A1 Refereed original research article in a scientific journal
Inhibition of the osteoclast V-ATPase by small interfering RNAs
Authors: Hu YW, Nyman J, Muhonen P, Vaananen HK, Laitala-Leinonen T
Publisher: ELSEVIER SCIENCE BV
Publication year: 2005
Journal: FEBS Letters
Journal name in source: FEBS LETTERS
Journal acronym: FEBS LETT
Volume: 579
Issue: 22
First page : 4937
Last page: 4942
Number of pages: 6
ISSN: 0014-5793
DOI: https://doi.org/10.1016/j.febslet.2005.07.078
Abstract
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.
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