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

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

The Journal of biological chemistry, 16 February 2007, Vol.282(7), pp.4545-52 [Peer Reviewed Journal]

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  • Title:
    Mouse and human granzyme B have distinct tetrapeptide specificities and abilities to recruit the bid pathway
  • Author: Casciola-Rosen, Livia ; Garcia-Calvo, Margarita ; Bull, Herbert G ; Becker, Joseph W ; Hines, Tonie ; Thornberry, Nancy A ; Rosen, Antony
  • Description: 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...
  • Is Part Of: The Journal of biological chemistry, 16 February 2007, Vol.282(7), pp.4545-52
  • Identifier: ISSN: 0021-9258 ; PMID: 17179148 Version:1
  • Subjects: Bh3 Interacting Domain Death Agonist Protein -- Metabolism ; Granzymes -- Metabolism ; Oligopeptides -- Metabolism ; T-Lymphocytes, Cytotoxic -- Enzymology
  • Language: English
  • Source: MEDLINE/PubMed (U.S. National Library of Medicine)

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