PL EN


Preferences help
enabled [disable] Abstract
Number of results
2010 | 64 | 3-4 | 48-57
Article title

Rola 7􀄮- hydroksylazy cholesterolu i genu CYP7A1 w fi zjologii i patologii człowieka

Content
Title variants
EN
Role of the cholesterol 7􀄮- hydroxylase and CYP7A1 gene in human physiology and pathology
Languages of publication
PL
Abstracts
EN
Cholesterol 7􀄮- hydroxylase (CYP7A1) belongs to the big family of cytochrome p450. Biological signifi cance of cholesterol 7􀄮- hydroxylase is associated with beginning of cholesterol transformation to the bile acids. CYP7A1 affi nity to the cholesterol is determined by its unique protein structure, diff erent from the other proteins of cytochrome p450 family. CYP7A1 enzyme is enoded by CYP7A1 gene localized in short arm of chromosome 8. Expression of CYP7A1 gene could be regulated by farnesoid X receptor (FXR) or by kinases, which modulate nuclear receptor`s binding abilities to the gene promoter. Polymorphic variants and mutations present in the promoter region impact on the quality properties of the enzyme. CYP7A1 gene, encoding key enzyme of the cholesterol catabolic pathway is a main candidate to the research of its association with changes of serum lipids levels. Presence of genetic variants can be associated with changed levels of total cholesterol, triglycerides and Low- density lipoproteins (LDL). Promoter polymorphism of CYP7A1 is also main candidate for the research of association with such disease entities as gallbladder stone formation, colon cancer, gallbladder cancer or atherogenic- based diseases.
PL
7􀄮- hydroksylaza cholesterolu (CYP7A1) jest enzymem należącym do dużej rodziny cytochromu p450. Znaczenie biologiczne 7􀄮- hydroksylazy cholesterolu związane jest z rozpoczęciem szeregu przemian cholesterolu do kwasów żółciowych. Powinowactwo CYP7A1 do cholesterolu determinowane jest unikalną budową białka, odmienną od reszty białek rodziny cytochromu p450. Enzym ten kodowany jest przez gen CYP7A1, którego locus znajduje się na ramieniu krótkim chromosomu ósmego. Ekspresja tego genu może być regulowana przy udziale farnezylowego receptora X (FXR), bądź zachodzić poprzez szereg kinaz białkowych, modulujących zdolność przyłączania się swoistych receptorów jądrowych do promotora CYP7A1. Warianty polimorfi czne i mutacje, występujące w regionie promotorowym, wpływają na właściwości jakościowe enzymu. Gen CYP7A1, kodując kluczowy enzym w katabolizmie cholesterolu, jest głównym kandydatem do badań jego związku ze zmianami w osoczowym poziomie lipoprotein. Obecność wariantów genetycznych w promotorze genu CYP7A1 może być związana ze zmienionym poziomem cholesterolu całkowitego, triacylogliceroli czy LDL (Low- Density Lipoprotein). Polimorfizm promotora genu kodującego kluczowy enzym szlaku syntezy kwasów żółciowych i usuwania cholesterolu z organizmu jest głównym kandydatem do badań asocjacyjnych z takimi jednostkami chorobowymi, jak kamica żółciowa, nowotwory jelita grubego i woreczka żółciowego czy choroby o podłożu miażdżycowym.
Discipline
Year
Volume
64
Issue
3-4
Pages
48-57
Physical description
References
  • 1. Russell D.W. The enzymes, regulation and genetics of bile acid synthesis Annu Rev Biochem. 2003;72:137-74.
  • 2. Björkhem I., Wikvall K., Araya Z., Rudling M., Angelin B., Einarsson C. Differences in the Regulation of the Classical and the Alternative Pathway for Bile Acid Synthesis in Human Liver. J. Biol. Chem. 2002; 277, 30:26804- 26807.
  • 3. Ogishima T., Deguchi S., Okuda K. Purifi cation and characterization of cholesterol 7a- hydroxylase from rat liver microsomes: J. Biol. Chem. 1987; 262:16 7646- 7650
  • 4. Nakayama K., Puchkaev K., Pikuleva I. Membrane Winding and substrate access merge in cytochrome p450 7A, a key enzyme in degradation of cholesterol J. Biol. Chem. 2001; 17,276(33):31459-65.
  • 5. Pikuleva I. Cholesterol- metabolizing cytochromes p450 Drug Metabolism and Disposition 2006; 34:513- 520.
  • 6. Noshiro M., Okuda K. Molecular cloning and sequence analysis of cDNA encoding human cholesterol 7􀄮- hydroxylase FEBS Lett. 1990; 268(1):137-40.
  • 7. Chiang J.Y.L. Bile acids: regulation and synthesis; J. Lipid Res. 2009; 50: 1955- 1966.
  • 8. Li T., Chiang J.Y.L. Regulation of bile acid and cholesterol metabolism by PPARs; PPAR Res. vol. 2009; ID- 501739.
  • 9. Li T., Chiang J.Y. Mechanism of Rifampicin and Pregnane X Receptor (PXR) inhibition of Human Cholesterol 7􀄮- Hydroxylase Gene Am J. Physiol. Gastrointest. Liver Physiol. 2004; 288:G74- G84.
  • 10. Miao J.S., Fang S., Bae Y., Kemper J.K. Functional inhibitory crosstalk between car and HNF-4 in hepatic lipid/glucose metabolism is mediated by competition for binding to the DR-1 motif and to the common coactivators, GRIP-1 and PGC-1 alpha. J. Biol. Chem. 2006; 281: 14537- 14546.
  • 11. Davis R., Miyake J.H., Hui T.Y., Spann N.J. Regulation of cholesterol-7􀄮- hydroxylase: BAREly missing SHP; J. Lipid. Res. 2002; 43: 533- 543.
  • 12. Li T., Jahan., A, Chiang J.Y.L. Bile acids and cytokines inhibit the human cholesterol 7-􀄮- hydroxylase gene via the JNK/cjun pathway in human liver cells: Hepatology 2006; 43: 1202- 1210.
  • 13. Holt J.A., Luo G., Billin A.N., Bisi J., McNeill Y.Y., Kozarsky K.F., Donahee M., Wang D.Y., Mansfi eld T.A., Kliewer S.A., Goodwin B,, Jones S.A. Deffi nition of novel gromth factor- dependent signal cascade for the suppression of bile acid biosynthesis: Gen. Develop. 2003; 17: 1581- 1591.
  • 14. Nakamoto K., Wang S., Jenison R.D, Guo G.L., Klaassen C.D., Wan Y-J Y., Zhong X-b Linkage disequilibrium blocks, haplotype structure, and htSNPs of human CYP7A1 gene BMC Genet. 2006; 7:29.
  • 15. Abrahamsson A., Krapivner S., Gustafsson U., Muhrbeck O., Eggertsen G., Johansson I., Persson I., Angelin B., Ingelman- Sundberg M., Björhem I., Einarsson C., van`t Hooft F.M. Common polymorphisms in the CYP7A1 gebe do not contribute to variation in the rates of the bile acids synthesis and plasma LDL cholesterol concentration Atherosclerosis 2005; 182:37-45.
  • 16. Leniček M., Komárek V., Zimolová M., Kovař J., Jirsa M., Lukaš M., Vitek L. CYP7A1 promoter polymorphism -203A/ C aff ects bile salt synthesis rate in the patients after ileal dissection J. Lipid Res. 2008; 49(12):2664-7.
  • 17. Pullinger C., Eng C., Salen G., Shefer S, Batta A.K., Erickson S.K., Verhagen A.G., Rivera C.R., Mulvihill SJ., Malloy MJ., Kane J.P. Human 7􀄮- hydroxylase (CYP7A1) defi ciency has a hypercholesterolemic phenotype J. Clin. Invest. 2002; 110:109-117.
  • 18. Couture P., Otvos J.D., Cupples A., Wilson P.W.F., Schaefer E.J., Ordovas J.M. Association of the A-204C cholesterol 7􀄮- hydroxylasegene with variations in plasma low density lipoprotein cholesterol levels in the Framingham Off spring Study J. Lipid Res. 1999 40: 1883- 1889.
  • 19. Hofman M., Princen H. M. G., Zwinderman A. H., Jukemans W. Genetic variation in the rate limiting enzyme I n cholesterol catabolism (cholesterol 7􀄮- hydroxylase) infl uences the progression of atherosclerosis and risk of new clinical events; Clin. Sci. 2005; 108; 539- 545.
  • 20. Kovař J., Suchanek P., Hubáček J.A., Poledne R. The A-204C polymorhism in the cholesterol 7alpha- hydroxylase determines in cholesterolemia responsiveness to a high- fat diet Physiol. Res. 2004; 53(5):565-8.
  • 21. Barcelos A.L.V., Chies R., Almeida S.E.M., Fiegenbaum M., Schweigert ID., Chula F.G.L., Rosetti M.L., Silva C.M.D Association of CYP7A1 -278A>C polymorphism and the response of plasma triglyceride after dietary intervention in dyslipidemic patients Braz J. Med. Biol. Res. 2009; 42: 487- 493.
  • 22. Hubácek J.A., Pistulková H., Skodová Z., Lánská V., Poledne R. Polymorhism in the regulatory part of cholesterol 7 alpha hydroxylase gene in the children with high and low levels of cholesterol Cas. Lek. Cesk. 2003;142(7):423-6.
  • 23. Jiang Z.Y., Han T.Q., Suo G.J., Feng D.X., Chen S., Cai X.X., Jiang Z.H., Shang J., Zhang Y., Jiang Y., Zhang S.D. Polymorphisms at cholesterol 7a-hydroxylase, apolipoproteins B and E and low density lipoprotein receptor genes in patients with gallbladder stone disease; World J. Gastroenterol. 2004; 10(10):1508-1512.
  • 24. Juzyszyn Z., Kurzawski M., Lener A., Modrzejewski A., Pawlik A., Droździk M. Cholesterol 7alpha-hydrolase (CYP7A1) c.- 278A>C promoter polymorphism in gallstone disease patients Genet. Test. 2008; 12(1):97-100.
  • 25. Srivastavaa A., Pandey S.N., Choudhuri G., Mittala B. Role of genetic variant A- 204C of cholesterol 7alpha-hydroxylase (CYP7A1) in susceptibility to gallbladder cancer. Mol Genet. Metab. 2008; 94(1):83-9.
  • 26. Misra S., Chaturvedi A., Misra N.C. and I.D. Sharma, Carcinoma of the gallbladder, Lancet Oncol 2003; 4: 167–176.
  • 27. Srivastavaa A., Choudhurib G., Mittala B. CYP7A1 (−204 A>C; rs3808607 and −469 T>C; rs3824260) promoter polymorphisms and risk of gallbladder cancer in North Indian population; Metabolism 14 December 2009.
  • 28. Milovic V., Teller I.C., Faust D., Caspary W.F., Stein J. Eff ects of deoxycholate on human colon cancer cells: apoptosis or proliferation. Eur. J. Clin. Invest. 2002; 32:29–34.
  • 29. Hagiwara T., Kono S., Yin G., Toyomura K., Nagano J., Mizoue T., Mibu R., Tanaka M., Kakeji Y., Maehara Y., Okamura T., Ikejiri K., Futami K., Yasunami Y., Maekawa T., Takenaka K., Ichimiya H., Imaizumi N., Genetic Polymorphism in Cytochrome P450 7A1 and Risk of Colorectal Cancer: The Fukuoka Colorectal Cancer Stud; Cancer Res. 2005; 65(7): 2979-82.
  • 30. Tabata S., Yin G., Ogawa S., Yamaguchi K., Mineshita M., Kono S. Genetic polymorphism of cholesterol 7alpha-hydroxylase (CYP7A1) and colorectal adenomas: Self Defense Forces Health Study; Cancer Sci. 2006; 97(5):406-10.
  • 31. Lambrinoudaki I.V., Kaparos G.I., Vlachou S.A., Stamatelopoulos K.S., Georgiopoulos G.A., Sergentanis T.N., Panoulis C.P., Christodoulakos G.E., Alexandrou A.P., Kouskouni E.E., Creatsa M.G., Papamichael C.M. CYP A-204C polymorphism is associated with subclinical atherosclerosis in postmenopausal women Menopause 2008; 5(6):1163-8.
Document Type
article
Publication order reference
YADDA identifier
bwmeta1.element.psjd-c25b8f4d-7888-40d9-8541-4313b0bec299
Identifiers
JavaScript is turned off in your web browser. Turn it on to take full advantage of this site, then refresh the page.