Cloning and expression of vacuolar proton-pumping ATPase subunits in the follicular epithelium of the bullfrog endolymphatic sac
| Autor: | Shinya Yajima, Yuichi Sasayama, Shigeyasu Tanaka, Hideaki Tomura, Makoto Kubota, Masakazu Suzuki, Takahiro Hasegawa, Takashi Nakakura, Nobuto Katagiri |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2007 |
| Předmět: |
Vacuolar Proton-Translocating ATPases
DNA Complementary ATPase Blotting Western Molecular Sequence Data Fluorescent Antibody Technique Biology Epithelium Gene Expression Regulation Enzymologic Endolymphatic sac Vacuolar H+-pumping ATPase Bullfrog Complementary DNA medicine Animals Amino Acid Sequence Cloning Molecular chemistry.chemical_classification Anti-peptide antibody Rana catesbeiana Base Sequence Molecular mass Molecular biology Amino acid Blot Open reading frame medicine.anatomical_structure chemistry biology.protein cDNA cloning Animal Science and Zoology Immunocytochemistry |
| Zdroj: | Zoological Science. 24(2):147-157 |
| ISSN: | 0289-0003 |
| Popis: | 金沢大学環日本海域環境研究センター生物多様性研究部門 In an investigation aimed at clarifying the mechanism of crystal dissolution of the calcium carbonate lattice in otoconia (the mineral particles embedded in the otolithic membrane) of the endolymphatic sac (ELS) of the bullfrog, cDNAs encoding the A- and E-subunits of bullfrog vacuolar proton-pumping ATPase (V-ATPase) were cloned and sequenced. The cDNA of the A-subunit consisted of an 11-bp 5′-untranslated region (UTR), a 1,854-bp open reading frame (ORF) encoding a protein comprising 617 amino acids with a calculated molecular mass of 68,168 Da, and a 248-bp 3′-UTR followed by a poly(A) tail. The cDNA of the E-subunit consisted of a 72-bp 5′-UTR, a 681-bp ORF encoding a protein of 226 amino acids with a calculated molecular mass of 26,020 Da, and a 799-bp 3′-UTR followed by a poly(A) tail. Western blot and immunofluorescence analyses using specific anti-peptide antisera against the V-ATPase A- and E-subunits revealed that these subunits were present in the ELS, urinary bladder, skin, testes, and kidneys. In the ELS, positive cells were scattered in the follicular epithelium which, as revealed by electron microscopy, corresponds to the location of mitochondria-rich cells. These findings suggest that V-ATPase, including the A- and E-subunits, exists in mitochondria-rich cells of the ELS, which might be involved in dissolution of the calcium carbonate crystals in the lumen of the ELS. © 2007 Zoological Society of Japan. |
| Databáze: | OpenAIRE |
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