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Investigation of phosphophoryn signa...
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Carnegie Mellon University.
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Investigation of phosphophoryn signaling mechanisms as a model for ECM-directed morphogenesis of mineralized tissues.
紀錄類型:
書目-語言資料,印刷品 : Monograph/item
正題名/作者:
Investigation of phosphophoryn signaling mechanisms as a model for ECM-directed morphogenesis of mineralized tissues./
作者:
Jadlowiec, Julie A.
面頁冊數:
235 p.
附註:
Advisers: Phil Campbell; Charles Sfeir.
Contained By:
Dissertation Abstracts International66-09B.
標題:
Biology, Animal Physiology. -
電子資源:
http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3186031
ISBN:
9780542296130
Investigation of phosphophoryn signaling mechanisms as a model for ECM-directed morphogenesis of mineralized tissues.
Jadlowiec, Julie A.
Investigation of phosphophoryn signaling mechanisms as a model for ECM-directed morphogenesis of mineralized tissues.
- 235 p.
Advisers: Phil Campbell; Charles Sfeir.
Thesis (Ph.D.)--Carnegie Mellon University, 2005.
The extracellular matrix (ECM) of bone/dentin is a unique microenvironment that provides spatial and temporal cues during tissue morphogenesis. Signals are relayed from the ECM to cells which interpret the stimuli into cell fate changes via intracellular signaling networks. The non-collagenous ECM protein, phosphophoryn (PP) regulates the mineral deposition phase of dentin presumably due to its highly acidic and anionic character. PP is a member of the SIBLING family of proteins and it is hypothesized that PP communicates with the cell via RGD/integrin interactions. The studies presented here define a signaling role for PP during cell differentiation of mineralized tissues. PP initiates changes in gene expression and cell phenotype in progenitor cells via integrin/MAPK signaling in fashion similar to BMP. PP also activates the Smad signaling pathway independently of BMP. PP synergizes with BMP to enhance marker gene expression and matrix mineralization. A potential mechanism for synergy may be through cross-talk between the MAPK and Smad pathways. PP therefore has two proposed functions: (1) As a regulator of mineral deposition and (2) As a signaling molecule that regulates cell differentiation and maintenance of the phenotype in mineralized tissues. The cross-talk between pathways suggests that PP may help to interpret multiple stimuli simultaneously from the ECM by signaling through a complex network of molecules. PP could be considered as a model ECM protein which regulates tissue morphogenesis.
ISBN: 9780542296130Subjects--Topical Terms:
1017835
Biology, Animal Physiology.
Investigation of phosphophoryn signaling mechanisms as a model for ECM-directed morphogenesis of mineralized tissues.
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The extracellular matrix (ECM) of bone/dentin is a unique microenvironment that provides spatial and temporal cues during tissue morphogenesis. Signals are relayed from the ECM to cells which interpret the stimuli into cell fate changes via intracellular signaling networks. The non-collagenous ECM protein, phosphophoryn (PP) regulates the mineral deposition phase of dentin presumably due to its highly acidic and anionic character. PP is a member of the SIBLING family of proteins and it is hypothesized that PP communicates with the cell via RGD/integrin interactions. The studies presented here define a signaling role for PP during cell differentiation of mineralized tissues. PP initiates changes in gene expression and cell phenotype in progenitor cells via integrin/MAPK signaling in fashion similar to BMP. PP also activates the Smad signaling pathway independently of BMP. PP synergizes with BMP to enhance marker gene expression and matrix mineralization. A potential mechanism for synergy may be through cross-talk between the MAPK and Smad pathways. PP therefore has two proposed functions: (1) As a regulator of mineral deposition and (2) As a signaling molecule that regulates cell differentiation and maintenance of the phenotype in mineralized tissues. The cross-talk between pathways suggests that PP may help to interpret multiple stimuli simultaneously from the ECM by signaling through a complex network of molecules. PP could be considered as a model ECM protein which regulates tissue morphogenesis.
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http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3186031
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