Document Detail

Phosphorylated and non-phosphorylated forms of catechol O-methyltransferase in rat liver, brain and other tissues.
MedLine Citation:
PMID:  18831714     Owner:  NLM     Status:  MEDLINE    
Seven different forms of the enzyme COMT (catechol O-methyltransferase) were found in isolated rat hepatocytes by two-dimensional gel electrophoresis and immunoblotting: five small variants (S-COMT) and two large variants (L-COMT). The identities of these COMT forms were verified by tryptic fingerprinting using MALDI-TOF (matrix-assisted laser-desorption ionization-time-of-flight) MS, and by amino acid sequencing using ESI-IT-MS/MS (electrospray ionization with ion-trap tandem MS). Analysis of tissue distributions showed that the S-COMT forms were highly expressed in liver and kidney, whereas L-COMT was expressed more strongly in other tissues. Both of the L-COMT forms were found in all of the tissues examined except the heart, which expressed only the most acidic form, and the kidney, which expressed only the most basic form. Subcellular fractionation revealed the presence of both S-COMT and L-COMT in soluble, as well as sedimentable, fractions, suggesting that they should be classified by size rather than (as previously) by localization. Several of the S-COMT forms were N-acetylated, and the two most acidic forms were found to be phosphorylated at Ser(260). One of the latter was unique to liver cells; the other was also found in kidney, brain and thymus. Among the non-phosphorylated S-COMT forms, one was ubiquitous, one was found in testis and liver, and a third was found in liver, kidney and thymus. No other phosphorylated sites were found, suggesting that the pI differences distinguishing between the various COMT forms are due to some as yet unidentified structural modification(s).
Anders Øverbye; Per O Seglen
Related Documents :
8302944 - Metabolism of caffeic acid in the isolated perfused rat liver.
11022824 - Effect of branched-chain amino acids on the composition and cytolytic activity of liver...
623794 - Interrelation of aerobic glycolysis and lipogenesis in isolated perfused liver of well-...
3093134 - Palmitic acid oxidation and incorporation into triglyceride by needle liver biopsy spec...
16962614 - Inhibition of soluble epoxide hydrolase reduces lps-induced thermal hyperalgesia and me...
22355414 - Requirements for efficient proteolytic cleavage of prelamin a by zmpste24.
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  The Biochemical journal     Volume:  417     ISSN:  1470-8728     ISO Abbreviation:  Biochem. J.     Publication Date:  2009 Jan 
Date Detail:
Created Date:  2008-12-22     Completed Date:  2009-01-15     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  2984726R     Medline TA:  Biochem J     Country:  England    
Other Details:
Languages:  eng     Pagination:  535-45     Citation Subset:  IM    
Proteomics Section DNR, Department of Cell Biology, Institute for Cancer Research, The Norwegian Radium Hospital, Rikshospitalet University Hospital, Montebello, Oslo, Norway.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Amino Acid Sequence
Brain / enzymology*
Catechol O-Methyltransferase / chemistry,  metabolism*
Conserved Sequence
Electrophoresis, Gel, Two-Dimensional
Liver / enzymology*
Molecular Sequence Data
Organ Specificity
Rats, Wistar
Sequence Alignment
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Reg. No./Substance:
EC O-Methyltransferase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

Previous Document:  Isolation at physiological temperature of detergent-resistant membranes with properties expected of ...
Next Document:  Overview of advanced non-small-cell lung cancer treatment in Mexico.