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CD8+ T lymphocyte apoptosis is regul...

Van Dyken, Steven John.

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CD8+ T lymphocyte apoptosis is regulated by protein O-glycosylation.

Record Type:	Electronic resources : Monograph/item
Title/Author:	CD8+ T lymphocyte apoptosis is regulated by protein O-glycosylation./
Author:	Van Dyken, Steven John.
Description:	111 p.
Notes:	Source: Dissertation Abstracts International, Volume: 67-07, Section: B, page: 3692.
Contained By:	Dissertation Abstracts International67-07B.
Subject:	Health Sciences, Immunology. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3226770
ISBN:	9780542778100

CD8+ T lymphocyte apoptosis is regulated by protein O-glycosylation.
Van Dyken, Steven John.

CD8+ T lymphocyte apoptosis is regulated by protein O-glycosylation. - 111 p.

Source: Dissertation Abstracts International, Volume: 67-07, Section: B, page: 3692.

Thesis (Ph.D.)--University of California, San Diego, 2006.

Homeostasis is maintained after an immune response by apoptotic death of the majority of clonally expanded T cells. Evidence for the involvement of specific extracellular O-glycan modifications occurring during immune activation has previously emerged from analysis of CD8+ T cells deficient in ST3Gal-I, which express the activated O-glycan phenotype and undergo apoptosis in vivo in the absence of activation stimuli. The studies described in this dissertation further explore the influence of ST3Gal-I-mediated sialylation on CD8+ T cell apoptosis and the maintenance of homeostasis throughout immune responses produced in vitro and in vivo. To determine the effect of constitutive presence of ST3Gal-I on O-glycans production during immune activation, mice expressing an ST3Gal-I transgene in the T cell lineage were generated, characterized, and challenged with various immunologic stimuli. The specific involvement of potential mediators of CD8+ T cell apoptosis induced by ST3Gal-I deficiency was tested by analyzing double mutant mice. Finally, the mechanism of apoptosis was addressed by determining the involvement of intracellular signaling proteins Bcl-2 and Bim, which have been previously implicated in mediating CD8 + T cell apoptosis.

ISBN: 9780542778100Subjects--Topical Terms:

1017716
Health Sciences, Immunology.

CD8+ T lymphocyte apoptosis is regulated by protein O-glycosylation.
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100 1 $a Van Dyken, Steven John. $3 1919868
245 1 0 $a CD8+ T lymphocyte apoptosis is regulated by protein O-glycosylation.
300 $a 111 p.
500 $a Source: Dissertation Abstracts International, Volume: 67-07, Section: B, page: 3692.
500 $a Adviser: Jamey D. Marth.
502 $a Thesis (Ph.D.)--University of California, San Diego, 2006.
520 $a Homeostasis is maintained after an immune response by apoptotic death of the majority of clonally expanded T cells. Evidence for the involvement of specific extracellular O-glycan modifications occurring during immune activation has previously emerged from analysis of CD8+ T cells deficient in ST3Gal-I, which express the activated O-glycan phenotype and undergo apoptosis in vivo in the absence of activation stimuli. The studies described in this dissertation further explore the influence of ST3Gal-I-mediated sialylation on CD8+ T cell apoptosis and the maintenance of homeostasis throughout immune responses produced in vitro and in vivo. To determine the effect of constitutive presence of ST3Gal-I on O-glycans production during immune activation, mice expressing an ST3Gal-I transgene in the T cell lineage were generated, characterized, and challenged with various immunologic stimuli. The specific involvement of potential mediators of CD8+ T cell apoptosis induced by ST3Gal-I deficiency was tested by analyzing double mutant mice. Finally, the mechanism of apoptosis was addressed by determining the involvement of intracellular signaling proteins Bcl-2 and Bim, which have been previously implicated in mediating CD8 + T cell apoptosis.
520 $a These studies reveal novel mechanistic and structural features of apoptosis regulated by protein O-glycosylation, and a clear relationship to the post-immune contraction of CD8+ T cells. On wild-type CD8+ T cells, increased presence of unsialylated Core 1 O-glycans correlates with apoptosis and sensitizes them to in vitro apoptotic death induced by O-glycan crosslinking. Immune activation of ST3Gal-I transgenic CD8+ T cells reveals that unsialylated Core 1 O-glycans can be generated specifically on cells undergoing apoptotic death, by a post-transcriptional mechanism. This O-glycan-dependent CD8 T cell apoptosis does not act through CD43, Core 2 GlcNAcT-1-generated Core 2 O-glycan structures, or Galgt1-generated complex gangliosides. Furthermore, CD8+C cell apoptosis mediated by O-glycans does not rely on Bcl-2 levels, and can attenuate the in vivo accumulation of CD8+ T cells normally induced by the absence of Bcl2 family member Bim. Thus, these studies reveal novel mechanistic features of an essential physiologic mechanism of CD8+ T cell apoptosis that follows TCR stimulation and enables contraction upon immune signal attenuation.
590 $a School code: 0033.
650 4 $a Health Sciences, Immunology. $3 1017716
690 $a 0982
710 2 0 $a University of California, San Diego. $3 1018093
773 0 $t Dissertation Abstracts International $g 67-07B.
790 1 0 $a Marth, Jamey D., $e advisor
790 $a 0033
791 $a Ph.D.
792 $a 2006
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3226770