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Investigation of phosphophoryn signa...

Carnegie Mellon University.

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Investigation of phosphophoryn signaling mechanisms as a model for ECM-directed morphogenesis of mineralized tissues.

Record Type:	Language materials, printed : Monograph/item
Title/Author:	Investigation of phosphophoryn signaling mechanisms as a model for ECM-directed morphogenesis of mineralized tissues./
Author:	Jadlowiec, Julie A.
Description:	235 p.
Notes:	Advisers: Phil Campbell; Charles Sfeir.
Contained By:	Dissertation Abstracts International66-09B.
Subject:	Biology, Animal Physiology. -
Online resource:	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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005 20110921
008 110921s2005 eng d
020 $a 9780542296130
035 $a (UnM)AAI3186031
035 $a AAI3186031
040 $a UnM $c UnM
100 1 $a Jadlowiec, Julie A. $3 1293982
245 1 0 $a Investigation of phosphophoryn signaling mechanisms as a model for ECM-directed morphogenesis of mineralized tissues.
300 $a 235 p.
500 $a Advisers: Phil Campbell; Charles Sfeir.
500 $a Source: Dissertation Abstracts International, Volume: 66-09, Section: B, page: 4580.
502 $a Thesis (Ph.D.)--Carnegie Mellon University, 2005.
520 $a 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.
590 $a School code: 0041.
650 4 $a Biology, Animal Physiology. $3 1017835
650 4 $a Biology, Cell. $3 1017686
690 $a 0379
690 $a 0433
710 2 0 $a Carnegie Mellon University. $3 1018096
773 0 $t Dissertation Abstracts International $g 66-09B.
790 $a 0041
790 1 0 $a Campbell, Phil, $e advisor
790 1 0 $a Sfeir, Charles, $e advisor
791 $a Ph.D.
792 $a 2005
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3186031