HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Prydz, K. Articles by Pedersen, J. I. Search for Related Content PubMed PubMed Citation Articles by Prydz, K. Articles by Pedersen, J. I. Social Bookmarking                      What's this?

Journal of Lipid Research, Vol 27, 622-628, Copyright © 1986 by Lipid Research, Inc.

ARTICLES

Formation of chenodeoxycholic acid from 3 alpha, 7 alpha-dihydroxy-5 beta-cholestanoic acid by rat liver peroxisomes

K Prydz, BF Kase, I Bjorkhem and JI Pedersen

The oxidation of the side chain of 3 alpha, 7 alpha-dihydroxy-5 beta- cholestanoic acid (DHCA) into chenodeoxycholic acid has been studied in subcellular fractions of rat liver. The product was separated from the substrate by high pressure liquid chromatography and identified by gas- liquid chromatography-mass spectrometry. The highest specific rate of conversion was found in the heavy (M) and the light (L) mitochondrial fractions with the highest enrichment in the L fraction. Washing the M fraction reduced the side chain cleavage activity by 90%. The peroxisomal marker enzyme urate oxidase was reduced to the same extent. The activity found in the M fraction may thus be due to peroxisomal contamination. After centrifugation of the L fraction on a Nycodenz density gradient, the highest specific activity for side chain cleavage of DHCA (31 nmol X mg-1 X h-1) was found in the fraction with the highest peroxisomal marker enzyme activity. This fraction also catalyzed conversion of 3 alpha,7 alpha,12 alpha-5 beta-cholestanoic acid (THCA) into cholic acid at the highest rate (32 nmol X mg-1 X h- 1). The peroxisomal oxidation of DHCA into chenodeoxycholic acid required the presence of ATP, CoA, Mg2+, and NAD in the incubation medium. The reaction was not inhibited by KCN. It is concluded that rat liver peroxisomes contain enzymes able to catalyze the cleavage of the side chain of both DHCA and THCA. The enzymes involved are similar to, but not necessarily identical to, those involved in the peroxisomal beta-oxidation of fatty acids.
CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				K. Solaas, B. F. Kase, V. Pham, K. Bamberg, M. C. Hunt, and S. E. H. Alexson Differential regulation of cytosolic and peroxisomal bile acid amidation by PPAR{alpha} activation favors the formation of unconjugated bile acids J. Lipid Res., June 1, 2004; 45(6): 1051 - 1060. [Abstract] [Full Text] [PDF]

				K. Solaas, A. Ulvestad, O. Söreide, and B. F. Kase Subcellular organization of bile acid amidation in human liver: a key issue in regulating the biosynthesis of bile salts J. Lipid Res., July 1, 2000; 41(7): 1154 - 1162. [Abstract] [Full Text]

				J. I. Pedersen, G. Eggertsen, U. Hellman, U. Andersson, and I. Bjorkhem Molecular Cloning and Expression of cDNA Encoding 3alpha ,7alpha ,12alpha -Trihydroxy-5beta -cholestanoyl-CoA Oxidase from Rabbit Liver J. Biol. Chem., July 18, 1997; 272(29): 18481 - 18489. [Abstract] [Full Text] [PDF]

				T. J. Kotti, K. Savolainen, H. M. Helander, A. Yagi, D. K. Novikov, N. Kalkkinen, E. Conzelmann, J. K. Hiltunen, and W. Schmitz In Mouse alpha -Methylacyl-CoA Racemase, the Same Gene Product Is Simultaneously Located in Mitochondria and Peroxisomes J. Biol. Chem., June 30, 2000; 275(27): 20887 - 20895. [Abstract] [Full Text] [PDF]

				M. C. Hunt, K. Solaas, B. F. Kase, and S. E. H. Alexson Characterization of an Acyl-CoA Thioesterase That Functions as a Major Regulator of Peroxisomal Lipid Metabolism J. Biol. Chem., January 4, 2002; 277(2): 1128 - 1138. [Abstract] [Full Text] [PDF]