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Information on EC 3.4.21.79 - granzyme B and Organism(s) Mus musculus and UniProt Accession P04187
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- 3.4.21.79
- perforin
- t-cells
- cd8
-
cytolytic
-
immunotherapy
- vaccine
- lymphoma
-
rejection
- tnf
- dendritic
-
cell-mediated
- ifn-gamma
-
allograft
-
tregs
- tia-1
- fasl
- foxp3
-
autologous
- interferon-gamma
-
caspases
-
degranulation
-
allogeneic
-
epstein-barr
-
antigen-specific
-
virus-specific
-
immunophenotype
-
ctla-4
-
anti-cd3
-
tumor-infiltrating
-
nk-cell
-
extranodal
-
elispot
- synthesis
-
eomes
-
graft-versus-leukemia
-
cd45ro
-
alcls
- biotechnology
-
death-1
- analysis
-
intragraft
- lag-3
-
hiv-specific
- medicine
- diagnostics
- degradation
-
alloreactive
-
lymphocyte-mediated
-
lymphokine-activated
- crma
-
b-mediated
- pharmacology
-
ag-specific
-
banff
-
hepatosplenic
-
anti-pd-1
- interleukin-15
The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
granzyme b, gra-b, asp-ase, lymphocyte protease, gzm b, granzyme g, pro-apoptotic serine protease, progrb, ctla1, cytotoxic cell proteinase-1, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
C11
-
-
-
-
CCP1
-
-
-
-
CCPII
-
-
-
-
CTLA1
-
-
-
-
CTSGL1
-
-
-
-
Cytotoxic cell proteinase-1
-
-
-
-
Granzyme G
-
-
-
-
Granzyme H
-
-
-
-
HLp
-
-
-
-
Human lymphocyte protein
-
-
-
-
Lymphocyte protease
-
-
-
-
Proteinase, CCP1
-
-
-
-
SECT
-
-
-
-
T-cell serine protease 1-3E
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
143180-74-9
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acetyl-IETD-7-amido-4-methylcoumarin + H2O
acetyl-IETD + 7-amino-4-methylcoumarin
-
-
-
-
?
BCL2/adenovirus E1B 19-kDa protein-interacting protein 2 + H2O
?
-
generated with similar efficiency by mouse and human recombinant granzyme B
-
-
?
Hsp70/Hsp90-organizing protein + H2O
?
-
directly cleaved at Asp186 in vitro and in cells undergoing GzmB-induced death. Processing by GzmB is caspase-independent. Cleavage by GzmB destroys known functions of Hsp70/Hsp90-organizing protein in Hsp binding and hormone receptor assembly
-
-
?
LEADKGKLEYD + H2O
LEAD + KGKLEYD
-
is a far better substrate for mouse granzyme B as compared with human granzyme B
-
-
?
Nalpha-tert-Butyloxycarbonyl-Ala-Ala-Met thiobenzyl ester + H2O
?
-
-
-
-
?
Nalpha-tert-Butyloxycarbonyl-L-Ala-L-Ala-L-Asp thiobenzyl ester + H2O
?
-
-
-
-
?
polypyrimidine tract-binding protein + H2O
?
-
2times more efficiently cleaved by mouse versus human recombinant granzyme B
-
-
?
pro-caspase-3 + H2O
?
-
activates caspase-3, whether of human or murine origin, with a similar efficiency
-
-
?
pro-caspase-7 + H2O
?
-
activates caspase-7, whether of human or murine origin, with a similar efficiency
-
-
?
pro-CPP32 + H2O
?
-
processes the caspase into its enzymatically active form
-
?
pro-mCASP-3 + H2O
caspase-3 + ?
-
activational cleavage of the caspase proform
-
?
pro-mCASP-7 + H2O
caspase-7 + ?
-
activational cleavage of the caspase proform
-
?
pro-caspase-3 + H2O
caspase-3 + ?
-
cleaves human pro-caspase-3 but only generates a 21-kDa fragment, no autocatalytic removal of the caspase-3 prodomain. Efficiently cleaves and activates mouse procaspase-3, producing predominantly the 17-kDa fragment
-
-
?
additional information
?
-
-
the substrate preference of granzyme B is determined by a positive charge in the specificity pocket
-
-
?
additional information
?
-
-
preference for substrates with Glu or Asp as the residue amino-terminal to the scissile bond, little or no activity with oligopeptide substrates for trypsin-like, chymotrypsin-like, and elastase-like proteases
-
-
?
additional information
?
-
-
involved in cell killing by cytotoxic T lymphocytes, activates the apoptotic death pathway in the target cell
-
?
additional information
?
-
-
involved in cell killing by cytotoxic T lymphocytes, activates the apoptotic death pathway in the target cell
-
?
additional information
?
-
-
proforms of mCASP-2 and mCASP-1 are not substrates, pro-mCASP-6 is not proteolytically cleaved by granzyme B, mCASP-11 and mCASP-12 are not processed
-
?
additional information
?
-
-
requirement for aspartic acid in the substrate P1 position, induces DNA fragmentation in isolated nuclei in the presence of cytosolic factors
-
?
additional information
?
-
-
both human or mouse BID are highly resistant to cleavage by mouse GrB
-
-
?
additional information
?
-
-
BID is a poor substrate for mouse GzmB. Fails to cleave caspase-8 and ICAD from either human or murine origin. Cleaves nucleophosmin of human origin very inefficiently, does not cleave nucleophosmin within J774 cell free extracts
-
-
?
additional information
?
-
-
both human or mouse BID are highly resistant to cleavage by mouse GrB. It is unable to cleave BID in cell lysates in which caspases are inactivated but induces BID cleavage, albeit inefficiently, in lysates supporting caspase activity. BID pathway is not a prominent primary mediator of the effects of mouse GrB
-
-
?
additional information
?
-
-
no efficient cleavage of mouse and human Bid by mouse granzyme B
-
-
?
additional information
?
-
-
platelets from septic granzyme B null (-/-) mice show no lymphotoxicity
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
pro-mCASP-3 + H2O
caspase-3 + ?
-
activational cleavage of the caspase proform
-
?
pro-mCASP-7 + H2O
caspase-7 + ?
-
activational cleavage of the caspase proform
-
?
additional information
?
-
-
involved in cell killing by cytotoxic T lymphocytes, activates the apoptotic death pathway in the target cell
-
?
additional information
?
-
-
both human or mouse BID are highly resistant to cleavage by mouse GrB
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CaCl2
-
50 mM, enhances Nalpha-tert-butyloxycarbonyl-L-Ala-L-Ala-L-Asp thiobenzyl esterase activity
NaCl
-
0.1-1.0 M, highest activity with Nalpha-tert-butyloxycarbonyl-Ala-Ala-Met thiobenzyl ester
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(S)-3-((2S,5S)-5-((2S,3S)-2-acetamido-3-methylpentanamido)-4-oxo-1,2,4,5,6,7-hexahydroazepino[3,2,1-hi]indole-2-carboxamido)-4-oxobutanoic acid
-
peptide-mimetic analog of IEPD-aldehyde
serpina3n
-
inhibitor for human and mouse GrB, expressed by Sertoli cells. Inhibitor shares homology with human alpha-1-anti-chymotrypsin
-
additional information
-
no inhibition with 100K assembly protein of human adenovirus type 5
-
additional information
-
inhibition of caspases may clonogenically rescue cells from mouse GzmB
-
additional information
-
to protect beta cells from allogeneic CTL attack, one needs to inhibit the perforin/granzyme and probably also the TNFalpha pathway. Granzyme B-dependent death of NIT-1 cells is not inhibited by Bcl-2 overexpression
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
granzyme B expression in Treg cells is activated by syngeneic tumor cell line
-
additional information
-
induction of granzyme B by a DNase1 hypersensitive site 3.9 kb upstream of the transcription start site of granzyme B
-
additional information
-
secreted after Fcepsilon-receptor-mediated activation in cytoplasmic granules of bone marrow-derived mast cells
-
additional information
-
sepsis induces platelet granzyme B expression. In septic mice, granzyme B expression significantly increases by 24 h in megakaryocytes and platelets
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000025
(S)-3-((2S,5S)-5-((2S,3S)-2-acetamido-3-methylpentanamido)-4-oxo-1,2,4,5,6,7-hexahydroazepino[3,2,1-hi]indole-2-carboxamido)-4-oxobutanoic acid
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
septic megakaryocytes produce platelets with acutely altered mRNA profiles, and these platelets mediate lymphotoxicity via granzyme B
-
transcripts of the granzyme G gene are detected at the 2-cell stage, but are absent at the oocyte, 1-cell, 96 hr, and later stages. Spatial expression is confined to the extra-embryonic trophoblasts during the middle implantation stage of the mouse placenta
-
skin-, but not lung-associated primary mast cells as well as in vitro-differentiated bone marrow-derived mast cells express GzmB
-
septic megakaryocytes produce platelets with acutely altered mRNA profiles, and these platelets mediate lymphotoxicity via granzyme B
additional information
-
of activated CTL lines, grown in the presence of recombinant interleukin 2
-
expresses gzmB. Positive gzmB cytotoxic T-lymphocyte cells abrogate target cell proliferation by inducing cell death, independent of caspases and mitochondrial signaling. Positive gzmB cytotoxic T-lymphocyte cells independently induce pro-apoptotic processes either via caspase-3/-7, leading to plasma membrane perturbance and ROS production or via Bid/Bak/Bax, resulting in cytochrome c release, whereby both pathways elicit loss of mitochondrial membrane potential
-
wild-type CD8alpha+ intraepithelial lymphocytes constitutively express granzyme B
-
granzyme B and granzyme C expression is detected in CD4+ and CD8+ T cells activated with CD3/CD28 beads or MLRs
additional information
-
granzyme B is not expressed in naive Treg cells but is highly expressed in 5%-30% of CD4(+)Foxp3(+) Treg cells in the tumor environment
additional information
-
in activated but not resting primary CD8+ T cells, a DNase1 hypersensitive site pesent upstream of the granzyme B gene. Thymocytes do not express granzyme B. MTL 2.8.2 cell line constitutively expresses granzyme B at a high level. CTLL R8 cell line constitutively expresses endogenous granzyme B gene
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
cytoplasmic granules of cytotoxic T lymphocytes and natural killer cells
-
cytoplasmic granules of cytotoxic T lymphocytes anf natural killer cells
-
is associated with cytoplasmic granules of bone marrow-derived mast cells
-
of 2-cell stage, protein completely disappears by the 16-cell stage
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
the mouse pathogen Brucella microti persists in mice lacking perforin or granzyme B as well as in mice depleted of Tc cells
metabolism
gzmB+ cytotoxic T cell-mediated apoptosis (via phosphatidylserine translocation, mitochondrial depolarization, cytochrome c release, and caspase-3 activation) is severely reduced in 3T9 cells lacking either Bim or both Bak and Bax, gzmB+ cytotoxic T cell-mediated apoptosis is not affected in SV40-transformed mouse embryonic fibroblast cells lacking Bak/Bax.Role of Bim in gzmB-mediated apoptosis, overview
physiological function
malfunction
-
knockout GzmB-/- mice which have a small deletion in the granzyme B gene express granzyme C earlier and more abundantly in lymphocytes on a per-cell basis compared to wild-type, suggesting that the deleted 350-bp region in the granzyme B gene is important for the regulation of both granzymes B and granzyme C. Intraepithelial lymphocytes in GzmB-/- knockout mice likewise express granzyme C
physiological function
physiological function
cytotoxic T cells use perforin and granzyme B to kill virus-infected cells and cancer cells. Granzyme B activates the mitochondrial cell death pathway in a Bim-dependent fashion in cytotoxic T lymphocytes
physiological function
the enzyme is required for elimination of the mouse pathogen Brucella microti from liver and spleen and is necessary to inhibit Brucella microti replication in primary macrophages
physiological function
both CD4+ and CD8+ T-cells respond to Listeria monocytogenes, but unlike poorly responding CD4+ T-cells, CD8+ T-cells readily proliferate and express high levels of recombinant chimeric GZMB-Tom as early as 2 days after infection. Using the GZMBTom-OT1 T cells, rapid CD8+ T-cell division and expression of GZMB-Tom following intravenous infection with ActA-/OVA bacteria
physiological function
-
gzmB-induced cell death is accompanied by a caspase-dependent pathway of extra-mitochondrial reactive oxygen species production, through activation of NADPH oxidase
physiological function
-
antisense morpholino oligonucleotide knock-down leads to arrest of early development at the 2- to 4-cell stages. Only 11.6% of treated embryos overcome 2-cell arrest and develop into 4-cell stage embryos. Embryos exhibited decreased zygotic gene transcription
physiological function
-
granzyme B-deficient mice, and to a lesser extent perforin-deficient mice, exhibit a significant increase in the number of Ag-specific CD8+ T cells in the lungs and draining lymph nodes of virally infected animals. Viral titers in granzyme B-deficient mice are similar to wild-type mice and significantly less than perforin-deficient mice. Regulatory T cells from wild-type mice express high levels of granzyme B in response to infection, and depletion of regulatory T cells from these mice results in an increase in the number of Ag-specific CD8+ T cells, similar to that observed in granzyme B-deficient mice. Granzyme B-deficient regulatory T cells display defective suppression of CD8+ T cell proliferation in vitro
physiological function
-
in filarial infection with Litomosoides sigmodontis, worm loads are significantly reduced in gzmA/gzmB and in gzmB knockout mice during the whole course of infection, but enhanced only early in gzmA knockout compared with wild-type mice. GzmA/gzmB deficiency is associated with a defense-promoting Th2 cytokine and Ab shift, enhanced early inflammatory gene expression, and a trend of reduced alternatively activated macrophage induction
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). GRAB_MOUSE
247
0
27470
Swiss-Prot
Secretory Pathway (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
-
GrB is synthesized as a zymogen (proGrB) and activated in cytotoxic granules by cathepsin C and cathepsin H. Mice lacking both cathepsin C and cathepsin H show reduced convertase activity. Despite this, cytotoxic lymphocytes from transgenic mice retain cytotoxic activity and some residual GrB activity, indicating that other proteases must also possess convertase activity
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
R226G
-
replacing Arg-226 by a glycine yields an enzyme with chymase-like activity cleaving like cathepsin G after Phe
additional information
additional information
construction of functional fluorescent chimeric GZMB-Tomato (GZMB-Tom) fusion protein. The GZMB-Tom knock-in mice in which GZMB-Tom faithfully reproduce GZMB expression, provide useful tools to dissect mechanisms leading to the development of anti-bacterial effector and memory CD8+ T-cells and reactivation of the memory response to cognate antigen or inflammatory signals. The use of CD8+ T-cells from knock in mice expressing a functional fluorescent chimeric GZMB-Tom protein in place of GZMB allow the evaluation of the induction of GZMB during CD8+ T-cell differentiation as a function of T-cell division. Mice homozygous for GZMB-Tom and heterozygous for the OT1 (GZMB-Tom-OT1) or OT2 (GZMB-Tom-OT2) transgenic T-cell receptors are used. Congenic C57BL/6 (CD45.1) mice are used as recipients
additional information
-
deletion of the DNase1 hypersensitive site upstream of the granzyme B gene results in a 10fold reduction in expression
additional information
-
granzyme A/B-deficient mice exhibit significantly reduced survival compared to wild-type mice. Granzyme B-deficient mice clear both allogeneic and syngeneic tumor cell lines more efficiently than do wild-type mice. NK and CD8+ T cell death in tumor ascites of granzyme B-deficient mice is reduced after Treg cell depletion
additional information
-
granzyme B deficient mice lack expression of linked granzyme-loci, due to accidental effects of the thymidine kinase enhancer integrated into the granzyme locus on mouse Chromosome 14
additional information
-
granzyme B-deficient mice possess a normal phenotype, with the exception of reduced CTL-mediated target cell apoptosis, antiviral responses, and tumor cell clearance. Treg cells from granzyme B-deficient mice can not suppress immune responses as effectively as Treg cells from wild-type mice. Granzyme B-deficient recipient mice exhibit reduced allograft vasculopathy and increased susceptibility to allgergen-induced asthma. Hearts from 129J donor mice transplanted into granzyme B-KO mice exhibit significantly smaller lesions and luminal narrowing compared with wild-type recipients
additional information
-
gzmB-deficient mice do not cause cell death in susceptible adherent target cells
additional information
-
mice deficient in granzyme B are up to 100000fold more sensitive to the natural mouse proxivirus pathogen ectromelia than are wild-type mice
additional information
-
target cells with reduced levels of Hsp70/Hsp90-organizing protein are no more susceptible than control target cells to GzmB-/-/deltaPGK-neo and GzmB-/-/+PGK-neo natural killer effectors. GzmA-/- x GzmB-/-/deltaPGK-neo and GzmA-/- x GzmB-/-/+PGK-neo doubly deficient natural killer effectors, likewise, show no differences in susceptibility between control and Hsp70/Hsp90-organizing protein knockdown target cells
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant expression of functional fluorescent chimeric GZMB-Tom mutant enzyme fusion protein in murine CD8+ T-cells
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
the protease may be a therapeutic target for the prevention of bacterial sepsis without affecting immune control of the pathogen
analysis
-
caution in the design and interpretation of experiments using GrBs from different species due to distinct tetrapeptide specificities and abilities to recruit the BID pathway
degradation
-
human and murine GzmB are distinct enzymes with different substrate preferences. Subtle differences in enzyme structure can radically affect substrate selection. Caspases are essential for apoptosis initiated by mouse GzmB
medicine
additional information
-
cytotoxic granule-mediated death of both primary and transformed beta cells requires granzyme B. Early cell death is completely dependent on granzyme B. Death induced by granzyme B is dependent on cosecretion with perforin
medicine
-
cytolytic T-lymphocytes from enzyme or granzyme A deficient mice similarly induce early proapoptotic features such as phosphatidyl serine exposure on plasma membrane, or reactive oxygen radical generation, though with distinct kinetics. Cytolytic T-lymphocytes from granzyme A, but not granzyme B deficient animals activate caspase 3 and 9. All granzyme-induced apoptotic features depend critically on perforin
medicine
-
activated mast cells contribute, via secreted gzmB, to cell death, increased vascular permeability, leukocyte extravasation and subsequent inflammatory processes in affected tissues. GzmB-induced detachment of adherent mouse embryonic fibroblasts leads to anoikis. GzmB induces a disorganization of endothelial cell-cell contacts
medicine
-
granzyme B may play a key role in ateromatous diseases. Role in cardiac allograft vasculopathy and atherosclerosis
medicine
-
Hsp70/Hsp90-organizing protein per se does not set the threshold for susceptibility to GzmB-induced apoptosis
medicine
-
pleiotropic pro-apoptotic function of gzmB presumably to counteract evasion strategies of pathogens and to control tumors
medicine
-
Treg cells derived from the tumor environment can induce NK and CD8(+) T cell death in a granzyme B- and perforin-dependent fashion. Granzyme B and perforin are relevant for Treg cell-mediated suppression of tumor clearance in vivo
medicine
-
granzyme B-deficient mice, and to a lesser extent perforin-deficient mice, exhibit a significant increase in the number of Ag-specific CD8+ T cells in the lungs and draining lymph nodes of virally infected animals. Viral titers in granzyme B-deficient mice are similar to wild-type mice and significantly less than perforin-deficient mice. Regulatory T cells from wild-type mice express high levels of granzyme B in response to infection, and depletion of regulatory T cells from these mice results in an increase in the number of Ag-specific CD8+ T cells, similar to that observed in granzyme B-deficient mice. Granzyme B-deficient regulatory T cells display defective suppression of CD8+ T cell proliferation in vitro
medicine
-
proinflammatory gzmA and anti-inflammatory gzmB are novel modulators of the Th1/2 balance and defense in helminth infection
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Odake, S.; Kam, C.M.; Narasimhan, L.; Poe, M.; Blake, J.T.; Krahenbuhl, O.; Tschopp, J.; Powers, J.C.
Human and murine cytotoxic T lymphocyte serine proteases: subsite mapping with peptide thioester substrates and inhibition of enzyme activity and cytolysis by isocoumarins
Biochemistry
30
2217-2227
1991
Homo sapiens, Mus musculus
Peitsch, M.C.; Tschopp, J.
Granzyme B
Methods Enzymol.
244
80-87
1994
Homo sapiens, Mus musculus
Caputo, A.; James, M.N.G.; Powers, J.C.; Hudig, D.; Bleackley, R.C.
Conversion of the substrate specificity of mouse proteinase granzyme B
Nat. Struct. Biol.
1
364-367
1994
Mus musculus
Xia, Z.; Kam, C.M.; Huang, C.; Powers, J.C.; Mandle, R.J.; Stevens, R.L.; Lieberman, J.
Expression and purification of enzymatically active recombinant granzyme B in a baculovirus system
Biochem. Biophys. Res. Commun.
243
384-389
1998
Homo sapiens, Mus musculus
Van de Craen, M.; Van den Brande, I.; Declercq, W.; Irmler, M.; Beyaert, R.; Tschopp, J.; Fiers, W.; Vandenabeele, P.
Cleavage of caspase family members by granzyme B. A comparative study in vitro
Eur. J. Immunol.
27
1296-1299
1997
Mus musculus
Shi, L.; Yang, X.; Froelich, C.J.; Greenberg, A.H.
Purification and use of granzyme B
Methods Enzymol.
322
125-143
2000
Homo sapiens, Mus musculus, Rattus norvegicus
Andrade, F.; Casciola-Rosen, L.A.; Rosen, A.
A novel domain in adenovirus L4-100K is required for stable binding and efficient inhibition of human granzyme B: possible interaction with a species-specific exosite
Mol. Cell. Biol.
23
6315-6326
2003
Homo sapiens, Mus musculus, Rattus norvegicus
Pardo, J.; Bosque, A.; Brehm, R.; Wallich, R.; Naval, J.; Mullbacher, A.; Anel, A.; Simon, M.M.
Apoptotic pathways are selectively activated by granzyme A and/or granzyme B in CTL-mediated target cell lysis
J. Cell Biol.
167
457-468
2004
Mus musculus
Duggan, B.L.; Cabilio, N.R.; Dickie, P.; Witmer, J.; Goping, I.S.; Underhill, D.A.; Bleackley, R.C.
A novel lineage-specific hypersensitive site is essential for position independent granzyme B expression in transgenic mice
Biochem. Biophys. Res. Commun.
368
357-363
2008
Mus musculus
Chamberlain, C.M.; Granville, D.J.
The role of Granzyme B in atheromatous diseases
Can. J. Physiol. Pharmacol.
85
89-95
2007
Homo sapiens, Mus musculus
Pardo, J.; Wallich, R.; Ebnet, K.; Iden, S.; Zentgraf, H.; Martin, P.; Ekiciler, A.; Prins, A.; Muellbacher, A.; Huber, M.; Simon, M.M.
Granzyme B is expressed in mouse mast cells in vivo and in vitro and causes delayed cell death independent of perforin
Cell Death Differ.
14
1768-1779
2007
Mus musculus
Pardo, J.; Wallich, R.; Martin, P.; Urban, C.; Rongvaux, A.; Flavell, R.A.; Muellbacher, A.; Borner, C.; Simon, M.M.
Granzyme B-induced cell death exerted by ex vivo CTL: discriminating requirements for cell death and some of its signs
Cell Death Differ.
15
567-579
2008
Mus musculus
Cao, X.; Cai, S.F.; Fehniger, T.A.; Song, J.; Collins, L.I.; Piwnica-Worms, D.R.; Ley, T.J.
Granzyme B and perforin are important for regulatory T cell-mediated suppression of tumor clearance
Immunity
27
635-646
2007
Mus musculus, Mus musculus 129/SvJ
Bredemeyer, A.J.; Carrigan, P.E.; Fehniger, T.A.; Smith, D.F.; Ley, T.J.
Hop cleavage and function in granzyme B-induced apoptosis
J. Biol. Chem.
281
37130-37141
2006
Homo sapiens, Mus musculus
Casciola-Rosen, L.; Garcia-Calvo, M.; Bull, H.G.; Becker, J.W.; Hines, T.; Thornberry, N.A.; Rosen, A.
Mouse and human granzyme B have distinct tetrapeptide specificities and abilities to recruit the bid pathway
J. Biol. Chem.
282
4545-4552
2007
Homo sapiens, Mus musculus
Cullen, S.P.; Adrain, C.; Luethi, A.U.; Duriez, P.J.; Martin, S.J.
Human and murine granzyme B exhibit divergent substrate preferences
J. Cell Biol.
176
435-444
2007
Homo sapiens, Mus musculus
Sutton, V.R.; Estella, E.; Li, C.; Chen, M.; Thomas, H.E.; Kay, T.W.; Trapani, J.A.
A critical role for granzyme B, in addition to perforin and TNFalpha, in alloreactive CTL-induced mouse pancreatic beta cell death
Transplantation
81
146-154
2006
Mus musculus
Waterhouse, N.J.; Trapani, J.A.
H is for helper: granzyme H helps granzyme B kill adenovirus-infected cells
Trends Immunol.
28
373-375
2007
Homo sapiens, Mus musculus
Freishtat, R.J.; Natale, J.; Benton, A.S.; Cohen, J.; Sharron, M.; Wiles, A.A.; Ngor, W.M.; Mojgani, B.; Bradbury, M.; Degnan, A.; Sachdeva, R.; Debiase, L.M.; Ghimbovschi, S.; Chow, M.; Bunag, C.; Kristosturyan, E.; Hoffman, E.P.
Sepsis alters the megakaryocyte-platelet transcriptional axis resulting in granzyme B-mediated lymphotoxicity
Am. J. Respir. Crit. Care Med.
179
467-473
2009
Homo sapiens, Mus musculus
Van Damme, P.; Maurer-Stroh, S.; Plasman, K.; Van Durme, J.; Colaert, N.; Timmerman, E.; De Bock, P.J.; Goethals, M.; Rousseau, F.; Schymkowitz, J.; Vandekerckhove, J.; Gevaert, K.
Analysis of protein processing by N-terminal proteomics reveals novel species-specific substrate determinants of granzyme B orthologs
Mol. Cell. Proteomics
8
258-272
2009
Homo sapiens, Mus musculus
Aguilo, J.I.; Anel, A.; Catalan, E.; Sebastian, A.; Acin-Perez, R.; Naval, J.; Wallich, R.; Simon, M.M.; Pardo, J.
Granzyme B of cytotoxic T cells induces extramitochondrial reactive oxygen species production via caspase-dependent NADPH oxidase activation
Immunol. Cell Biol.
88
545-554
2010
Mus musculus
Kurschus, F.; Jenne, D.
Delivery and therapeutic potential of human granzyme B
Immunol. Rev.
235
159-171
2010
Homo sapiens, Mus musculus
D'Angelo, M.E.; Bird, P.I.; Peters, C.; Reinheckel, T.; Trapani, J.A.; Sutton, V.R.
Cathepsin H is an additional convertase of pro-granzyme B
J. Biol. Chem.
285
20514-20519
2010
Homo sapiens, Mus musculus
Cai, S.F.; Fehniger, T.A.; Cao, X.; Mayer, J.C.; Brune, J.D.; French, A.R.; Ley, T.J.
Differential expression of granzyme B and C in murine cytotoxic lymphocytes
J. Immunol.
182
6287-6297
2009
Mus musculus
Boivin, W.A.; Cooper, D.M.; Hiebert, P.R.; Granville, D.J.
Intracellular versus extracellular granzyme B in immunity and disease: challenging the dogma
Lab. Invest.
89
1195-1220
2009
Homo sapiens, Mus musculus
Tsai, T.; Lin, W.; Yang, S.; Cheng, W.; Cheng, E.; Lee, M.; Chong, K.; Chen, C.
Granzyme G is expressed in the two-cell stage mouse embryo and is required for the maternal-zygotic transition
BMC Dev. Biol.
10
88
2010
Mus musculus
Hartmann, W.; Marsland, B.J.; Otto, B.; Urny, J.; Fleischer, B.; Korten, S.
A novel and divergent role of granzyme A and B in resistance to helminth infection
J. Immunol.
186
2472-2481
2011
Mus musculus
Salti, S.M.; Hammelev, E.M.; Grewal, J.L.; Reddy, S.T.; Zemple, S.J.; Grossman, W.J.; Grayson, M.H.; Verbsky, J.W.
Granzyme B regulates antiviral CD8+ T cell responses
J. Immunol.
187
6301-6309
2011
Mus musculus
Arias, M.A.; Jimenez de Baguees, M.P.; Aguilo, N.; Menao, S.; Hervas-Stubbs, S.; de Martino, A.; Alcaraz, A.; Simon, M.M.; Froelich, C.J.; Pardo, J.
Elucidating sources and roles of granzymes A and B during bacterial infection and sepsis
Cell Rep.
8
420-429
2014
Mus musculus (P04187), Mus musculus, Mus musculus B6 (P04187)
Catalan, E.; Jaime-Sanchez, P.; Aguilo, N.; Simon, M.M.; Froelich, C.J.; Pardo, J.
Mouse cytotoxic T cell-derived granzyme B activates the mitochondrial cell death pathway in a Bim dependent fashion
J. Biol. Chem.
290
6868-6877
2015
Mus musculus (P04187), Mus musculus, Mus musculus B6 (P04187)
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