Mouse and human granzyme B have distinct tetrapeptide specificities and abilities to recruit the bid pathway.

Mouse and human granzyme B have distinct tetrapeptide specificities and abilities to recruit the bid pathway. Research Abstract Details 

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Mouse and human granzyme B have distinct tetrapeptide specificities and abilities to recruit the bid pathway. Abstract Text:

Livia Casciola-Rosen,Margarita Garcia-Calvo,Herbert G Bull,Joseph W Becker,Tonie Hines,Nancy A Thornberry,Antony Rosen,

Granzyme B is an important mediator of cytotoxic lymphocyte granule-induced death of target cells, accomplishing this through cleavage of Bid and cleavage and activation of caspases as well as direct cleavage of downstream substrates. Significant controversy exists regarding the primary pathways used by granzyme B to induce cell death, perhaps arising from the use of different protease/substrate combinations in different studies. The primary sequence of human, rat, and mouse granzymes B is well conserved, and the substrate specificity and crystal structure of the human and rat proteases are extremely similar. Although little is known about the substrate specificity of mouse granzyme B, recent studies suggest that it may differ significantly from the human protease. In these studies we show that the specificities of human and mouse granzymes B differ significantly. Human and mouse granzyme B cleave species-specific procaspase-3 more efficiently than the unmatched substrates. The distinct specificities of human and mouse granzyme B highlight a previously unappreciated requirement for Asp(192) in the acquisition of catalytic activity upon cleavage of procaspase-3 at Asp(175). Although human granzyme B efficiently cleaves human or mouse Bid, these substrates are highly resistant to cleavage by the mouse protease, strongly indicating that the Bid pathway is not a major primary mediator of the effects of mouse granzyme B. These studies provide important insights into the substrate specificity and function of the granzyme B pathway in different species and highlight that caution is essential when designing and interpreting experiments with different forms of granzyme B.

Mouse and human granzyme B have distinct tetrapeptide specificities and abilities to recruit the bid pathway. Publishing Authors By Initials

L Casciola-Rosen,M Garcia-Calvo,HG Bull,JW Becker,T Hines,NA Thornberry,A Rosen,

For similar cells: blood cells: leukocytes: leukocytes, mononuclear: lymphocytes: t-lymphocytes: cd8-positive t-lymphocytes: t-lymphocytes, cytotoxic research abstracts see: cells: blood cells: leukocytes: leukocytes, mononuclear: lymphocytes: t-lymphocytes: cd8-positive t-lymphocytes: t-lymphocytes, cytotoxic research

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Mouse and human granzyme B have distinct tetrapeptide specificities and abilities to recruit the bid pathway. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: The Journal of biological chemistry

VOLUME: 282

Page Numbers: 4545-52

Journal Abbreviation: J. Biol. Chem.

ISSN: 0021-9258

DAY: 19

MONTH: 12

YEAR: 2006

Mouse and human granzyme B have distinct tetrapeptide specificities and abilities to recruit the bid pathway. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 2985121

Mouse and human granzyme B have distinct tetrapeptide specificities and abilities to recruit the bid pathway. Keywords Mesh Terms:

KEYWORDS: T-Lymphocytes, Cytotoxic

MESH TERMS: immunology

Chemical & Substance for Abstract: Mouse and human granzyme B have distinct tetrapeptide specificities and abilities to recruit the bid pathway. Information

Substance Name: Caspase 3

Registry Number: EC 3.4.22.-

Grant and Affiliation Information for Mouse and human granzyme B have distinct tetrapeptide specificities and abilities to recruit the bid pathway.

AFFILIATION: Departments of Medicine, Cell Biology, and Pathology, Johns Hopkins University School of Medicine, Baltimore, Maryland 21224, USA. lcr@jhmi.edu

Country: United States

AGENCY: United States NHLBI

GRANT: HL 56091

ACRONYM: HL

MEDLINETA: J Biol Chem

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