A1 Vertaisarvioitu alkuperäisartikkeli tieteellisessä lehdessä
Inhibition of the osteoclast V-ATPase by small interfering RNAs
Tekijät: Hu YW, Nyman J, Muhonen P, Vaananen HK, Laitala-Leinonen T
Kustantaja: ELSEVIER SCIENCE BV
Julkaisuvuosi: 2005
Journal: FEBS Letters
Tietokannassa oleva lehden nimi: FEBS LETTERS
Lehden akronyymi: FEBS LETT
Vuosikerta: 579
Numero: 22
Aloitussivu: 4937
Lopetussivu: 4942
Sivujen määrä: 6
ISSN: 0014-5793
DOI: https://doi.org/10.1016/j.febslet.2005.07.078
Tiivistelmä
The multisubunit enzyme V-ATPase harbours isoforms of individual subunits. a3 is one of four 116 kDa subunit a isoforms, and it is crucial for bone resorption. We used small interfering RNA (siRNA) molecules to knock down a3 in rat osteoclast cultures. Labeled siRNA-molecules entered osteoclasts via endocytosis and knocked down the a3 mRNA. Bone resorption was decreased in siRNA-treated samples due to decreased acidification and osteoclast inactivation. Expression of at did not respond to decreased a3 levels, suggesting that a1 does not compensate for a3 in osteoclast cultures. Subunit a3 is thus an interesting target for novel nucleic acid therapy. (c) 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
The multisubunit enzyme V-ATPase harbours isoforms of individual subunits. a3 is one of four 116 kDa subunit a isoforms, and it is crucial for bone resorption. We used small interfering RNA (siRNA) molecules to knock down a3 in rat osteoclast cultures. Labeled siRNA-molecules entered osteoclasts via endocytosis and knocked down the a3 mRNA. Bone resorption was decreased in siRNA-treated samples due to decreased acidification and osteoclast inactivation. Expression of at did not respond to decreased a3 levels, suggesting that a1 does not compensate for a3 in osteoclast cultures. Subunit a3 is thus an interesting target for novel nucleic acid therapy. (c) 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.