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{{Infobox_gene}}
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'''Granulysin''', also known as '''GNLY''', is a [[protein]] which in humans is encoded by the ''GNLY'' [[gene]].<ref name="entrez"/>
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== Function ==
| update_protein_box = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
Granulysin is a [[protein]] present in cytotoxic granules of [[cytotoxic T cells]] and [[natural killer cells]]. Granulysin is a member of the [[saposin]]-like protein (SAPLIP) family and is released from cytotoxic T cells upon antigen stimulation. Granulysin has [[antimicrobial]] activity against [[M. tuberculosis]] and other organisms. Granulysin is alternatively spliced, resulting in the NKG5 and 519 transcripts.<ref name="entrez">{{cite web | title = Entrez Gene: GNLY granulysin| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10578| accessdate = }}</ref>
{{GNF_Protein_box
| image = PBB_Protein_GNLY_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1l9l.
| PDB = {{PDB2|1l9l}}
| Name = Granulysin
| HGNCid = 4414
| Symbol = GNLY
| AltSymbols =; 519; D2S69E; LAG-2; LAG2; NKG5; TLA519
| OMIM = 188855
| ECnumber = 
| Homologene = 88739
| MGIid = 
| GeneAtlas_image1 = PBB_GE_GNLY_37145_at_tn.png
| GeneAtlas_image2 = PBB_GE_GNLY_205495_s_at_tn.png
| Function =
| Component = {{GNF_GO|id=GO:0005615 |text = extracellular space}}
| Process = {{GNF_GO|id=GO:0006805 |text = xenobiotic metabolic process}} {{GNF_GO|id=GO:0006968 |text = cellular defense response}} {{GNF_GO|id=GO:0042742 |text = defense response to bacterium}} {{GNF_GO|id=GO:0050832 |text = defense response to fungus}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 10578
    | Hs_Ensembl = ENSG00000115523
    | Hs_RefseqProtein = NP_006424
    | Hs_RefseqmRNA = NM_006433
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 2
    | Hs_GenLoc_start = 85774925
    | Hs_GenLoc_end = 85779380
    | Hs_Uniprot = P22749
    | Mm_EntrezGene = 
    | Mm_Ensembl = 
    | Mm_RefseqmRNA = 
    | Mm_RefseqProtein = 
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 
    | Mm_GenLoc_start = 
    | Mm_GenLoc_end = 
    | Mm_Uniprot = 
  }}
}}
'''Granulysin''', also known as '''GNLY''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: GNLY granulysin| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10578| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
Granulysin is a cytolytic and proinflammatory molecule first identified by a screen for genes expressed “late” (3–5 days) after activation of human peripheral blood mononuclear cells.<ref name="pmid2434598">{{cite journal |vauthors=Jongstra J, Schall TJ, Dyer BJ, Clayberger C, Jorgensen J, Davis MM, Krensky AM | title = The isolation and sequence of a novel gene from a human functional T cell line | journal = J. Exp. Med. | volume = 165 | issue = 3 | pages = 601–14 |date=March 1987 | pmid = 2434598 | pmc = 2188281 | doi = 10.1084/jem.165.3.601| url =  }}</ref> Granulysin is present in cytolytic granules of cytotoxic T lymphocytes (CTL) and natural killer (NK) cells. Granulysin is made as a 15 kD molecule, and a portion of it is cleaved at both the amino and carboxy termini into a 9 kD form. The 9 kD form is released by receptor-mediated granule exocytosis while the 15 kD form is constitutively secreted.  Recombinant 9 kD granulysin is broadly cytolytic against tumors and microbes, including gram positive and gram negative bacteria, fungi/yeast and parasites.<ref name="pmid9756476">{{cite journal |vauthors=Stenger S, Hanson DA, Teitelbaum R, Dewan P, Niazi KR, Froelich CJ, Ganz T, Thoma-Uszynski S, Melián A, Bogdan C, Porcelli SA, Bloom BR, Krensky AM, Modlin RL | title = An antimicrobial activity of cytolytic T cells mediated by granulysin | journal = Science | volume = 282 | issue = 5386 | pages = 121–5 |date=October 1998 | pmid = 9756476 | doi = 10.1126/science.282.5386.121 | url =  }}</ref> 9kD granulysin is also a chemoattractant for T lymphocytes, monocytes, and other inflammatory cells and activates the expression of a number of cytokines, including RANTES, MCP-1, MCP-3, MIP-1α, IL-10, IL-1, IL-6 and IFNα.<ref name="pmid15843520">{{cite journal |vauthors=Deng A, Chen S, Li Q, Lyu SC, Clayberger C, Krensky AM | title = Granulysin, a cytolytic molecule, is also a chemoattractant and proinflammatory activator | journal = J. Immunol. | volume = 174 | issue = 9 | pages = 5243–8 |date=May 2005 | pmid = 15843520 | doi = 10.4049/jimmunol.174.9.5243| url = http://www.jimmunol.org/cgi/content/abstract/174/9/5243 }}</ref>  Mice do not have a granulysin homolog, but  transgenic mice expressing human granulysin have been engineered.<ref name="pmid17182542">{{cite journal |vauthors=Huang LP, Lyu SC, Clayberger C, Krensky AM | title = Granulysin-Mediated Tumor Rejection in Transgenic Mice | journal = J. Immunol. | volume = 178 | issue = 1 | pages = 77–84 |date=January 2007 | pmid = 17182542 | doi = 10.4049/jimmunol.178.1.77| url = http://www.jimmunol.org/cgi/content/full/178/1/77| pmc = 2664664 }}</ref> Granulysin has been implicated in a myriad of diseases including [[infection]], [[cancer]], [[Organ transplantation|transplantation]], [[autoimmunity]], skin and reproductive maladies.<ref name="pmid19254247">{{cite journal |vauthors=Krensky AM, Clayberger C | title = Biology and clinical relevance of granulysin | journal = Tissue Antigens | volume = 73 | issue = 3 | pages = 193–8 |date=March 2009 | pmid = 19254247 | doi = 10.1111/j.1399-0039.2008.01218.x | url = | pmc = 2679253 }}</ref>
{{PBB_Summary
| section_title =  
| summary_text = Granulysin is a protein present in cytotoxic granules of cytotoxic T lymphocytes and natural killer cells. Granulysin is a member of the saposin-like protein (SAPLIP) family and is located in the cytotoxic granules of T cells, which are released upon antigen stimulation. Granulysin has antimicrobial activity against M. tuberculosis and other organisms. Granulysin is alternatively spliced, resulting in the NKG5 and 519 transcripts.<ref name="entrez">{{cite web | title = Entrez Gene: GNLY granulysin| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10578| accessdate = }}</ref>
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=Peña SV, Krensky AM |title=Granulysin, a new human cytolytic granule-associated protein with possible involvement in cell-mediated cytotoxicity. |journal=Semin. Immunol. |volume=9 |issue= 2 |pages= 117-25 |year= 1997 |pmid= 9194222 |doi= 10.1006/smim.1997.0061 }}
*{{cite journal  |vauthors=Peña SV, Krensky AM |title=Granulysin, a new human cytolytic granule-associated protein with possible involvement in cell-mediated cytotoxicity |journal=Semin. Immunol. |volume=9 |issue= 2 |pages= 117–25 |year= 1997 |pmid= 9194222 |doi= 10.1006/smim.1997.0061 }}
*{{cite journal  | author=Krensky AM |title=Granulysin: a novel antimicrobial peptide of cytolytic T lymphocytes and natural killer cells. |journal=Biochem. Pharmacol. |volume=59 |issue= 4 |pages= 317-20 |year= 2000 |pmid= 10644038 |doi=  }}
*{{cite journal  | author=Krensky AM |title=Granulysin: a novel antimicrobial peptide of cytolytic T lymphocytes and natural killer cells |journal=Biochem. Pharmacol. |volume=59 |issue= 4 |pages= 317–20 |year= 2000 |pmid= 10644038 |doi=10.1016/S0006-2952(99)00177-X }}
*{{cite journal  | author=Donlon TA, Krensky AM, Clayberger C |title=Localization of the human T lymphocyte activation gene 519 (D2S69E) to chromosome 2p12----q11. |journal=Cytogenet. Cell Genet. |volume=53 |issue= 4 |pages= 230-1 |year= 1990 |pmid= 2209093 |doi=  }}
*{{cite journal  |vauthors=Donlon TA, Krensky AM, Clayberger C |title=Localization of the human T lymphocyte activation gene 519 (D2S69E) to chromosome 2p12----q11 |journal=Cytogenet. Cell Genet. |volume=53 |issue= 4 |pages= 230–1 |year= 1990 |pmid= 2209093 |doi=10.1159/000132938 }}
*{{cite journal  | author=Yabe T, McSherry C, Bach FH, Houchins JP |title=A cDNA clone expressed in natural killer and T cells that likely encodes a secreted protein. |journal=J. Exp. Med. |volume=172 |issue= 4 |pages= 1159-63 |year= 1990 |pmid= 2212946 |doi=  }}
*{{cite journal  |vauthors=Yabe T, McSherry C, Bach FH, Houchins JP |title=A cDNA clone expressed in natural killer and T cells that likely encodes a secreted protein |journal=J. Exp. Med. |volume=172 |issue= 4 |pages= 1159–63 |year= 1990 |pmid= 2212946 |doi=10.1084/jem.172.4.1159  | pmc=2188624 }}
*{{cite journal  | author=Jongstra J, Schall TJ, Dyer BJ, ''et al.'' |title=The isolation and sequence of a novel gene from a human functional T cell line. |journal=J. Exp. Med. |volume=165 |issue= 3 |pages= 601-14 |year= 1987 |pmid= 2434598 |doi=  }}
*{{cite journal  |vauthors=Jongstra J, Schall TJ, Dyer BJ |title=The isolation and sequence of a novel gene from a human functional T cell line |journal=J. Exp. Med. |volume=165 |issue= 3 |pages= 601–14 |year= 1987 |pmid= 2434598 |doi=10.1084/jem.165.3.601  | pmc=2188281 |display-authors=etal}}
*{{cite journal  | author=Houchins JP, Kricek F, Chujor CS, ''et al.'' |title=Genomic structure of NKG5, a human NK and T cell-specific activation gene. |journal=Immunogenetics |volume=37 |issue= 2 |pages= 102-7 |year= 1993 |pmid= 8423048 |doi=  }}
*{{cite journal  |vauthors=Houchins JP, Kricek F, Chujor CS |title=Genomic structure of NKG5, a human NK and T cell-specific activation gene |journal=Immunogenetics |volume=37 |issue= 2 |pages= 102–7 |year= 1993 |pmid= 8423048 |doi=10.1007/BF00216832 |display-authors=etal}}
*{{cite journal  | author=Peña SV, Hanson DA, Carr BA, ''et al.'' |title=Processing, subcellular localization, and function of 519 (granulysin), a human late T cell activation molecule with homology to small, lytic, granule proteins. |journal=J. Immunol. |volume=158 |issue= 6 |pages= 2680-8 |year= 1997 |pmid= 9058801 |doi=  }}
*{{cite journal  |vauthors=Peña SV, Hanson DA, Carr BA |title=Processing, subcellular localization, and function of 519 (granulysin), a human late T cell activation molecule with homology to small, lytic, granule proteins |journal=J. Immunol. |volume=158 |issue= 6 |pages= 2680–8 |year= 1997 |pmid= 9058801 |doi=  |display-authors=etal}}
*{{cite journal  | author=Stenger S, Hanson DA, Teitelbaum R, ''et al.'' |title=An antimicrobial activity of cytolytic T cells mediated by granulysin. |journal=Science |volume=282 |issue= 5386 |pages= 121-5 |year= 1998 |pmid= 9756476 |doi=  }}
*{{cite journal  |vauthors=Stenger S, Hanson DA, Teitelbaum R |title=An antimicrobial activity of cytolytic T cells mediated by granulysin |journal=Science |volume=282 |issue= 5386 |pages= 121–5 |year= 1998 |pmid= 9756476 |doi=10.1126/science.282.5386.121 |display-authors=etal}}
*{{cite journal  | author=Hanson DA, Kaspar AA, Poulain FR, Krensky AM |title=Biosynthesis of granulysin, a novel cytolytic molecule. |journal=Mol. Immunol. |volume=36 |issue= 7 |pages= 413-22 |year= 1999 |pmid= 10449094 |doi=  }}
*{{cite journal  |vauthors=Hanson DA, Kaspar AA, Poulain FR, Krensky AM |title=Biosynthesis of granulysin, a novel cytolytic molecule |journal=Mol. Immunol. |volume=36 |issue= 7 |pages= 413–22 |year= 1999 |pmid= 10449094 |doi=10.1016/S0161-5890(99)00063-2 }}
*{{cite journal  | author=Kaspar AA, Okada S, Kumar J, ''et al.'' |title=A distinct pathway of cell-mediated apoptosis initiated by granulysin. |journal=J. Immunol. |volume=167 |issue= 1 |pages= 350-6 |year= 2001 |pmid= 11418670 |doi=  }}
*{{cite journal  |vauthors=Kaspar AA, Okada S, Kumar J |title=A distinct pathway of cell-mediated apoptosis initiated by granulysin |journal=J. Immunol. |volume=167 |issue= 1 |pages= 350–6 |year= 2001 |pmid= 11418670 |doi=  10.4049/jimmunol.167.1.350|display-authors=etal}}
*{{cite journal  | author=Kitamura N, Koshiba M, Horie O, Ryo R |title=Expression of granulysin mRNA in the human megakaryoblastic leukemia cell line CMK. |journal=Acta Haematol. |volume=108 |issue= 1 |pages= 13-8 |year= 2002 |pmid= 12145461 |doi=  }}
*{{cite journal  |vauthors=Kitamura N, Koshiba M, Horie O, Ryo R |title=Expression of granulysin mRNA in the human megakaryoblastic leukemia cell line CMK |journal=Acta Haematol. |volume=108 |issue= 1 |pages= 13–8 |year= 2002 |pmid= 12145461 |doi=10.1159/000063061 }}
*{{cite journal  | author=Ma LL, Spurrell JC, Wang JF, ''et al.'' |title=CD8 T cell-mediated killing of Cryptococcus neoformans requires granulysin and is dependent on CD4 T cells and IL-15. |journal=J. Immunol. |volume=169 |issue= 10 |pages= 5787-95 |year= 2003 |pmid= 12421959 |doi=  }}
*{{cite journal  |vauthors=Ma LL, Spurrell JC, Wang JF |title=CD8 T cell-mediated killing of Cryptococcus neoformans requires granulysin and is dependent on CD4 T cells and IL-15 |journal=J. Immunol. |volume=169 |issue= 10 |pages= 5787–95 |year= 2003 |pmid= 12421959 |doi=  10.4049/jimmunol.169.10.5787|display-authors=etal}}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal  |vauthors=Strausberg RL, Feingold EA, Grouse LH |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 |display-authors=etal}}
*{{cite journal  | author=Ericson KG, Fadeel B, Andersson M, ''et al.'' |title=Sequence analysis of the granulysin and granzyme B genes in familial hemophagocytic lymphohistiocytosis. |journal=Hum. Genet. |volume=112 |issue= 1 |pages= 98-9 |year= 2003 |pmid= 12483306 |doi= 10.1007/s00439-002-0841-0 }}
*{{cite journal  |vauthors=Ericson KG, Fadeel B, Andersson M |title=Sequence analysis of the granulysin and granzyme B genes in familial hemophagocytic lymphohistiocytosis |journal=Hum. Genet. |volume=112 |issue= 1 |pages= 98–9 |year= 2003 |pmid= 12483306 |doi= 10.1007/s00439-002-0841-0 |display-authors=etal}}
*{{cite journal  | author=Anderson DH, Sawaya MR, Cascio D, ''et al.'' |title=Granulysin crystal structure and a structure-derived lytic mechanism. |journal=J. Mol. Biol. |volume=325 |issue= 2 |pages= 355-65 |year= 2003 |pmid= 12488100 |doi=  }}
*{{cite journal  |vauthors=Anderson DH, Sawaya MR, Cascio D |title=Granulysin crystal structure and a structure-derived lytic mechanism |journal=J. Mol. Biol. |volume=325 |issue= 2 |pages= 355–65 |year= 2003 |pmid= 12488100 |doi=10.1016/S0022-2836(02)01234-2 |display-authors=etal}}
*{{cite journal  | author=Gansert JL, Kiessler V, Engele M, ''et al.'' |title=Human NKT cells express granulysin and exhibit antimycobacterial activity. |journal=J. Immunol. |volume=170 |issue= 6 |pages= 3154-61 |year= 2003 |pmid= 12626573 |doi=  }}
*{{cite journal  |vauthors=Gansert JL, Kiessler V, Engele M |title=Human NKT cells express granulysin and exhibit antimycobacterial activity |journal=J. Immunol. |volume=170 |issue= 6 |pages= 3154–61 |year= 2003 |pmid= 12626573 |doi=  10.4049/jimmunol.170.6.3154|display-authors=etal}}
*{{cite journal  | author=Ogawa K, Takamori Y, Suzuki K, ''et al.'' |title=Granulysin in human serum as a marker of cell-mediated immunity. |journal=Eur. J. Immunol. |volume=33 |issue= 7 |pages= 1925-33 |year= 2003 |pmid= 12884856 |doi= 10.1002/eji.200323977 }}
*{{cite journal  |vauthors=Ogawa K, Takamori Y, Suzuki K |title=Granulysin in human serum as a marker of cell-mediated immunity |journal=Eur. J. Immunol. |volume=33 |issue= 7 |pages= 1925–33 |year= 2003 |pmid= 12884856 |doi= 10.1002/eji.200323977 |display-authors=etal}}
*{{cite journal  | author=Kotsch K, Mashreghi MF, Bold G, ''et al.'' |title=Enhanced granulysin mRNA expression in urinary sediment in early and delayed acute renal allograft rejection. |journal=Transplantation |volume=77 |issue= 12 |pages= 1866-75 |year= 2004 |pmid= 15223905 |doi=  }}
*{{cite journal  |vauthors=Kotsch K, Mashreghi MF, Bold G |title=Enhanced granulysin mRNA expression in urinary sediment in early and delayed acute renal allograft rejection |journal=Transplantation |volume=77 |issue= 12 |pages= 1866–75 |year= 2004 |pmid= 15223905 |doi=10.1097/01.TP.0000131157.19937.3F |display-authors=etal}}
}}
}}
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{{refend}}
{{PDB Gallery|geneid=10578}}
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Latest revision as of 08:53, 31 August 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Granulysin, also known as GNLY, is a protein which in humans is encoded by the GNLY gene.[1]

Function

Granulysin is a protein present in cytotoxic granules of cytotoxic T cells and natural killer cells. Granulysin is a member of the saposin-like protein (SAPLIP) family and is released from cytotoxic T cells upon antigen stimulation. Granulysin has antimicrobial activity against M. tuberculosis and other organisms. Granulysin is alternatively spliced, resulting in the NKG5 and 519 transcripts.[1]

Granulysin is a cytolytic and proinflammatory molecule first identified by a screen for genes expressed “late” (3–5 days) after activation of human peripheral blood mononuclear cells.[2] Granulysin is present in cytolytic granules of cytotoxic T lymphocytes (CTL) and natural killer (NK) cells. Granulysin is made as a 15 kD molecule, and a portion of it is cleaved at both the amino and carboxy termini into a 9 kD form. The 9 kD form is released by receptor-mediated granule exocytosis while the 15 kD form is constitutively secreted. Recombinant 9 kD granulysin is broadly cytolytic against tumors and microbes, including gram positive and gram negative bacteria, fungi/yeast and parasites.[3] 9kD granulysin is also a chemoattractant for T lymphocytes, monocytes, and other inflammatory cells and activates the expression of a number of cytokines, including RANTES, MCP-1, MCP-3, MIP-1α, IL-10, IL-1, IL-6 and IFNα.[4] Mice do not have a granulysin homolog, but transgenic mice expressing human granulysin have been engineered.[5] Granulysin has been implicated in a myriad of diseases including infection, cancer, transplantation, autoimmunity, skin and reproductive maladies.[6]

References

  1. ↑ 1.0 1.1 "Entrez Gene: GNLY granulysin".
  2. ↑ Jongstra J, Schall TJ, Dyer BJ, Clayberger C, Jorgensen J, Davis MM, Krensky AM (March 1987). "The isolation and sequence of a novel gene from a human functional T cell line". J. Exp. Med. 165 (3): 601–14. doi:10.1084/jem.165.3.601. PMC 2188281. PMID 2434598.
  3. ↑ Stenger S, Hanson DA, Teitelbaum R, Dewan P, Niazi KR, Froelich CJ, Ganz T, Thoma-Uszynski S, Melián A, Bogdan C, Porcelli SA, Bloom BR, Krensky AM, Modlin RL (October 1998). "An antimicrobial activity of cytolytic T cells mediated by granulysin". Science. 282 (5386): 121–5. doi:10.1126/science.282.5386.121. PMID 9756476.
  4. ↑ Deng A, Chen S, Li Q, Lyu SC, Clayberger C, Krensky AM (May 2005). "Granulysin, a cytolytic molecule, is also a chemoattractant and proinflammatory activator". J. Immunol. 174 (9): 5243–8. doi:10.4049/jimmunol.174.9.5243. PMID 15843520.
  5. ↑ Huang LP, Lyu SC, Clayberger C, Krensky AM (January 2007). "Granulysin-Mediated Tumor Rejection in Transgenic Mice". J. Immunol. 178 (1): 77–84. doi:10.4049/jimmunol.178.1.77. PMC 2664664. PMID 17182542.
  6. ↑ Krensky AM, Clayberger C (March 2009). "Biology and clinical relevance of granulysin". Tissue Antigens. 73 (3): 193–8. doi:10.1111/j.1399-0039.2008.01218.x. PMC 2679253. PMID 19254247.

Further reading



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