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Conference Paper: Uncovering functions of long-chain polyphosphate in higher eukaryotes: storage and synthesis of polyphosphate in matrix vesicles during mineralization

TitleUncovering functions of long-chain polyphosphate in higher eukaryotes: storage and synthesis of polyphosphate in matrix vesicles during mineralization
Authors
Issue Date2013
PublisherPan Pacific Connective Tissue Societies.
Citation
The 9th Pan Pacific Connective Tissue Societies Symposium (PPCTSS2013), Hong Kong, 24-27 November 2013. How to Cite?
AbstractInorganic polyphosphate (polyP) is a fundamental molecule that occurs throughout life. PolyP has been found in mammalian tissues with particularly high levels of polyP in bone and cartilage, however its metabolism and functions remain poorly understood. Here, we initially demonstrate the highest concentrations of polyP yet observed in a higher eukaryote in matrix vesicles (MVs) secreted from mineralized osteoblasts. We also observed that MVs isolated from both osteoblasts and chondrocytes have a remarkable ability to synthesize very long-chain polyP under physiological condition. PolyP could be hydrolysed to Pi by one of the critical enzymes of mineralization, tissue non-specific alkaline phosphatase (TNAP). PolyP was consumed during mineralization induced by MVs. Extravesicular PolyP acted as an efficient inhibitor to suppress MV-induced HA formation. Biochemical properties of polyP synthesis were consistent with membrane-bound enzyme activity within the MV. Taken together, our work introduces a new fundamental macromolecule that could be a critical modulator of mineralization in the extracellular matrix.
DescriptionSymposium Theme: The Extracellular Matrix Niche
Poster: abstract no. 0052
Persistent Identifierhttp://hdl.handle.net/10722/203818

 

DC FieldValueLanguage
dc.contributor.authorLi, Len_US
dc.contributor.authorLui, ELHen_US
dc.contributor.authorBuchet, Ren_US
dc.contributor.authorMebarek, Sen_US
dc.contributor.authorTanner, JAen_US
dc.date.accessioned2014-09-19T16:41:13Z-
dc.date.available2014-09-19T16:41:13Z-
dc.date.issued2013en_US
dc.identifier.citationThe 9th Pan Pacific Connective Tissue Societies Symposium (PPCTSS2013), Hong Kong, 24-27 November 2013.-
dc.identifier.urihttp://hdl.handle.net/10722/203818-
dc.descriptionSymposium Theme: The Extracellular Matrix Niche-
dc.descriptionPoster: abstract no. 0052-
dc.description.abstractInorganic polyphosphate (polyP) is a fundamental molecule that occurs throughout life. PolyP has been found in mammalian tissues with particularly high levels of polyP in bone and cartilage, however its metabolism and functions remain poorly understood. Here, we initially demonstrate the highest concentrations of polyP yet observed in a higher eukaryote in matrix vesicles (MVs) secreted from mineralized osteoblasts. We also observed that MVs isolated from both osteoblasts and chondrocytes have a remarkable ability to synthesize very long-chain polyP under physiological condition. PolyP could be hydrolysed to Pi by one of the critical enzymes of mineralization, tissue non-specific alkaline phosphatase (TNAP). PolyP was consumed during mineralization induced by MVs. Extravesicular PolyP acted as an efficient inhibitor to suppress MV-induced HA formation. Biochemical properties of polyP synthesis were consistent with membrane-bound enzyme activity within the MV. Taken together, our work introduces a new fundamental macromolecule that could be a critical modulator of mineralization in the extracellular matrix.-
dc.languageengen_US
dc.publisherPan Pacific Connective Tissue Societies.-
dc.relation.ispartof9th Pan Pacific Connective Tissue Societies Symposium Program Book-
dc.rightsCreative Commons: Attribution 3.0 Hong Kong License-
dc.titleUncovering functions of long-chain polyphosphate in higher eukaryotes: storage and synthesis of polyphosphate in matrix vesicles during mineralizationen_US
dc.typeConference_Paperen_US
dc.identifier.emailLi, L: linali@hku.hken_US
dc.identifier.emailTanner, JA: jatanner@hku.hken_US
dc.identifier.authorityTanner, JA=rp00495en_US
dc.description.naturepostprint-
dc.identifier.hkuros238507en_US

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