Osteoclastogenesis is negatively regulated by D‐serine produced by osteoblasts
Identifieur interne : 000246 ( Main/Exploration ); précédent : 000245; suivant : 000247Osteoclastogenesis is negatively regulated by D‐serine produced by osteoblasts
Auteurs : Takeshi Takarada [Japon] ; Mika Takarada-Iemata [Japon] ; Yoshifumi Takahata [Japon] ; Daisuke Yamada [Japon] ; Tomomi Yamamoto [Japon] ; Yukari Nakamura [Japon] ; Eiichi Hinoi [Japon] ; Yukio Yoneda [Japon]Source :
- Journal of Cellular Physiology [ 0021-9541 ] ; 2012-10.
English descriptors
- Teeft :
- 3pgdh, Amem, Amino, Amino acid transporter, Ascorbic acid, Asct2, Assay, Atb0, Binding site, Biochem biophys, Biol chem, Bone cells, Bone marrows, Calvarial, Calvarial osteoblasts, Cell lysates, Cells transfected, Cellular, Cellular differentiation, Cellular physiology, Chondrocytes, Common primers, Concentration range, Consecutive days, Constitutive expression, Control sirna, Control value, Culture medium, Culture period, Culture periods, Cultured, Cultured osteoblasts, Cultured osteoclasts, Extracellular, Functional expression, Further culture, Glutamate, Gure, Hinoi, Kanazawa, Kanazawa university graduate school, Luciferase, Luciferase activity, Master regulator, Mature osteoclasts, Medium change, Metabotropic glutamate receptors, Mouse osteoclasts, Mrna, Mrna expression, Mrna levels, Multinucleated cells, Neonatal rats, Nmdar, Nrf2, Nuclear factor, Online version, Osteoblast, Osteoblastic, Osteoblastic cells, Osteoclast, Osteoclastic, Osteoclastic cells, Osteoclastic differentiation, Osteoclastogenesis, Oxidative, Oxidative stress, Physiology, Positive control, Primer, Proc natl acad, Promoter, Quantitative data, Rankl, Real time, Receptor, Recombinant, Room temperature, Runx2, Serine, Serine racemase, Similar results, Sirna, Subsequent determination, Subunit, Takarada, Tibial sections, Transcription, Transcription factor, Transfected, Transporter, Trap staining, Trophic, Typical pictures, Wang, Yoneda.
Abstract
We have shown the functional expression by chondrocytes of serine racemase (SR) which is responsible for the synthesis of D‐serine (Ser) from L‐Ser in cartilage. In this study, we evaluated the possible functional expression of SR by bone‐forming osteoblasts and bone‐resorbing osteoclasts. Expression of SR mRNA was seen in osteoblasts localized at the cancellous bone surface in neonatal rat tibial sections and in cultured rat calvarial osteoblasts endowed to release D‐Ser into extracellular medium, but not in cultured osteoclasts differentiated from murine bone marrow progenitor cells. Sustained exposure to D‐Ser failed to significantly affect alkaline phosphatase activity and Ca2+ accumulation in cultured osteoblasts, but significantly inhibited differentiation and maturation in a concentration‐dependent manner at a concentration range of 0.1–1 mM without affecting cellular survival in cultured osteoclasts. By contrast, L‐Ser promoted osteoclastic differentiation in a manner sensitive to the inhibition by D‐Ser. Matured osteoclasts expressed mRNA for the amino acid transporter B0,+ (ATB0,+) and the system alanine, serine, and cysteine amino acid transporter‐2 (ASCT2), which are individually capable of similarly incorporating extracellular L‐ and D‐Ser. Knockdown of these transporters by siRNA prevented both the promotion by L‐Ser and the inhibition by D‐Ser of osteoclastic differentiation in pre‐osteoclastic RAW264.7 cells. These results suggest that D‐Ser may play a pivotal role in osteoclastogenesis through a mechanism related to the incorporation mediated by both ATB0,+ and ASCT2 of serine enantiomers in osteoclasts after the synthesis and subsequent release from adjacent osteoblasts. J. Cell. Physiol. 227: 3477–3487, 2012. © 2012 Wiley Periodicals, Inc.
Url:
DOI: 10.1002/jcp.24048
Affiliations:
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Division of Pharmaceutical Sciences, Kanazawa University Graduate School of Natural Science and Technology, Kanazawa, Ishikawa</wicri:regionArea><wicri:noRegion>Ishikawa</wicri:noRegion></affiliation><affiliation wicri:level="1"><country xml:lang="fr">Japon</country><wicri:regionArea>Laboratory of Molecular Pharmacology, Division of Pharmaceutical Sciences, Kanazawa University Graduate School of Natural Science and Technology, Kakuma‐machi, Kanazawa, Ishikawa 920‐1192</wicri:regionArea><wicri:noRegion>Ishikawa 920‐1192</wicri:noRegion></affiliation></author></analytic><monogr></monogr><series><title level="j">Journal of Cellular Physiology</title><title level="j" type="abbrev">J. Cell. Physiol.</title><idno type="ISSN">0021-9541</idno><idno type="eISSN">1097-4652</idno><imprint><publisher>Wiley Subscription Services, Inc., A Wiley Company</publisher><pubPlace>Hoboken</pubPlace><date type="published" when="2012-10">2012-10</date><biblScope unit="volume">227</biblScope><biblScope unit="issue">10</biblScope><biblScope unit="page" from="3477">3477</biblScope><biblScope unit="page" to="3487">3487</biblScope></imprint><idno type="ISSN">0021-9541</idno></series><idno type="istex">8F6A5DF9557368A616CDEF8EBFB40511B32E56E9</idno><idno type="DOI">10.1002/jcp.24048</idno><idno type="ArticleID">JCP24048</idno></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0021-9541</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>3pgdh</term><term>Amem</term><term>Amino</term><term>Amino acid transporter</term><term>Ascorbic acid</term><term>Asct2</term><term>Assay</term><term>Atb0</term><term>Binding site</term><term>Biochem biophys</term><term>Biol chem</term><term>Bone cells</term><term>Bone marrows</term><term>Calvarial</term><term>Calvarial osteoblasts</term><term>Cell lysates</term><term>Cells transfected</term><term>Cellular</term><term>Cellular differentiation</term><term>Cellular physiology</term><term>Chondrocytes</term><term>Common primers</term><term>Concentration range</term><term>Consecutive days</term><term>Constitutive expression</term><term>Control sirna</term><term>Control value</term><term>Culture medium</term><term>Culture period</term><term>Culture periods</term><term>Cultured</term><term>Cultured osteoblasts</term><term>Cultured osteoclasts</term><term>Extracellular</term><term>Functional expression</term><term>Further culture</term><term>Glutamate</term><term>Gure</term><term>Hinoi</term><term>Kanazawa</term><term>Kanazawa university graduate school</term><term>Luciferase</term><term>Luciferase activity</term><term>Master regulator</term><term>Mature osteoclasts</term><term>Medium change</term><term>Metabotropic glutamate receptors</term><term>Mouse osteoclasts</term><term>Mrna</term><term>Mrna expression</term><term>Mrna levels</term><term>Multinucleated cells</term><term>Neonatal rats</term><term>Nmdar</term><term>Nrf2</term><term>Nuclear factor</term><term>Online version</term><term>Osteoblast</term><term>Osteoblastic</term><term>Osteoblastic cells</term><term>Osteoclast</term><term>Osteoclastic</term><term>Osteoclastic cells</term><term>Osteoclastic differentiation</term><term>Osteoclastogenesis</term><term>Oxidative</term><term>Oxidative stress</term><term>Physiology</term><term>Positive control</term><term>Primer</term><term>Proc natl acad</term><term>Promoter</term><term>Quantitative data</term><term>Rankl</term><term>Real time</term><term>Receptor</term><term>Recombinant</term><term>Room temperature</term><term>Runx2</term><term>Serine</term><term>Serine racemase</term><term>Similar results</term><term>Sirna</term><term>Subsequent determination</term><term>Subunit</term><term>Takarada</term><term>Tibial sections</term><term>Transcription</term><term>Transcription factor</term><term>Transfected</term><term>Transporter</term><term>Trap staining</term><term>Trophic</term><term>Typical pictures</term><term>Wang</term><term>Yoneda</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">We have shown the functional expression by chondrocytes of serine racemase (SR) which is responsible for the synthesis of D‐serine (Ser) from L‐Ser in cartilage. In this study, we evaluated the possible functional expression of SR by bone‐forming osteoblasts and bone‐resorbing osteoclasts. Expression of SR mRNA was seen in osteoblasts localized at the cancellous bone surface in neonatal rat tibial sections and in cultured rat calvarial osteoblasts endowed to release D‐Ser into extracellular medium, but not in cultured osteoclasts differentiated from murine bone marrow progenitor cells. Sustained exposure to D‐Ser failed to significantly affect alkaline phosphatase activity and Ca2+ accumulation in cultured osteoblasts, but significantly inhibited differentiation and maturation in a concentration‐dependent manner at a concentration range of 0.1–1 mM without affecting cellular survival in cultured osteoclasts. By contrast, L‐Ser promoted osteoclastic differentiation in a manner sensitive to the inhibition by D‐Ser. Matured osteoclasts expressed mRNA for the amino acid transporter B0,+ (ATB0,+) and the system alanine, serine, and cysteine amino acid transporter‐2 (ASCT2), which are individually capable of similarly incorporating extracellular L‐ and D‐Ser. Knockdown of these transporters by siRNA prevented both the promotion by L‐Ser and the inhibition by D‐Ser of osteoclastic differentiation in pre‐osteoclastic RAW264.7 cells. These results suggest that D‐Ser may play a pivotal role in osteoclastogenesis through a mechanism related to the incorporation mediated by both ATB0,+ and ASCT2 of serine enantiomers in osteoclasts after the synthesis and subsequent release from adjacent osteoblasts. J. Cell. Physiol. 227: 3477–3487, 2012. © 2012 Wiley Periodicals, Inc.</div></front></TEI><affiliations><list><country><li>Japon</li></country></list><tree><country name="Japon"><noRegion><name sortKey="Takarada, Takeshi" sort="Takarada, Takeshi" uniqKey="Takarada T" first="Takeshi" last="Takarada">Takeshi Takarada</name></noRegion><name sortKey="Hinoi, Eiichi" sort="Hinoi, Eiichi" uniqKey="Hinoi E" first="Eiichi" last="Hinoi">Eiichi Hinoi</name><name sortKey="Nakamura, Yukari" sort="Nakamura, Yukari" uniqKey="Nakamura Y" first="Yukari" last="Nakamura">Yukari Nakamura</name><name sortKey="Takahata, Yoshifumi" sort="Takahata, Yoshifumi" uniqKey="Takahata Y" first="Yoshifumi" last="Takahata">Yoshifumi Takahata</name><name sortKey="Takarada Emata, Mika" sort="Takarada Emata, Mika" uniqKey="Takarada Emata M" first="Mika" last="Takarada-Iemata">Mika Takarada-Iemata</name><name sortKey="Yamada, Daisuke" sort="Yamada, Daisuke" uniqKey="Yamada D" first="Daisuke" last="Yamada">Daisuke Yamada</name><name sortKey="Yamamoto, Tomomi" sort="Yamamoto, Tomomi" uniqKey="Yamamoto T" first="Tomomi" last="Yamamoto">Tomomi Yamamoto</name><name sortKey="Yoneda, Yukio" sort="Yoneda, Yukio" uniqKey="Yoneda Y" first="Yukio" last="Yoneda">Yukio Yoneda</name><name sortKey="Yoneda, Yukio" sort="Yoneda, Yukio" uniqKey="Yoneda Y" first="Yukio" last="Yoneda">Yukio Yoneda</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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