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Cadherin 2 bimodally regulates ECM a...

McMillen, Patrick Thomas.

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Cadherin 2 bimodally regulates ECM assembly through distinct and spatially non-overlapping mechanisms.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	Cadherin 2 bimodally regulates ECM assembly through distinct and spatially non-overlapping mechanisms./
作者:	McMillen, Patrick Thomas.
面頁冊數:	113 p.
附註:	Source: Dissertation Abstracts International, Volume: 76-11(E), Section: B.
Contained By:	Dissertation Abstracts International76-11B(E).
標題:	Developmental biology. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3663648
ISBN:	9781321957556

Cadherin 2 bimodally regulates ECM assembly through distinct and spatially non-overlapping mechanisms.
McMillen, Patrick Thomas.

Cadherin 2 bimodally regulates ECM assembly through distinct and spatially non-overlapping mechanisms. - 113 p.

Source: Dissertation Abstracts International, Volume: 76-11(E), Section: B.

Thesis (Ph.D.)--Yale University, 2015.

Scientists have been fascinated by the emergence of tissue form since the time of Aristotle. Recent advances in genetics, molecular biology and imaging are rapidly enabling us to study this process at a highly mechanistic level. In this thesis we extend the pioneering work of such early tissue biologists as Townes, Holtfreter and Steinberg by studying the function of differential adhesion within a self-assembling vertebrate tissue. Specifically, we employ a variety of quantitative imaging approaches to describe the function of the classical cell-cell adhesion protein Cadherin 2 during Zebrafish somitogenesis.

ISBN: 9781321957556Subjects--Topical Terms:

592588
Developmental biology.

Cadherin 2 bimodally regulates ECM assembly through distinct and spatially non-overlapping mechanisms.
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245 1 0 $a Cadherin 2 bimodally regulates ECM assembly through distinct and spatially non-overlapping mechanisms.
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500 $a Source: Dissertation Abstracts International, Volume: 76-11(E), Section: B.
500 $a Adviser: Scott Alan Holley.
502 $a Thesis (Ph.D.)--Yale University, 2015.
520 $a Scientists have been fascinated by the emergence of tissue form since the time of Aristotle. Recent advances in genetics, molecular biology and imaging are rapidly enabling us to study this process at a highly mechanistic level. In this thesis we extend the pioneering work of such early tissue biologists as Townes, Holtfreter and Steinberg by studying the function of differential adhesion within a self-assembling vertebrate tissue. Specifically, we employ a variety of quantitative imaging approaches to describe the function of the classical cell-cell adhesion protein Cadherin 2 during Zebrafish somitogenesis.
520 $a We identify a novel role for differential adhesion in somite morphogenesis. Surprisingly, we find that differential Cadherin 2 adhesion drives morphogenesis by stimulating extracellular matrix assembly. We find that this stimulation is partially redundant with activity of the Fibronectin receptor Intgerin alpha5, pointing to a fundamental functional convergence of these two very different adhesion regimes. We also describe a second, opposite role for Cadherin 2 in inhibiting ectopic mesenchymal extracellular matrix assembly. This role, too, is partially redundant with Integrin alpha5 activity, but functions through a distinct molecular mechanism from the stimulatory role. We thus conclude that Cadherin 2 is much more than a simple mediator of cell-cell adhesion, but rather is an important regulator of complex tissue level behaviors both within the mesenchyme and at tissue boundaries.
520 $a Finally, we describe ongoing work to integrate quantitative physical observations into our understanding of embryonic tissue assembly. We have generated a novel genetically encodable fluorescent stress probe that we are currently using to map the physical landscape of the forming somites.
590 $a School code: 0265.
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