Abstract
The biogenic amine histamine is an important modulator of numerous physiological processes, including neurotransmitt-ance, gastric acid secretion and smooth muscle tone. The biosynthesis of histamine is catalyzed by the enzyme, L-histi-dine decarboxylase (HDC). We have previously reported the cloning and sequence of the cDNA encoding rat HDC. Utilizing the rat HDC cDNA as probe the full-length cDNA encoding human HDC was identified and characterized. The encoded protein of 662 amino acid residues has a molecular weight of 74,148. Homology comparisons of the deduced amino acid sequence with rat HDC and dopa decarboxylases from three species have revealed highly related regions. These comparisons have identified domains of amino acid decarboxylases that are highly conserved and are likely important for enzyme-substrate interaction. A dissimilar region in human and rat HDC primary translated protein near the C-terminus would appear not to be important for catalysis and may be removed by proteolysis. This processing phenomenon could be in part responsible for regulation of HDC activity. The human HDC cDNA was also utilized to map the chromosomal location of the human HDC gene locus (HDQ. Analysis of human-rodent cell hybrids revealed that the HDC gene segregates with Chromosome 15. No restriction length polymorphisms in the human population were detected after cleavage of the DNAs with 12 restriction endonucleases.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 395-400 |
| Number of pages | 6 |
| Journal | Mitochondrial DNA |
| Volume | 1 |
| Issue number | 6 |
| DOIs | |
| State | Published - 1991 |
| Externally published | Yes |
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Keywords
- CDNA
- Dopa decarboxylase
- Histamine
- Histidine decarboxylase
- Human
ASJC Scopus subject areas
- Genetics
- Molecular Biology
- Biochemistry
- Endocrinology
Cite this
Cloning of the cDNA encoding human histidine decarboxylase from an erythroleukemia cell line and mapping of the gene locus to chromosome 15. / Zahnow, Cynthia; Yi, Hua Fanc; Mcbride, O. Wesley; Joseph, David R.
In: Mitochondrial DNA, Vol. 1, No. 6, 1991, p. 395-400.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Cloning of the cDNA encoding human histidine decarboxylase from an erythroleukemia cell line and mapping of the gene locus to chromosome 15
AU - Zahnow, Cynthia
AU - Yi, Hua Fanc
AU - Mcbride, O. Wesley
AU - Joseph, David R.
PY - 1991
Y1 - 1991
N2 - The biogenic amine histamine is an important modulator of numerous physiological processes, including neurotransmitt-ance, gastric acid secretion and smooth muscle tone. The biosynthesis of histamine is catalyzed by the enzyme, L-histi-dine decarboxylase (HDC). We have previously reported the cloning and sequence of the cDNA encoding rat HDC. Utilizing the rat HDC cDNA as probe the full-length cDNA encoding human HDC was identified and characterized. The encoded protein of 662 amino acid residues has a molecular weight of 74,148. Homology comparisons of the deduced amino acid sequence with rat HDC and dopa decarboxylases from three species have revealed highly related regions. These comparisons have identified domains of amino acid decarboxylases that are highly conserved and are likely important for enzyme-substrate interaction. A dissimilar region in human and rat HDC primary translated protein near the C-terminus would appear not to be important for catalysis and may be removed by proteolysis. This processing phenomenon could be in part responsible for regulation of HDC activity. The human HDC cDNA was also utilized to map the chromosomal location of the human HDC gene locus (HDQ. Analysis of human-rodent cell hybrids revealed that the HDC gene segregates with Chromosome 15. No restriction length polymorphisms in the human population were detected after cleavage of the DNAs with 12 restriction endonucleases.
AB - The biogenic amine histamine is an important modulator of numerous physiological processes, including neurotransmitt-ance, gastric acid secretion and smooth muscle tone. The biosynthesis of histamine is catalyzed by the enzyme, L-histi-dine decarboxylase (HDC). We have previously reported the cloning and sequence of the cDNA encoding rat HDC. Utilizing the rat HDC cDNA as probe the full-length cDNA encoding human HDC was identified and characterized. The encoded protein of 662 amino acid residues has a molecular weight of 74,148. Homology comparisons of the deduced amino acid sequence with rat HDC and dopa decarboxylases from three species have revealed highly related regions. These comparisons have identified domains of amino acid decarboxylases that are highly conserved and are likely important for enzyme-substrate interaction. A dissimilar region in human and rat HDC primary translated protein near the C-terminus would appear not to be important for catalysis and may be removed by proteolysis. This processing phenomenon could be in part responsible for regulation of HDC activity. The human HDC cDNA was also utilized to map the chromosomal location of the human HDC gene locus (HDQ. Analysis of human-rodent cell hybrids revealed that the HDC gene segregates with Chromosome 15. No restriction length polymorphisms in the human population were detected after cleavage of the DNAs with 12 restriction endonucleases.
KW - CDNA
KW - Dopa decarboxylase
KW - Histamine
KW - Histidine decarboxylase
KW - Human
UR - http://www.scopus.com/inward/record.url?scp=0026265385&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0026265385&partnerID=8YFLogxK
U2 - 10.3109/10425179109020795
DO - 10.3109/10425179109020795
M3 - Article
C2 - 1768863
AN - SCOPUS:0026265385
VL - 1
SP - 395
EP - 400
JO - DNA Sequence - Journal of DNA Sequencing and Mapping
JF - DNA Sequence - Journal of DNA Sequencing and Mapping
SN - 1940-1744
IS - 6
ER -