Acta Histochem Cytochem. 2009 Apr 28;42(2):55-64. doi: 10.1267/ahc.08012. Epub 2009 Apr 07.
Localization of adenylate kinase 4 in mouse tissues.
Acta histochemica et cytochemica
Keiko Miyoshi, Yuki Akazawa, Taigo Horiguchi, Takafumi Noma
Affiliations
Affiliations
- Department of Molecular Biology, Institute of Health Biosciences,The University of Tokushima Graduate School, 3-18-15 Kuramoto, Tokushima 770-8504, Japan.
PMID: 19492028
PMCID: PMC2685024 DOI: 10.1267/ahc.08012
Abstract
Adenylate kinase (AK) is a key enzyme in the high-energy phosphoryl transfer reaction in living cells. Of its isoforms, AK4 has a similar sequence and subcellular localization to that of AK3 in the mitochondrial matrix. However, unlike AK3, AK4 lacks the guanosine triphosphate: adenosine monophosphate phosphotransferase activity. To elucidate the physiological role of AK4, we explored the protein localization of AK4 in various mouse tissues by immunohistochemical analysis. AK4 protein was detected in the kidney, liver, brain, heart, stomach, intestine, and gonads but not in the lung and spleen. Interestingly, cell-type specific expression was evident in the brain, gastrointestinal tract, and gonads. In the cerebellum, AK4 was detected in granular cells but not in Purkinje cell bodies. In the gastrointestinal tract, AK4 was highly expressed in epithelia. In the ovary, AK4 was detected in oocytes and corpora lutea. In the testis, AK4 was detected in spermatocytes but not in spermatogonia. Our findings demonstrate that AK4 localizes uniquely in a cell-type and tissue-specific manner in mouse tissues.
Keywords: AK4; adenylate kinase; immunohistochemistry; mitochondria; protein expression
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