hamada, T., Imabayashi, S., Uchino, A., Yamada, K., Imaizumi, K. Biosci. Biotechnol. Biochem. (2003) [Pubmed]
  10. The crystal structure of bovine bile salt activated lipase: insights into the bile salt activation mechanism. Wang, X., Wang, C.S., Tang, J., Dyda, F., Zhang, X.C. Structure (1997) [Pubmed]
  11. Synthesis of tricyclic 1,3-oxazin-4-ones and kinetic analysis of cholesterol esterase and acetylcholinesterase inhibition. Pietsch, M., Gütschow, M. J. Med. Chem. (2005) [Pubmed]
  12. Pancreatic cholesterol esterases. 1. Pancreatic cholesterol esterase induction during maturation. Cox, D.G., Leung, C.K., Kyger, E.M., Spilburg, C.A., Lange, L.G. Biochemistry (1990) [Pubmed]
  13. Mass spectrometric characterization and glycosylation profile of bovine pancreatic bile salt-activated lipase. Wang, C.S., Jackson, K.W., Dashti, A., Downs, D., Zhang, X., Tang, J.J. Protein Expr. Purif. (1998) [Pubmed]
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