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Human Perforin 1 Protein expressed in Wheat germ - ABIN1316183
Lu, Lamontagne, Sun, Pinkerton, Block, Lu: Role of the inflammatory protein serine protease inhibitor Kazal in preventing cytolytic granule granzyme A-mediated apoptosis. in Immunology 2011
The decreased expression of perforin in circulating CD3 (show CD3 Proteins)+CD8 (show CD8A Proteins)+ positive T cells is an important biomarker of damaged antitumor immunity in advanced lung cancer.
Letter/Case Report: recurrent episodes of macrophage activation syndrome in peripheral spondyloarthritis with monoallelic missense mutations in PRF1.
PRF delivers granulysin (show GNLY Proteins) and granzymes into parasite infected cells to kill the parasite.
Among SLAMF4+ cells, the T cell fraction positive for perforin and granzyme B was higher in those obtained from healthy donors compared to SLE patients.
monoallelic mutations of PRF1 decrease NK-cell cytotoxicity should be considered in individuals presenting with the manifestations of immune deficiency states that impinge on NK-cell cytotoxicity.
Calcific aortic valve disease is characterized by increased expression of granzymes and perforin.
linking PRF1 missense mutations to lymphoma susceptibility and highlighting clinical variability within families. PRF1 mutations should, therefore, be considered as a cause of several diseases disparate to HLH.
PRF1 mutations are associated with hemophagocytic lymphohistiocytosis.
There is no association between gene polymorphisms of PRF1 gene and the susceptibility to hemophagocytic lymphohistiocytosis
A wide heterogeneity was observed in the nature of perforin gene mutations in familial hemophagocytic lymphohistiocytosis patients in India.
study shows that perforin is essential to facilitate beta cell destruction in mouse models of type 1 diabetes
Released granzyme B induces DNA fragmentation in intraepithelial lymphocytes independently of Perforin
serglycin (show SRGN Proteins) plays a critical role in the maturation of dense-core cytotoxic granules in cytotoxic lymphocytes and the trafficking and storage of perforin and granzyme B, whereas granzyme A (show GZMA Proteins) is unaffected
This suggests that LPS alters UNK cell migration and activates cytotoxic granule release.
it is proposed that Ca(2 (show CA2 Proteins)+) binding at the weakest affinity site triggers changes in the perforin C2 domain that facilitate its interaction with lipid membranes
a lack of perforin and absence of the specific activation of NK cells during acute MCMV infection lead to an unleashed CD8 (show CD8A Proteins)(+) T cell response that is detrimental for the host.
CD8 T cells are sufficient as a sole perforin-expressing cell type to cause BBB disruption in the PIFS model.
The rate and proportion of donor lymphoid cell engraftment and expansion of effector memory donor T cells were significantly increased within 5 to 7 days post-bone marrow transplantation in perforin-deficient recipients, compared with wild-type.
Regulatory effects of perforin on glucose tolerance are mechanistically linked to the control of T-cell proliferation and cytokine production in inflamed visceral adipose tissue.
Perforin (and granzyme B)-dependent apoptosis increases postapoptotic necrosis and inflammation in atherosclerosis.
It is a cytotoxic genes in the endometrium and hightly expressed in the peri (show PLIN1 Proteins)-implantation endometrium.
The protein encoded by this gene has structural and functional similarities to complement component 9 (C9). Like C9, this protein creates transmembrane tubules and is capable of lysing non-specifically a variety of target cells. This protein is one of the main cytolytic proteins of cytolytic granules, and it is known to be a key effector molecule for T-cell- and natural killer-cell-mediated cytolysis. Defects in this gene cause familial hemophagocytic lymphohistiocytosis type 2 (HPLH2), a rare and lethal autosomal recessive disorder of early childhood. Alternative splicing results in multiple transcript variants encoding the same protein.
perforin 1 (pore forming protein)
, lymphocyte pore forming protein
, lymphocyte pore-forming protein
, pore forming protein