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results of the study may imply that perforin gene variation has a role in modifying mortality in childhood ALL
Urothelial bladder cancer may suppress perforin expression in CD8+ T cells by an ICAM-1/TGFbeta2 mediated pathway
Perforin binds to membranes and undergoes substantial structural re-arrangement to form pores that enable diffusion of granzyme into the target cell [Review].
findings show that N-linked glycosylation of the perforin C-terminus at Asn549 within the endoplasmic reticulum inhibits oligomerisation of perforin monomers and protects the host cell from premature pore formation; studies reveal a post-translational regulatory mechanism essential for maintaining perforin in an inactive state until its secretion from the inhibitory acidic environment of the secretory granule
Study focuses on the role of perforin in both protecting and promoting human disease. It concludes with a novel hypothesis that diversity observed in the PRF1 gene may be an example of selective advantage that protects an individual from perforin-mediated pathology, such as blood-brain barrier disruption. [review]
Our studies suggest that although moderate levels of expression can result in partial amelioration of the hemophagocytic lymphohistiocytosis (HLH)phenotype, high levels of perforin expression per cell are required for complete correction of HLH.
Findings support an association between childhood DNA methylation patterns in PRF1 and a record of severe respiratory syncytial virus bronchiolitis in infancy.
our data provide the first evidence of a strict link between the absence of CD28 and the expression of perforin, which is likewise enhanced by the expression of NKG2D, within selected CD4(+) T cells from cervical cancer patients.
A girl with neurological manifestations of familial hemophagocytic lymphohistiocytosis 2 had reduced perforin 1 expression and was found to be homozygous for a mutation in PRF1 at codon 637 in exon 3 (c.673C>T p.Arg225Trp). Her non-consanguineous parents were both heterozygous carriers of this mutation.
Mutation in PRF1 gene is associated with hemophagocytic lymphohistiocytosis.
Increased TIM3+CD8+T cells with lower perforin and granzyme B expression and higher CD95 expression in MDS patients were observed.
ITP patients displayed an increased frequency of rare missense variations of the PRF1 gene
The decreased expression of perforin in circulating CD3+CD8+ 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.
A new heterozygous mutation (c.916G>A and c.65delC) was identified as familial hemophagocytic lymphohistiocytosis type 2 causing defect.
mutations result in severe chronic active Epstein-Barr virus disease
mutations result in hemophagocytic lymphohistiocytosis
PRF delivers granulysin 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.
elevated in the inflammatory lesions of placentas with villitis of unknown etiology
Study in mice models shows that perforin from antigen-specific cytotoxic T lymphocytes is required for Nlrp3 inflammasome activation in antigen-presenting cells. Furthermore, such activation of NLRP3 inflammasome contributes to the induction of antigen-specific antitumour immunity and pathogenesis of graft-versus-host diseases.
levetiracetam can still protect neurons with perforin knockout mice.
These studies indicate that CD8+ T cells against a single antigen can restrict Y. pseudotuberculosis colonization in a perforin-dependent manner, but ultimately are insufficient in their ability to provide sterilizing immunity and protect against death.
Furthermore, perforin production specifically by CD8 T cells was required to cause fatal edema during experimental cerebral malaria.
Our study suggests that perforin plays a role in dopaminergic neuron loss in PD.
IL-18-elicited NK cell perforin responses seem to be critical for coordinating mucosal inflammation during early infection
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 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 is unaffected
This suggests that LPS alters UNK cell migration and activates cytotoxic granule release.
it is proposed that Ca(2+) 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(+) 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.
Perforin has a role in atherosclerotic plaque development.
Defining the interaction of perforin with calcium and the phospholipid membrane.
miR-150 is a common post-transcriptional regulator for Prf1 in mouse and human NK cells that represses NK cell lytic activity.
Perforin and granzymes have complementary roles mediating epithelial injury by NK and CD8 T cells. The prevention of experimental biliary atresia can only be achieved by inhibiting both granules.
It is a cytotoxic genes in the endometrium and hightly expressed in the peri-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.
, lymphocyte pore forming protein
, lymphocyte pore-forming protein
, perforin 1 (pore forming protein)
, pore forming protein
, perforin 1 (pore forming protein) L homeolog
, perforin 1 L homeolog