title: Mechanical strain effect on bone-resorbing activity and messenger RNA expressions of marker enzymes in isolated osteoclast culture.
abstract: Adaptive modeling and remodeling are controlled by the activities of osteoblasts and osteoclasts, which are capable of sensing their mechanical environments and regulating deposition or resorption of bone matrix. The effects of mechanical stimuli on isolated osteoclasts have been scarcely examined because it has proven to be difficult to prepare a number of pure osteoclasts and to cultivate them on mineralized substratum during mechanical stimulation. Recently, we developed an apparatus for applying mechanical stretching to the ivory slice/plastic plate component on which cells could be cultured. The loading frequency, strain rate, and generated strain over an ivory surface could be controlled by a personal computer. Using this apparatus, we examined the role of mechanical stretching on the bone-resorbing activity of the osteoclasts. Mature and highly enriched osteoclasts were cultured for 2, 12, and 24 h on the ivory/plate component while being subjected to intermittent tensile strain. The stretched osteoclasts showed enhanced messenger RNA (mRNA) expression levels of osteoclast marker enzymes, tartrate-resistant acid phosphatase (TRAP), and cathepsin K and increases of resorbed-pit formation, suggesting that the mechanical stretching up-regulated the bone-resorbing activity of the osteoclasts. A stretch-activated cation (SA-cat) channel blocker significantly inhibited the increases of the mRNA level and pit formation after 24 h of stretching. This study suggested the possibility that the mature osteoclasts responded to mechanical stretching through a mechanism involving a SA-cat channel in the absence of mesenchymal cells and, as a result, up-regulated their bone-resorbing activity.
authors.affiliation: Department of Intelligent Machinery and Systems, Graduate School of Engineering, Kyushu University, Fukuoka, Japan.
authors.forename: K
authors.initials: K
authors.lastname: Kurata
authors.forename: T
authors.initials: T
authors.lastname: Uemura
authors.forename: A
authors.initials: A
authors.lastname: Nemoto
authors.forename: T
authors.initials: T
authors.lastname: Tateishi
authors.forename: T
authors.initials: T
authors.lastname: Murakami
authors.forename: H
authors.initials: H
authors.lastname: Higaki
authors.forename: H
authors.initials: H
authors.lastname: Miura
authors.forename: Y
authors.initials: Y
authors.lastname: Iwamoto
mesh_terms: D000135:Acid Phosphatase / Q000096:biosynthesis* / Q000235:genetics; D000818:Animals; D015415:Biomarkers; D001862:Bone Resorption; D056657:Cathepsin K; D002403:Cathepsins / Q000096:biosynthesis* / Q000235:genetics; D002412:Cations / Q000378:metabolism; D002448:Cell Adhesion; D002478:Cells, Cultured; D004790:Enzyme Induction; D005682:Gadolinium / Q000494:pharmacology; D005786:Gene Expression Regulation; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000096:biosynthesis / Q000235:genetics; D007473:Ion Channels / Q000378:metabolism; D017136:Ion Transport; D007527:Isoenzymes / Q000096:biosynthesis* / Q000235:genetics; D010010:Osteoclasts / Q000378:metabolism*; D012333:RNA, Messenger / Q000096:biosynthesis*; D011817:Rabbits; D020133:Reverse Transcriptase Polymerase Chain Reaction; D013314:Stress, Mechanical; D000071681:Tartrate-Resistant Acid Phosphatase
chemical_list: D015415:Biomarkers; D002412:Cations; D007473:Ion Channels; D007527:Isoenzymes; D012333:RNA, Messenger; D005682:Gadolinium; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases; D000135:Acid Phosphatase; D000071681:Tartrate-Resistant Acid Phosphatase; D002403:Cathepsins; D056657:Cathepsin K