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Regulation of alpha 5/beta 1 integri...

Morrisey, Edward Eugene.

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Regulation of alpha 5/beta 1 integrin function by the cytoplasmic domain of the alpha 5 subunit.

Record Type:	Electronic resources : Monograph/item
Title/Author:	Regulation of alpha 5/beta 1 integrin function by the cytoplasmic domain of the alpha 5 subunit./
Author:	Morrisey, Edward Eugene.
Description:	230 p.
Notes:	Source: Dissertation Abstracts International, Volume: 56-03, Section: B, page: 1201.
Contained By:	Dissertation Abstracts International56-03B.
Subject:	Cellular biology. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=9521774

Regulation of alpha 5/beta 1 integrin function by the cytoplasmic domain of the alpha 5 subunit.
Morrisey, Edward Eugene.

Regulation of alpha 5/beta 1 integrin function by the cytoplasmic domain of the alpha 5 subunit. - 230 p.

Source: Dissertation Abstracts International, Volume: 56-03, Section: B, page: 1201.

Thesis (Ph.D.)--Northwestern University, 1994.

The integrin family of cell surface receptors is comprised of heterodimeric, transmembrane glycoproteins containing $\alpha$ and $\beta$ subunits. Integrins mediate adhesion of cells to the extracellular matrix as well as the cell surface ligands. These interactions play an important role in cell locomotion, proliferation, and differentiation. The $\alpha5\beta1$ integrin mediates adhesion of cells to the cell binding domain of fibronectin. This integrin can be post-translationally regulated and exists in a low or high activity state in several hematopoietic cells. Activity of the $\alpha5\beta1$ integrin can be increased by stimulating cells with phorbol esters.Subjects--Topical Terms:

3172791
Cellular biology.

Regulation of alpha 5/beta 1 integrin function by the cytoplasmic domain of the alpha 5 subunit.
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008 170521s1994 ||||||||||||||||| ||eng d
035 $a (MiAaPQ)AAI9521774
035 $a AAI9521774
040 $a MiAaPQ $c MiAaPQ
100 1 $a Morrisey, Edward Eugene. $3 3191560
245 1 0 $a Regulation of alpha 5/beta 1 integrin function by the cytoplasmic domain of the alpha 5 subunit.
300 $a 230 p.
500 $a Source: Dissertation Abstracts International, Volume: 56-03, Section: B, page: 1201.
500 $a Adviser: Robert Holmgren.
502 $a Thesis (Ph.D.)--Northwestern University, 1994.
520 $a The integrin family of cell surface receptors is comprised of heterodimeric, transmembrane glycoproteins containing $\alpha$ and $\beta$ subunits. Integrins mediate adhesion of cells to the extracellular matrix as well as the cell surface ligands. These interactions play an important role in cell locomotion, proliferation, and differentiation. The $\alpha5\beta1$ integrin mediates adhesion of cells to the cell binding domain of fibronectin. This integrin can be post-translationally regulated and exists in a low or high activity state in several hematopoietic cells. Activity of the $\alpha5\beta1$ integrin can be increased by stimulating cells with phorbol esters.
520 $a Using DNA sequence information from a previously characterized partial murine $\alpha5$ cDNA, the 5$\sp\prime$ two-thirds of the coding sequence was isolated and sequenced. The partial cDNAs were combined to generate a full length $\alpha5$ cDNA to use for stable transfection of the murine pre-B lymphoid cell line PD31. Analysis of the transfected clonal cell lines by FACScan and cell surface iodination demonstrated that the $\alpha5$ subunit dimerized with the $\beta1$ subunit and was expressed on the cell surface. Expression of $\alpha5$ in PD31 cells resulted in an $\alpha5\beta1$ integrin that exhibited low activity. However, when cells were stimulated with PMA, the $\alpha5\beta1$ integrin exhibited a higher activity. The role of the $\alpha5$ cytoplasmic domain in this PMA stimulated binding was investigated by mutagenesis. These studies demonstrated that the $\alpha5$ cytoplasmic domain is important for regulation of activity and in particular the tyrosine was found to be crucial for the PMA stimulated binding of transfected the PD31 cells to the cell binding domain of fibronectin.
520 $a Mutagenic analysis of the highly conserved GFFKR sequence found in all integrin $\alpha$ subunits revealed that this sequence was important for protein expression of the plasma membrane bound $\alpha5\beta1$ integrin but not a secreted form of the heterodimer. Finally, preliminary studies have shown that a 16-18 kilodalton protein binds to the $\beta1$ cytoplasmic domain. This system may be helpful in the future to characterize potential regulators of integrins.
590 $a School code: 0163.
650 4 $a Cellular biology. $3 3172791
650 4 $a Molecular biology. $3 517296
690 $a 0379
690 $a 0307
710 2 $a Northwestern University. $3 1018161
773 0 $t Dissertation Abstracts International $g 56-03B.
790 $a 0163
791 $a Ph.D.
792 $a 1994
793 $a English
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=9521774