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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 (show HAVCR2 ELISA Kits)+CD8 (show CD8A ELISA Kits)+T cells with lower perforin and granzyme B (show Gzmb ELISA Kits) expression and higher CD95 (show FAS ELISA Kits) expression in MDS (show PAFAH1B1 ELISA Kits) patients were observed.
ITP (show ITPA ELISA Kits) patients displayed an increased frequency of rare missense variations of the PRF1 gene
The decreased expression of perforin in circulating CD3 (show CD3 ELISA Kits)+CD8 (show CD8A ELISA Kits)+ 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 ELISA Kits) and granzymes into parasite infected cells to kill the parasite.
Among SLAMF4 (show CD244 ELISA Kits)+ cells, the T cell fraction positive for perforin and granzyme B (show Gzmb ELISA Kits) 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.
Furthermore, perforin production specifically by CD8 (show CD8A ELISA Kits) 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 (show IL18 ELISA Kits)-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 (show Gzmb ELISA Kits) induces DNA fragmentation in intraepithelial lymphocytes independently of Perforin
serglycin (show SRGN ELISA Kits) 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 (show Gzmb ELISA Kits), whereas granzyme A (show GZMA ELISA Kits) is unaffected
This suggests that LPS alters UNK cell migration and activates cytotoxic granule release.
it is proposed that Ca(2 (show CA2 ELISA Kits)+) 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 ELISA Kits)(+) T cell response that is detrimental for the host.
CD8 (show CD8A ELISA Kits) T cells are sufficient as a sole perforin-expressing cell type to cause BBB (show ALMS1 ELISA Kits) disruption in the PIFS (show PROC ELISA Kits) model.
It is a cytotoxic genes in the endometrium and hightly expressed in the peri (show PLIN1 ELISA Kits)-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