Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1
|
| pubmed:dateCreated |
1997-5-2
|
| pubmed:databankReference | |
| pubmed:abstractText |
Several enzymes in the glycolytic pathway are reported to have spermatogenic cell-specific isozymes. We reported recently the cloning of cDNAs representing three unique type 1 hexokinase mRNAs (mHk1-sa, mHk1-sb, and mHk1-sc) present only in mouse spermatogenic cells and the patterns of expression of these mRNAs (Mori et al., 1993: Biol Reprod 49:191-203). The mRNAs contain a spermatogenic cell-specific sequence, but lack the sequence for the porin-binding domain that somatic cell hexokinases use to bind to a pore-forming protein in the outer mitochondrial membrane. We now report the cloning of cDNAs representing three unique human type 1 hexokinase mRNAs (hHK1-ta, hHK1-tb, and hHK1-tc) expressed in testis, but not detected by Northern analysis in other human tissues. These mRNAs also contain a testis-specific sequence not present in somatic cell type 1 hexokinase, but lack the sequence for the porin-binding domain. The hHK1-tb and hHK1-tc mRNAs each contain an additional unique sequence. The testis-specific sequence of the human mRNAs is similar to the spermatogenic cell-specific sequence of the mouse mRNAs. Furthermore, Northern analysis of RNA from mouse, hamster, guinea pig, rabbit, ram, human, and rat demonstrated expression of type 1 hexokinase mRNAs lacking the porin-binding domain in the testes of these mammals. These results suggest that hexokinase may have unique structural or functional features in spermatogenic cells and support a model proposed by others for hexokinase gene evolution in mammals.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
May
|
| pubmed:issn |
1040-452X
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
44
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
14-22
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:8722688-Amino Acid Sequence,
pubmed-meshheading:8722688-Animals,
pubmed-meshheading:8722688-Base Sequence,
pubmed-meshheading:8722688-Binding Sites,
pubmed-meshheading:8722688-Cloning, Molecular,
pubmed-meshheading:8722688-Cricetinae,
pubmed-meshheading:8722688-DNA,
pubmed-meshheading:8722688-Gene Expression,
pubmed-meshheading:8722688-Guinea Pigs,
pubmed-meshheading:8722688-Hexokinase,
pubmed-meshheading:8722688-Humans,
pubmed-meshheading:8722688-Male,
pubmed-meshheading:8722688-Mice,
pubmed-meshheading:8722688-Molecular Sequence Data,
pubmed-meshheading:8722688-Porins,
pubmed-meshheading:8722688-RNA, Messenger,
pubmed-meshheading:8722688-Rabbits,
pubmed-meshheading:8722688-Rats,
pubmed-meshheading:8722688-Rats, Sprague-Dawley,
pubmed-meshheading:8722688-Sequence Homology, Amino Acid,
pubmed-meshheading:8722688-Sequence Homology, Nucleic Acid,
pubmed-meshheading:8722688-Testis
|
| pubmed:year |
1996
|
| pubmed:articleTitle |
Testis-specific expression of mRNAs for a unique human type 1 hexokinase lacking the porin-binding domain.
|
| pubmed:affiliation |
Department of Anatomy, Faculty of Medicine, Kyoto University, Japan.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|