Results 211 to 220 of about 53,350 (260)

Extracellular granzyme K enhances PD-L1 transcription and stability via F2RL1 activation to facilitate tumor immune evasion in lung adenocarcinoma. [PDF]

J Immunother Cancer
Feng HM, Zhao Y, Zhai KR, Li B, Song TN, Meng YQ, Huang HR, Li Z, Cui BQ, Yang N, Su ZP.   +10 more
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Pteryxin enhances human NK-cell cytotoxicity by upregulating NKp30, NKp46, and 2B4 via ERK/AKT signaling. [PDF]

Front Pharmacol
Park ES, Kim JT, Hwang YS, Han J, Park HM, Yoon HR, Cho HJ, Lee HG.   +7 more
europepmc   +1 more source

Comparative proteome analyses of human natural killer cells from patients after allogeneic stem cell transplantation and healthy individuals challenged with <i>Aspergillus fumigatus</i>. [PDF]

Microlife
Springer J, Drobny M, Heilig L, Kraus S, Kniemeyer O, Krüger T, Olischer C, Bussemer L, Panagiotou G, Brakhage AA, Einsele H, Schäuble S, Löffler J.   +12 more
europepmc   +1 more source

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Granzymes and Mitochondria

Biochemistry (Moscow), 2020
Cytotoxic T lymphocytes and natural killer cells eliminate infected cells from the organism by triggering programmed cell death (apoptosis). The contents of the lytic granules of killer cells, including pore-forming proteins perforins and proteolytic enzymes granzymes, are released with the following penetration of the released proteins into the target
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Granzymes and cell death.

Methods in enzymology, 2008
Granzymes are cell death-inducing serine proteases released from cytotoxic granules of cytotoxic T lymphocytes and natural killer cells during granule exocytosis in response to viral infection or against transformed cells marked for elimination. A critical cofactor for the granule exocytosis pathway is perforin, which mediates the entry of granzymes ...
Martinvalet, Denis, Thiery, Jerome, Chowdhury, Dipanjan   +2 more
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Granzyme A is a proinflammatory protease

Blood, 2009
To the editor: We have read with great interest the paper by Zhu et al[1][1] that suggests poly ADP ribose polymerase 1 (PARP-1) is cleaved when granzyme A (gzmA) enters target cells. This new finding may have implications for the proinflammatory effects of this protease.[2][2][⇓][3]–[4][4]
Julián, Pardo, Markus M, Simon, Christopher J, Froelich   +2 more
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Controversies in granzyme biology

Tissue Antigens, 2012
AbstractGranzymes (Grz) are a family of serine proteases found in the granules of cytotoxic lymphocytes and are emerging as an important group of proteins involved in immune function and surveillance. Grz have both cytotoxic and more recently reported non‐cytotoxic roles, however these functions are still subject to thorough investigation.
O, Susanto, J A, Trapani, D, Brasacchio
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Human neutrophils lack granzyme A, granzyme B, and perforin

Blood, 2004
Wagner et al[1][1] and Hochegger et al[2][2] reported that human polymorphonuclear neutrophils (PMNs) express granzyme A (GzmA), granzyme B (GzmB), and perforin (PFN), postulating a role for these granule proteins in PMN-mediated antibody-dependent cellular cytotoxicity.
Sunil S. Metkar, Christopher J. Froelich
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[4] Granzyme A

1994
Publisher Summary Cytotoxic T lymphocytes (CTLs) and natural killer (NK) cells of human, mouse, and rat origin express a large number of homologous serine proteinases. These proteinases are termed “granzymes,” as they are stored within cytoplasmic granules.
Markus M. Simon, Michael D. Kramer
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Granzyme B-Induced Apoptosis

1996
In the last several years the major mechanisms by which both cytotoxic T lymphocytes (CTL) and natural killer (NK) cells mediate cell death and apoptosis have been identified. Cytotoxic lymphocytes of both types induce apoptosis through granule-or Fas-dependent pathway 1-4and perhaps TNF-α5.
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