PMID- 10552930
OWN - NLM
STAT- MEDLINE
DCOM- 20000214
LR  - 20071114
IS  - 0888-7543 (Print)
IS  - 0888-7543 (Linking)
VI  - 61
IP  - 3
DP  - 1999 Nov 1
TI  - Human indolethylamine N-methyltransferase: cDNA cloning and expression, gene
      cloning, and chromosomal localization.
PG  - 285-97
AB  - Indolethylamine N-methyltransferase (INMT) catalyzes the N-methylation of
      tryptamine and structurally related compounds. We recently cloned and
      characterized the rabbit INMT cDNA and gene as a step toward cloning the cDNA and
      gene for this enzyme in humans. We have now used a PCR-based approach to clone a 
      human INMT cDNA that had a 792-bp open reading frame that encoded a
      263-amino-acid protein 88% identical in sequence to rabbit INMT. Northern blot
      analysis of 35 tissues showed that a 2.7-kb INMT mRNA species was expressed in
      most tissues. When the cDNA was expressed in COS-1 cells, the recombinant enzyme 
      catalyzed the methylation of tryptamine with an apparent K(m) value of 2.9 mM.
      The human cDNA was then used to clone the human INMT gene from a human genomic
      BAC library. The gene was 5471 bp in length, consisted of three exons, and was
      structurally similar to the rabbit INMT gene as well as genes for nicotinamide
      N-methyltransferase and phenylethanolamine N-methyltransferase in several
      species. All INMT exon-intron splice junctions conformed to the "GT-AG" rule, and
      no canonical TATA or CAAT sequences were present within the 5'-flanking region of
      the gene. Human INMT mapped to chromosome 7p15.2-p15.3 on the basis of both PCR
      analysis and fluorescence in situ hybridization. Finally, two possible single
      nucleotide polymorphisms were identified within exon 3, both of which altered the
      encoded amino acid. The cloning and expression of a human INMT cDNA, as well as
      the cloning, structural characterization, and mapping of its gene represent steps
      toward future studies of the function and regulation of this methyltransferase
      enzyme in humans.
CI  - Copyright 1999 Academic Press.
FAU - Thompson, M A
AU  - Thompson MA
AD  - Department of Pharmacology, Mayo Medical School/Mayo Clinic/Mayo Foundation,
      Rochester, Minnesota, 55905, USA.
FAU - Moon, E
AU  - Moon E
FAU - Kim, U J
AU  - Kim UJ
FAU - Xu, J
AU  - Xu J
FAU - Siciliano, M J
AU  - Siciliano MJ
FAU - Weinshilboum, R M
AU  - Weinshilboum RM
LA  - eng
SI  - GENBANK/AF128846
SI  - GENBANK/AF128847
SI  - GENBANK/AF128848
GR  - R01CA34936/CA/NCI NIH HHS/United States
GR  - R01GM28157/GM/NIGMS NIH HHS/United States
GR  - R01GM35720/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, Non-P.H.S.
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Genomics
JT  - Genomics
JID - 8800135
RN  - 0 (DNA Primers)
RN  - 0 (DNA, Complementary)
RN  - 0 (Recombinant Proteins)
RN  - EC 2.1.1.- (Methyltransferases)
RN  - EC 2.1.1.49 (tryptamine N-methyltransferase)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Base Sequence
MH  - Blotting, Northern
MH  - Blotting, Western
MH  - COS Cells
MH  - *Chromosome Mapping
MH  - *Cloning, Molecular
MH  - DNA Primers
MH  - DNA, Complementary/genetics
MH  - Humans
MH  - Methyltransferases/chemistry/*genetics/*metabolism
MH  - Molecular Sequence Data
MH  - Open Reading Frames/genetics
MH  - Rabbits
MH  - Recombinant Proteins/metabolism
MH  - Sequence Alignment
EDAT- 1999/11/24 09:00
MHDA- 2000/02/19 09:00
CRDT- 1999/11/24 09:00
PHST- 1999/11/24 09:00 [pubmed]
PHST- 2000/02/19 09:00 [medline]
PHST- 1999/11/24 09:00 [entrez]
AID - 10.1006/geno.1999.5960 [doi]
AID - S0888-7543(99)95960-8 [pii]
PST - ppublish
SO  - Genomics. 1999 Nov 1;61(3):285-97. doi: 10.1006/geno.1999.5960.