The disulfide linkage and the free sulfhydryl accessibility of acyl-coenzyme A:cholesterol acyltransferase 1 as studied by using mPEG 5000-maleimide

Biochemistry

Volumn 44, Issue 17, 2005, Pages 6537-6546

  Guo, Zhan Yun ^a   Chang, Catherine C Y ^a   Lu, Xiaohui ^a   Chen, Jiang ^b   Li, Bo Liang ^b   Chang, Ta Yuan ^a  

^a DARTMOUTH MEDICAL SCHOOL   (United States)

^b Shanghai Jiao Tong University Affiliated Sixth People s Hospital   (China)

Author keywords

[No Author keywords available]

Indexed keywords

CHEMICAL BONDS; ENZYMES; HUMAN ENGINEERING; HYDROPHOBICITY; POLYPEPTIDES; PROTEINS;

ACYL-COENZYME A:CHOLESTEROL ACYLTRANSFERASE (ACAT); DISULFIDE LINKAGE; ENDOPLASMIC RETICULUM (ER); MICROSOMAL VESICLES;

BIOCHEMISTRY;

CHOLESTEROL ACYLTRANSFERASE; DISULFIDE; DITHIOTHREITOL; HEMAGGLUTININ; IODOACETAMIDE; LYSINE; MACROGOL 5000; MACROGOL DERIVATIVE; MALEIMIDE; PROTEINASE; THIOL DERIVATIVE; UNCLASSIFIED DRUG;

ANIMAL CELL; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; CYTOPLASM; DENATURATION; DISULFIDE BOND; ENDOPLASMIC RETICULUM; FEMALE; HUMAN; HUMAN CELL; HYDROPHOBICITY; MICROSOME; MUTANT; NONHUMAN; POLYACRYLAMIDE GEL ELECTROPHORESIS; PREDICTION; PRIORITY JOURNAL; WESTERN BLOTTING; WILD TYPE;

ALANINE; ALKYLATING AGENTS; AMINO ACID SUBSTITUTION; ANIMALS; CELL LINE, TUMOR; CHO CELLS; CRICETINAE; CYSTEINE; DISULFIDES; HEMAGGLUTININS; HUMANS; HYDROLYSIS; MACROPHAGES; MALEIMIDES; METALLOENDOPEPTIDASES; PEPTIDE FRAGMENTS; POLYETHYLENE GLYCOLS; PROTEIN DENATURATION; RECOMBINANT PROTEINS; STEROL O-ACYLTRANSFERASE; SULFHYDRYL COMPOUNDS;

EID: 17844399790     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi047409b     Document Type: Article

References (39)

1. Chang, T. Y., Chang, C. C. Y., and Cheng, D. (1997) Acyl-coenzyme A:cholesterol acyltransferase, Annu. Rev. Biochem. 66, 613-638.
2. Chang, C. C. Y., Huh, H. Y., Cadigan, K. M., and Chang, T. Y. (1993) Molecular cloning and functional expression of human acyl-coenzyme A:cholesterol acyltransferase cDNA in mutant Chinese hamster ovary cells, J. Biol. Chem. 268, 20747-20755.
3. Anderson, R. A., Joyce, C., Davis, M., Reagan, J. W., Clark, M., Shelness, G. S., and Rudel, L. L. (1998) Identification of a form of acyl-CoA:cholesterol acyltransferase specific to liver and intestine in nonhuman primates, J. Biol. Chem. 273, 26747-26754.
4. Cases, S., Novak, S., Zheng, Y. W., Myers, H., Lear, S. R., Sande, E., Welch, C. B., Lusis, A. J., Spencer, T. A., Krause, B. R., Erickson, S. K., and Farese, R. V., Jr. (1998) ACAT-2, a second mammalian acyl-CoA:cholesterol acyltransferase. Its cloning, expression, and characterization, J. Biol. Chem. 273, 26755-26764.
5. Oelkers, P., Behari, A., Cromley, D., Billheimer, J. T., and Sturley, S. L. (1998) Characterization of two human genes encoding acyl coenzyme A:cholesterol acyltransferase-related enzymes, J. Biol. Chem. 273, 26756-26771.
6. Lee, O., Chang, C. C. Y., Lee, W., and Chang, T. Y. (1998) Immunodepletion experiments suggest that acyl-coenzyme A:cholesterol acyltransferase-1 (ACAT-1) plays a major catalytic role in adult human liver, adrenal gland, microphages, and kidney, but not in intestines, J. Lipid Res. 39, 1722-1727.
7. Sakashita, N., Miyazaki, A., Takeya, M., Horiuchi, S., Chang, C. C. Y., Chang, T. Y., and Takahashi, K. (2000) Localization of human acyl-coenzyme A:cholesterol acyltransferase-1 in microphages and in various tissues, Am. J. Pathol. 156, 227-236.
8. Chang, C. C. Y., Sakashita, N., Ornvold, K., Lee, O., Chang, E., Dong, R., Lin, S., Lee, C. Y. G., Strom, S., Kashyap, R., Fung, J., Farese, R. V., Jr., Patoiseau, J. F., Delhon, A., and Chang, T. Y. (2000) Immunological quantitation and localization of ACAT-1 and ACAT-2 in human liver and small intestine, J. Biol. Chem. 275, 28083-28092.
9. Sakashita, N., Miyazaki, A., Chang, C. C., Chang, T. Y., Kiyota, E., Satoh, M., Komohara, Y., Morganelli, P. M., Horiuchi, S., and Takeya, M. (2003) Acyl-coenzyme A:cholesterol acyltransferase 2 (ACAT2) is induced in monocyte-derived macrophages: in vivo and in vitro studies, Lab. Invest. 83, 1569-1581.
10. Parini, P., Davis, M., Lada, A. T., Erickson, S. K., Wright, T. L., Gustafsson, U., Sahlin, S., Einarsson, C., Eriksson, M., Angelin, B., Tomoda, H., Omura, S., Willingham, M. C., and Rudel, L. L. (2004) ACAT2 is localized to hepatocytes and is the major cholesterol-esterifying enzyme in human liver. Circulation 110, 2017-2023.
11. Ross, A. C., Go, K. J., Heider, J. G., and Rothblat, G. H. (1984) Selective inhibition of acyl conenzyme A:cholesterol acyltransferase by compound 58-035, J. Biol. Chem. 259, 185-189.
12. Bocan, T. M. A., Bak-Mueller, S., Uhlendorf, P. D., Newton, R. S., and Krause, B. R. (1991) Comparison of CI-976, an ACAT inhibitor, and selected lipid-lowering agents for antiatherosclerotic activity in iliac-femoral and thoracic aortic lesions: a biochemical, morphological and morphometric evaluation. Arterioscler. Thromb. 11, 1830-1943.
13. Alegret, M., Llaverias, G., and Silvestre, J. S. (2004) Acyl-coenzyme A:cholesterol acyltransferase inhibitors as hypolipidemic and antiatherosclerotic drugs. Methods Find. Exp. Clin. Pharmacol. 26, 563-586.
14. Chang, C. C. Y., Lee, C. Y. G., Chang, E. T., Cruz, J. C., Levesque, M. C., and Chang, T. Y. (1998) Recombinant human acyl-coenzyme A:cholesterol acyltransferase-1 (ACAT-1) purified to essential homogeneity utilizes cholesterol in mixed micelles or vesicles in a highly cooperative manner, J. Biol. Chem. 273, 35132-35141.
15. Lin, S., Cheng, D., Liu, M. S., Chen, J., and Chang, T. Y. (1999) Human acyl-CoA:cholesterol acyltransferase-1 in the endoplasmic reticulum contains seven transmembrane domains. J. Biol. Chem. 274, 23276-23285.
16. Joyce, C. W., Shelness, G. S., Davis, M. A., Lee, R. G., Skinner, K., Anderson, R. A., and Rudel, L. L. (2000) ACAT1 and ACAT2 membrane topology segregates a serine residue essential for activity to opposite sides of the endoplasmic reticulum membrane, Mol. Biol. Cell 11, 3675-3687.
17. Yu, C., Chen, J., Lin, S., Liu, J., Chang, C. C. Y., and Chang, T. Y. (1999) Human acyl-CoA:cholesterol acyltransferase-1 is a homotetrameric enzyme in intact cells and in vitro, J. Biol. Chem. 274, 36139-36145.
18. Yu, C., Zhang, Y., Lu, X. H., Chen, J., Chang, C. C. Y., and Chang, T. Y. (2002) The role of the N-terminal hydrophilic domain of acyl-coenzyme A:cholesterol acyltransferase 1 on the enzyme's quaternary structure and catalytic efficiency, Biochemistry 41, 3762-3769.
19. Zhang, Y., Yu, C., Liu, J., Spencer, T. A., Chang, C. C., and Chang, T. Y. (2003) Cholesterol is superior to 7-ketocholesterol or 7 alpha- hydroxycholesterol as an allosteric activator for acyl-coenzyme A:cholesterol acyltransferase 1, J. Biol. Chem. 278, 11642-11647.
20. Liu, J., Chang, C. C. Y., Westover, E. J., Covey, D. F., and Chang, T. Y. (2005) Investigating the allosterism of acyl coenzyme A:cholesterol acyltransferase (ACAT) by using various sterols: in vitro and intact cell studies (submitted for publication).
21. Kinnunen, P. M., DeMichele, A., and Lange, L. G. (1988) Chemical modification of acyl-CoA:cholesterol acyltransferase O-acyltransferase. 1. Identification of acyl-CoA:cholesterol acyl-transferase O-acyltransferase subtypes by differential diethyl pyrocarbonate sensitivity, Biochemistry 27, 7344-7350.
22. Kinnunen, P. M., DeMichele, A., and Lange, L. G. (1988) Chemical modification of acyl-CoA:cholesterol acyltransferase O-acyltransferase. 2. Identification of a coenzyme A regulatory site by p-mercuribenzoate modification, Biochemistry 27, 7351-7356.
23. Hofmann, K. (2000) A superfamily of membrane bound O-acyltransferase with implications for Wnt signaling, Trends Biochem. Sci. 25, 111-112.
24. Chang, T. Y., Chang, C. C., Lu, X., and Lin, S. (2001) Catalysis of ACAT may be completed within the plane of the membrane: a working hypothesis, J. Lipid Res. 42, 1933-1938.
25. Lin, S., Lu, X., Chang, C. C., and Chang, T. Y. (2003) Human acyl-coenzyme A:cholesterol acyltransferase expressed in Chinese hamster ovary cells: membrane topology and active site location, Mol. Biol. Cell 14, 2447-2460.
26. Lu, X. H., Lin, S., Chang, C. C. Y., and Chang, T. Y. (2002) Mutant acyl-coenzyme A:cholesterol acyltransferase 1 (ACAT1) devoid of cysteine residues remains catalytically active, J. Biol. Chem. 277, 711-718.
27. Cadigan, K. M., Heider, J. G., and Chang, T. Y. (1988) Isolation and characterization of Chinese hamster ovary cell mutants deficient in acyl-coenzyme A:cholesterol acyltransferase activity, J. Biol. Chem. 263, 274-282.
28. Yang, L., Lee, O., Chen, J., Chen, J., Chang, C. C., Zhou, P., Wang, Z. Z., Ma, H. H., Sha, H. F., Feng, J. X., Wang, Y., Yang, X. Y., Wang, L., Dong, R., Ornvold, K., Li, B. L., and Chang, T. Y. (2004) Human acyl-coenzyme A:Cholesterol acyltransferase 1 (acat1) sequences located in two different chromosomes (7 and 1) are required to produce a novel ACAT1 isoenzyme with additional sequence at the N-terminal, J. Biol. Chem. 279, 46253-46262.
29. Chang, C. C. Y., Doolittle, G. M., and Chang, T. Y. (1986) Cycloheximide-sensitivity in regulation of acyl-CoA:cholesterol acyltransferase activity in Chinese hamster ovary cells, Biochemistry 25, 1693-1699.
30. Chang, T. Y., Limanek, J. S., and Chang, C. C. Y. (1981) Evidence indicating that inactivation of 3-hydroxy-3-methylglutaryl coenzyme A reductase by low density lipoprotein or by 25-hydroxy-cholesterol requires mediator proteins with rapid turnover rate, Anal. Biochem. 116, 298-302.
31. Fernandez, S., Andrews, L., and Mische, S. M. (1993) An improved procedure for enzymatic digestion of polyvinylidene difluoride-bound proteins for internal sequence analysis, Anal. Biochem. 218, 112-117.
32. Schagger, H., and von Jagow, G. (1987) Tricine-sodium dodecyl sulfate-polyacrilamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa, Anal. Biochem. 166, 368-379.
33. Lu, J., and Deutsch, C. (2001) Pegylation: a method for assessing the topology accessibility in Kv1.3, Biochemistry 40, 13288-13301.
34. Hwang, C., Sinskey, A. J., and Lodish, H. F. (1992) Oxidized redox state of glutathione in the endoplasmic reticulum, Science 257, 1496-1502.
35. Bader, M., Muse, W., Ballon, D. P., Gassner, C., and Bardwell, J. C. A. (1999) Oxidative protein folding is driven by the electron transport system, Cell 98, 217-227.
36. Sevier, C. S., and Kaiser, C. A. (2002) Formation and transfer of disulfide bonds in living cells, Nat. Rev. Mol. Cell Biol. 3, 836-847.
37. Gross, E., Kastner, D. B., Kaiser, C. A., and Pass, D. (2004) Structure of Erolp, source of disulfide bonds for oxidative protein folding in the cell, Cell 117, 601-610.
38. + channel T1 recognition domain, J. Biol. Chem. 287, 4305-4313.
39. Katzen, F., and Beckwith, J. (2003) Role and location of the unusual redox-active cysteines in the hydrophobic domain of the transmembrane electron transporter DsbD, Proc. Natl. Acad. Sci. U.S.A. 100, 10471-10476.