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a substance that partly or completely destroys animal cells

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2014/07/27 21:48:44」(JST)

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Perforin-1 is a protein that in humans is encoded by the PRF1 gene.^[2]^[3]^[4]

Function

Perforin is a cytolytic protein found in the granules of Cytotoxic T lymphocytes (CTLs) and NK cells. Upon degranulation, perforin inserts itself into the target cell's plasma membrane, forming a pore. The lytic membrane-inserting part of perforin is the MACPF domain.^[5] This region shares homology with cholesterol-dependent cytolysins from Gram-positive bacteria.^[1]

Perforin 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.^[4] Perforin is thought to act by creating holes in the plasma membrane which triggers an influx of calcium and initiates membrane repair mechanisms. These repair mechanisms bring perforin and granzymes into early endosomes.^[6]

Clinical significance

Defects in this gene cause familial hemophagocytic lymphohistiocytosis type 2 (HPLH2), a rare and lethal autosomal recessive disorder of infancy.^[4]

Interactions

Perforin has been shown to interact with Calreticulin.^[7]

References

^ ^a ^b Rosado CJ, Buckle AM, Law RH, Butcher RE, Kan WT, Bird CH, Ung K, Browne KA, Baran K, Bashtannyk-Puhalovich TA, Faux NG, Wong W, Porter CJ, Pike RN, Ellisdon AM, Pearce MC, Bottomley SP, Emsley J, Smith AI, Rossjohn J, Hartland EL, Voskoboinik I, Trapani JA, Bird PI, Dunstone MA, Whisstock JC (2007). "A common fold mediates vertebrate defense and bacterial attack". Science 317 (5844): 1548–51. doi:10.1126/science.1144706. PMID 17717151.
^ Fink TM, Zimmer M, Weitz S, Tschopp J, Jenne DE, Lichter P (Sep 1992). "Human perforin (PRF1) maps to 10q22, a region that is syntenic with mouse chromosome 10". Genomics 13 (4): 1300–2. doi:10.1016/0888-7543(92)90050-3. PMID 1505959.
^ Shinkai Y, Yoshida MC, Maeda K, Kobata T, Maruyama K, Yodoi J, Yagita H, Okumura K (Jan 1990). "Molecular cloning and chromosomal assignment of a human perforin (PFP) gene". Immunogenetics 30 (6): 452–7. doi:10.1007/BF02421177. PMID 2592021.
^ ^a ^b ^c "Entrez Gene: PRF1 perforin 1 (pore forming protein)".
^ Tschopp J, Masson D, Stanley KK (1986). "Structural/functional similarity between proteins involved in complement- and cytotoxic T-lymphocyte-mediated cytolysis". Nature 322 (6082): 831–4. doi:10.1038/322831a0. PMID 2427956.
^ Thiery J, Keefe D, Boulant S, Boucrot E, Walch M, Martinvalet D, Goping IS, Bleackley RC, Kirchhausen T, Lieberman J (2011). "Perforin pores in the endosomal membrane trigger the release of endocytosed granzyme B into the cytosol of target cells". Nat. Immunol. 12 (8): 770–7. doi:10.1038/ni.2050. PMC 3140544. PMID 21685908.
^ Andrin C, Pinkoski MJ, Burns K, et al. (July 1998). "Interaction between a Ca2+-binding protein calreticulin and perforin, a component of the cytotoxic T-cell granules". Biochemistry 37 (29): 10386–94. doi:10.1021/bi980595z. PMID 9671507.

External links

perforin at the US National Library of Medicine Medical Subject Headings (MeSH)

Perforin at NLM Genetics Home Reference

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UpToDate Contents

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5. 移植片対宿主病の病因 pathogenesis of graft versus host disease

English Journal

Protective effect of polysaccharides on simulated microgravity-induced functional inhibition of human NK cells.

Huyan T, Li Q, Yang H, Jin ML, Zhang MJ, Ye LJ, Li J, Huang QS, Yin DC.SourceKey Laboratory for Space Bioscience and Space Biotechnology, School of Life Sciences, Northwestern Polytechnical University, 127 Youyi Xilu, Xi'an 710072, Shaanxi, PR China; School of Materials Science and Engineering, Northwestern Polytechnical University, 127 Youyi Xilu, Xi'an 710072, Shaanxi, PR China.
Carbohydrate polymers.Carbohydr Polym.2014 Jan 30;101:819-27. doi: 10.1016/j.carbpol.2013.10.021. Epub 2013 Oct 12.
Polysaccharides are believed to be strong immunostimulants that can promote the proliferation and activity of T cells, B cells, macrophages and natural killer (NK) cells. This study aimed to investigate the effects of five polysaccharides (Grifola frondosa polysaccharide (GFP), lentinan (LNT), G. lu
PMID 24299844

The PFP/RAG2 double-knockout mouse in metastasis research: small-cell lung cancer and prostate cancer.

Müller I, Ullrich S.SourceInstitute for Anatomy, Experimental Morphology, University Medical Center Hamburg-Eppendorf, Hamburg, Germany.
Methods in molecular biology (Clifton, N.J.).Methods Mol Biol.2014;1070:191-201. doi: 10.1007/978-1-4614-8244-4_14.
Patients with small-cell lung cancer (SCLC) and prostate cancer (PCa) as well as other solid tumors may have micro- or macro-metastatic spread at an early stage of the disease. SCLC and PCa xenograft transfer models in immunodeficient mice fail to model this metastatic spread in vivo. In both tumor
PMID 24092441

Defining the interaction of perforin with calcium and the phospholipid membrane.

Traore DA, Brennan AJ, Law RH, Dogovski C, Perugini MA, Lukoyanova N, Leung EW, Norton RS, Lopez JA, Browne KA, Yagita H, Lloyd GJ, Ciccone A, Verschoor S, Trapani JA, Whisstock JC, Voskoboinik I.Source††Crystallography, Institute of Structural and Molecular Biology, Birkbeck College, Malet Street, London WC1E 7HX, U.K.
The Biochemical journal.Biochem J.2013 Dec 15;456(3):323-35. doi: 10.1042/BJ20130999.
Following its secretion from cytotoxic lymphocytes into the immune synapse, perforin binds to target cell membranes through its Ca2+-dependent C2 domain. Membrane-bound perforin then forms pores that allow passage of pro-apoptopic granzymes into the target cell. In the present study, structural and
PMID 24070258

Japanese Journal

未感作T細胞を強く活性化するウレアーゼ欠損HSP70-MMP-II融合蛋白産生性リコンビナントBCGの作出

牧野正彦,向井徹
日本ハンセン病学会雑誌 = Japanese journal of leprosy 81(3), 199-203, 2012-09-01
… From naïve CD8+ T cells, effector T cells producing perforin and memory T cells having migration markers, were produced by BCG-D70M stimulation. …
NAID 10031026346

Adult hemophagocytic lymphohistiocytosis with severe pulmonary hypertension and a novel perforin gene mutation

GERARD Lauren M.,XING Katharine,SHERIFI Ines,GRANTON John,BARTH David,ABDELHALEEM Mohamed,BERGERON Catherine,WEITZMAN Sheila,CSERTI-GAZDEWICH Christine
International journal of hematology 95(4), 445-450, 2012-04-01
NAID 10030632732

Lymphoid Neoplasms in Swine

OGIHARA Kikumi,OHBA Takemi,TAKAI Hikaru [他],ISHIKAWA Yoshiharu,KADOTA Koichi
Journal of Veterinary Medical Science 74(2), 149-154, 2012
… Instead of TdT, perforin was expressed in γδ T cell lymphomas (cases 13-17), whose histological characteristics were epitheliotropism, homing into T cell zones of lymphatic tissues, and cytological atypia and pleomorphism. …
NAID 130001033059

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★リンクテーブル★

リンク元	「cytolysin」「パーフォリン」

「cytolysin」

Perforin 1 (pore forming protein)
	; The structure of a MACPF domain containing protein Plu-MACPF: PDB 2QP2 The MACPF domain is in cyan/pink. Another domain, the β prism domain is in orange. Two calcium atoms are in grey.
Identifiers
Symbols	PRF1 ; FLH2; HPLH2; P1; PFN1; PFP
External IDs	OMIM: 170280 MGI: 97551 HomoloGene: 3698 ChEMBL: 5480 GeneCards: PRF1 Gene
Gene ontology
Molecular function	• calcium ion binding; • protein binding; • wide pore channel activity;
Cellular component	• extracellular region; • plasma membrane; • integral to membrane; • cytoplasmic membrane-bounded vesicle; • endosome lumen; • cytolytic granule;
Biological process	• defense response to tumor cell; • immune response to tumor cell; • apoptotic process; • cellular defense response; • cytolysis; • protein homooligomerization; • defense response to virus;
	Sources: Amigo / QuickGO
RNA expression pattern
	More reference expression data
Orthologs
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