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Examination of RGD-dependent cell ad...

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Examination of RGD-dependent cell adhesion in the sea urchin embryo and the role of the ECM in specification of the endoderm.

Record Type:	Language materials, printed : Monograph/item
Title/Author:	Examination of RGD-dependent cell adhesion in the sea urchin embryo and the role of the ECM in specification of the endoderm./
Author:	Klinzing, David Charles.
Description:	91 p.
Notes:	Adviser: Susan G. Ernst.
Contained By:	Dissertation Abstracts International58-09B.
Subject:	Biology, Cell. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoeng/servlet/advanced?query=9807437
ISBN:	9780591577198

Examination of RGD-dependent cell adhesion in the sea urchin embryo and the role of the ECM in specification of the endoderm.
Klinzing, David Charles.

Examination of RGD-dependent cell adhesion in the sea urchin embryo and the role of the ECM in specification of the endoderm. - 91 p.

Adviser: Susan G. Ernst.

Thesis (Ph.D.)--Tufts University, 1997.

Endo16 is an extracellular matrix (ECM) molecule expressed specifically by the endodermal cells undergoing the movements of gastrulation in the sea urchin embryo. This large, multidomain protein has been shown to contain an RGD sequence, a known site of cell attachment to ECM proteins. I have examined the ability of the RGD sequence found within Endo16 to act as an adhesion ligand using RGD-containing peptides in a non-radioactive cell adhesion assay. I have found that the RGDI sequence of Endo16 inhibits cell adhesion in a concentration dependent manner and in a cell type specific manner. An RGDS peptide also inhibits cell adhesion, however relative to the RGDI peptide, the RGDS peptide has been found to have a greater ability to inhibit adhesion of cells from an ectoderm-enriched cell fraction. Using an antibody which recognizes vertebrate $\beta\sb1$ integrin, I have identified a cross-reacting protein in the sea urchin embryo and have demonstrated by affinity chromatography that this molecule binds to the Endo16 RGDI sequence. This is the first demonstration of a sea urchin protein that cross reacts with an antibody against a vertebrate $\beta$ integrin and of an integrin-RGD interaction in the sea urchin embryo.

ISBN: 9780591577198Subjects--Topical Terms:

1017686
Biology, Cell.

Examination of RGD-dependent cell adhesion in the sea urchin embryo and the role of the ECM in specification of the endoderm.
LDR:03017nam 2200301 a 45 001 858050
005 20100712
008 100712s1997 ||||||||||||||||| ||eng d
020 $a 9780591577198
035 $a (UMI)AAI9807437
035 $a AAI9807437
040 $a UMI $c UMI
100 1 $a Klinzing, David Charles. $3 1025076
245 1 0 $a Examination of RGD-dependent cell adhesion in the sea urchin embryo and the role of the ECM in specification of the endoderm.
300 $a 91 p.
500 $a Adviser: Susan G. Ernst.
500 $a Source: Dissertation Abstracts International, Volume: 58-09, Section: B, page: 4564.
502 $a Thesis (Ph.D.)--Tufts University, 1997.
520 $a Endo16 is an extracellular matrix (ECM) molecule expressed specifically by the endodermal cells undergoing the movements of gastrulation in the sea urchin embryo. This large, multidomain protein has been shown to contain an RGD sequence, a known site of cell attachment to ECM proteins. I have examined the ability of the RGD sequence found within Endo16 to act as an adhesion ligand using RGD-containing peptides in a non-radioactive cell adhesion assay. I have found that the RGDI sequence of Endo16 inhibits cell adhesion in a concentration dependent manner and in a cell type specific manner. An RGDS peptide also inhibits cell adhesion, however relative to the RGDI peptide, the RGDS peptide has been found to have a greater ability to inhibit adhesion of cells from an ectoderm-enriched cell fraction. Using an antibody which recognizes vertebrate $\beta\sb1$ integrin, I have identified a cross-reacting protein in the sea urchin embryo and have demonstrated by affinity chromatography that this molecule binds to the Endo16 RGDI sequence. This is the first demonstration of a sea urchin protein that cross reacts with an antibody against a vertebrate $\beta$ integrin and of an integrin-RGD interaction in the sea urchin embryo.
520 $a Gastrulation and formation of the endoderm in the sea urchin embryo is dependent on the formation of a mature, post-translationally modified ECM. Embryos in which collagen maturation has been disrupted by treatment with $\beta $a PN have been found to be developmentally arrested at the mesenchyme blastula stage and fail to undergo gastrulation. I have examined the specification of the endoderm in embryos treated with $\beta $a PN to determine if the failure of embryos to gastrulate is due to the absence of specified endoderm. Using Endo16 gene expression as a marker for endoderm specification, we have shown that within $\beta $a PN-treated embryos, Endo16/ is still expressed, suggesting that endoderm specification has taken place. Therefore, the inability to gastrulate is not due to the lack of a presumptive endoderm.
590 $a School code: 0234.
650 4 $a Biology, Cell. $3 1017686
650 4 $a Biology, Molecular. $3 1017719
650 4 $a Biology, Zoology. $3 1018632
690 $a 0307
690 $a 0379
690 $a 0472
710 2 $a Tufts University. $3 1017847
773 0 $t Dissertation Abstracts International $g 58-09B.
790 $a 0234
790 1 0 $a Ernst, Susan G., $e advisor
791 $a Ph.D.
792 $a 1997
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoeng/servlet/advanced?query=9807437