NDLI: Human catechol-O-methyltransferase: cloning and expression of the membrane-associated form.

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Human catechol-O-methyltransferase: cloning and expression of the membrane-associated form.

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Human catechol-O-methyltransferase: cloning and expression of the membrane-associated form.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Dembic, Z. Malherbe, P. Bertocci, B. Da Prada, M. Lahm, H. W. Miggiano, V.
Description	Author Affiliation: Bertocci B ( Pharma Research Central Nervous System, F. Hoffman-La Roche Ltd, Basel, Switzerland.);
Abstract	A cDNA clone for human catechol-O-methyltransferase (hCOMT; S-adenosyl-L-methionine:catechol O-methyltransferase; EC 2.1.1.6) was isolated from a human hepatoma cell line (Hep G2) cDNA library by hybridization screening with a porcine cDNA probe. The cDNA clone was sequenced and found to have an insert of 1226 nucleotides. The deduced primary structure of hCOMT is composed of 271 amino acid residues with the predicted molecular mass of 30 kDa. At its N terminus it has a hydrophobic segment of 21 amino acid residues that may be responsible for insertion of hCOMT into the endoplasmic reticulum membrane. The primary structure of hCOMT exhibits high homology to the porcine partial cDNA sequence (93%). The deduced amino acid sequence contains two tryptic peptide sequences (T-22, T-33) found in porcine liver catechol-O-methyltransferase (COMT). The coding region of hCOMT cDNA was placed under the control of the cytomegalovirus promoter to transfect human kidney 293 cells. The endogenous COMT activity, which was approximately 9.98 units per mg of protein in the untransfected cells, increased to 206 units per mg of protein upon transfection with a plasmid containing the COMT cDNA. The COMT activity of recombinant protein was inhibited competitively (IC50 = 700 nM) by the selective COMT inhibitor Ro 40-7592. An anti-COMT monoclonal antibody recognized, on immunoblots, a major polypeptide with apparent molecular mass of 29 kDa, in reasonable agreement with the predicted molecular mass. The recombinant hCOMT was shown by immunoblot analysis to be mainly associated with the membrane fraction. RNA blot analysis revealed one COMT mRNA transcript of 1.4 kilobases in Hep G2 poly(A)+ RNA.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	4
Volume Number	88
Language	English
Publisher	National Academy of Sciences
Publisher Date	1991-03-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Catechol O-Methyltransferase Genetics Endoplasmic Reticulum Enzymology Isoenzymes Amino Acid Sequence Animals Carcinoma, Hepatocellular Cell Line Cloning, Molecular DNA, Neoplasm Isolation & Purification Gene Library Liver Liver Neoplasms Molecular Sequence Data Plasmids Protein Conformation Restriction Mapping Sequence Homology, Nucleic Acid Swine Transfection Comparative Study Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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