|
rdf:type |
|
|
lifeskim:mentions |
umls-concept:C0007634,
umls-concept:C0017262,
umls-concept:C0017337,
umls-concept:C0019605,
umls-concept:C0086418,
umls-concept:C0185117,
umls-concept:C0205245,
umls-concept:C0221292,
umls-concept:C0440744,
umls-concept:C0936012,
umls-concept:C1519595,
umls-concept:C2911684
|
|
pubmed:issue |
2
|
|
pubmed:dateCreated |
1992-12-3
|
|
pubmed:databankReference |
|
|
pubmed:abstractText |
L-Histidine decarboxylase (HisDC) is the enzyme catalyzing the formation of histamine from L-histidine. HisDC activity is expressed specifically in mast cells/basophils, endocrine cells in stomach, and histaminergic neurons in brain. As a first step in the analysis of the regulation of HisDC gene expression, we have cloned the cDNA coding for HisDC from a cDNA library of a human basophilic leukemia cell line, KU-812-F. We identified two types of HisDC cDNA, representing the 2.4-kb and 3.4-kb HisDC mRNA constitutively expressed in these cells. Sequence analysis of these cDNA revealed that the 3.4-kb mRNA contains the insert sequence of 824 bases and suggests that both 2.4-kb and 3.4-kb mRNA may represent the alternatively spliced transcripts of the HisDC gene. Using expression plasmids containing a cDNA for each HisDC mRNA, we analyzed the function of possible HisDC isoforms. We show that only the 2.4-kb mRNA encodes functional HisDC and is expressed in human brain and lung. However, we were unable to detect the 3.4-kb mRNA in these tissues. Thus, the 3.4-kb mRNA may be generated by KU-812-F cell-specific splicing of the HisDC gene transcripts. Furthermore, we demonstrated the increase in the level of 2.4-kb HisDC mRNA and HisDC activity in KU-812-F cells following treatment with phorbol 12-myristate 13-acetate.
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Oct
|
|
pubmed:issn |
0014-2956
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
15
|
|
pubmed:volume |
209
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
533-9
|
|
pubmed:dateRevised |
2007-7-23
|
|
pubmed:meshHeading |
pubmed-meshheading:1425659-Alternative Splicing,
pubmed-meshheading:1425659-Amino Acid Sequence,
pubmed-meshheading:1425659-Animals,
pubmed-meshheading:1425659-Base Sequence,
pubmed-meshheading:1425659-Gene Expression,
pubmed-meshheading:1425659-Gene Library,
pubmed-meshheading:1425659-Histidine Decarboxylase,
pubmed-meshheading:1425659-Humans,
pubmed-meshheading:1425659-Leukemia, Basophilic, Acute,
pubmed-meshheading:1425659-Mice,
pubmed-meshheading:1425659-Molecular Sequence Data,
pubmed-meshheading:1425659-Molecular Weight,
pubmed-meshheading:1425659-Oligodeoxyribonucleotides,
pubmed-meshheading:1425659-Polymerase Chain Reaction,
pubmed-meshheading:1425659-RNA, Messenger,
pubmed-meshheading:1425659-Rats,
pubmed-meshheading:1425659-Restriction Mapping,
pubmed-meshheading:1425659-Sequence Homology, Amino Acid,
pubmed-meshheading:1425659-Transcription, Genetic,
pubmed-meshheading:1425659-Tumor Cells, Cultured
|
|
pubmed:year |
1992
|
|
pubmed:articleTitle |
Functional analysis of alternatively spliced transcripts of the human histidine decarboxylase gene and its expression in human tissues and basophilic leukemia cells.
|
|
pubmed:affiliation |
First Department of Internal Medicine, Tohoku University School of Medicine, Japan.
|
|
pubmed:publicationType |
Journal Article,
Comparative Study
|
