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TLRs are highly conserved from ''Drosophila'' to humans and share structural and functional similarities. They recognize [[pathogen-associated molecular pattern]]s (PAMPs) that are expressed on infectious agents, and mediate the production of [[cytokine]]s necessary for the development of effective immunity. The various TLRs exhibit different patterns of expression. This gene is ubiquitously expressed, and at higher levels than other TLR genes. Different length transcripts presumably resulting from use of alternative polyadenylation site, and/or from alternative splicing, have been noted for this gene.<ref name="urlGene Result">{{cite web | url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7096 | title = SRF serum response factor | author = | authorlink = | format = | work = Entrez Gene | publisher = National Center for Biotechnology Information, National Institutes of Health| pages = | archiveurl = | archivedate = | quote = | accessdate = }}</ref>
TLRs are highly conserved from ''Drosophila'' to humans and share structural and functional similarities. They recognize [[pathogen-associated molecular pattern]]s (PAMPs) that are expressed on infectious agents, and mediate the production of [[cytokine]]s necessary for the development of effective immunity. The various TLRs exhibit different patterns of expression. This gene is ubiquitously expressed, and at higher levels than other TLR genes. Different length transcripts presumably resulting from use of alternative polyadenylation site, and/or from alternative splicing, have been noted for this gene.<ref name="urlGene Result">{{cite web | url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7096 | title = SRF serum response factor | author = | authorlink = | format = | work = Entrez Gene | publisher = National Center for Biotechnology Information, National Institutes of Health| pages = | archiveurl = | archivedate = | quote = | accessdate = }}</ref>


TLR1 recognises [[peptidoglycan]] and (triacyl) [[lipoprotein]]s in concert with [[TLR2]] (as a heterodimer).<ref name="pmid18056480">{{cite journal | vauthors = Farhat K, Riekenberg S, Heine H, Debarry J, Lang R, Mages J, Buwitt-Beckmann U, Röschmann K, Jung G, Wiesmüller KH, Ulmer AJ | title = Heterodimerization of TLR2 with TLR1 or TLR6 expands the ligand spectrum but does not lead to differential signaling | journal = J. Leukoc. Biol. | volume = 83 | issue = 3 | pages = 692–701 | date = March 2008 | pmid = 18056480 | doi = 10.1189/jlb.0807586 }}</ref><ref name="pmid17889651">{{cite journal | vauthors = Jin MS, Kim SE, Heo JY, Lee ME, Kim HM, Paik SG, Lee H, Lee JO | title = Crystal structure of the TLR1-TLR2 heterodimer induced by binding of a tri-acylated lipopeptide | journal = Cell | volume = 130 | issue = 6 | pages = 1071–82 | date = September 2007 | pmid = 17889651 | doi = 10.1016/j.cell.2007.09.008 }}</ref> Toll-like receptors, including TLR-1, found on the epithelial cell layer that lines the small and large intestine are important players the management of the [[Microbiota (human)|gut microbiota]] and detection of pathogens.<ref>{{cite journal | vauthors = de Kivit S, Tobin MC, Forsyth CB, Keshavarzian A, Landay AL | title = Regulation of Intestinal Immune Responses through TLR Activation: Implications for Pro- and Prebiotics | journal = Frontiers in Immunology | volume = 5 | pages = 60 | date = 2014 | pmid = 24600450 | pmc = 3927311 | doi = 10.3389/fimmu.2014.00060 }}</ref> It is also found on the surface of [[macrophage]]s and [[neutrophil]]s.
TLR1 recognises [[peptidoglycan]] and (triacyl) [[lipoprotein]]s in concert with [[TLR2]] (as a heterodimer).<ref name="pmid18056480">{{cite journal | vauthors = Farhat K, Riekenberg S, Heine H, Debarry J, Lang R, Mages J, Buwitt-Beckmann U, Röschmann K, Jung G, Wiesmüller KH, Ulmer AJ | title = Heterodimerization of TLR2 with TLR1 or TLR6 expands the ligand spectrum but does not lead to differential signaling | journal = J. Leukoc. Biol. | volume = 83 | issue = 3 | pages = 692–701 | date = March 2008 | pmid = 18056480 | doi = 10.1189/jlb.0807586 }}</ref><ref name="pmid17889651">{{cite journal | vauthors = Jin MS, Kim SE, Heo JY, Lee ME, Kim HM, Paik SG, Lee H, Lee JO | title = Crystal structure of the TLR1-TLR2 heterodimer induced by binding of a tri-acylated lipopeptide | journal = Cell | volume = 130 | issue = 6 | pages = 1071–82 | date = September 2007 | pmid = 17889651 | doi = 10.1016/j.cell.2007.09.008 }}</ref> Toll-like receptors, including TLR-1, found on the epithelial cell layer that lines the small and large intestine are important players in the management of the [[Microbiota (human)|gut microbiota]] and detection of pathogens.<ref>{{cite journal | vauthors = de Kivit S, Tobin MC, Forsyth CB, Keshavarzian A, Landay AL | title = Regulation of Intestinal Immune Responses through TLR Activation: Implications for Pro- and Prebiotics | journal = Frontiers in Immunology | volume = 5 | pages = 60 | date = 2014 | pmid = 24600450 | pmc = 3927311 | doi = 10.3389/fimmu.2014.00060 }}</ref> It is also found on the surface of [[macrophage]]s and [[neutrophil]]s.


== Interactions ==
== Interactions ==

Latest revision as of 11:58, 10 January 2019

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TLR 1 is a member of the toll-like receptor family (TLR) of pattern recognition receptors of the innate immune system.[1][2] TLR1 recognizes pathogen-associated molecular pattern with a specificity for gram-positive bacteria. TLR1 has also been designated as CD281 (cluster of differentiation 281).

TLRs are highly conserved from Drosophila to humans and share structural and functional similarities. They recognize pathogen-associated molecular patterns (PAMPs) that are expressed on infectious agents, and mediate the production of cytokines necessary for the development of effective immunity. The various TLRs exhibit different patterns of expression. This gene is ubiquitously expressed, and at higher levels than other TLR genes. Different length transcripts presumably resulting from use of alternative polyadenylation site, and/or from alternative splicing, have been noted for this gene.[3]

TLR1 recognises peptidoglycan and (triacyl) lipoproteins in concert with TLR2 (as a heterodimer).[4][5] Toll-like receptors, including TLR-1, found on the epithelial cell layer that lines the small and large intestine are important players in the management of the gut microbiota and detection of pathogens.[6] It is also found on the surface of macrophages and neutrophils.

Interactions

TLR 1 has been shown to interact with TLR 2.[7]

References

  1. ↑ Rock FL, Hardiman G, Timans JC, Kastelein RA, Bazan JF (January 1998). "A family of human receptors structurally related to Drosophila Toll". Proc. Natl. Acad. Sci. U.S.A. 95 (2): 588–93. doi:10.1073/pnas.95.2.588. PMC 18464. PMID 9435236.
  2. ↑ Lien E, Ingalls RR (January 2002). "Toll-like receptors". Crit. Care Med. 30 (1 Suppl): S1–11. doi:10.1097/00003246-200201001-00001. PMID 11782555.
  3. ↑ "SRF serum response factor". Entrez Gene. National Center for Biotechnology Information, National Institutes of Health.
  4. ↑ Farhat K, Riekenberg S, Heine H, Debarry J, Lang R, Mages J, Buwitt-Beckmann U, Röschmann K, Jung G, Wiesmüller KH, Ulmer AJ (March 2008). "Heterodimerization of TLR2 with TLR1 or TLR6 expands the ligand spectrum but does not lead to differential signaling". J. Leukoc. Biol. 83 (3): 692–701. doi:10.1189/jlb.0807586. PMID 18056480.
  5. ↑ Jin MS, Kim SE, Heo JY, Lee ME, Kim HM, Paik SG, Lee H, Lee JO (September 2007). "Crystal structure of the TLR1-TLR2 heterodimer induced by binding of a tri-acylated lipopeptide". Cell. 130 (6): 1071–82. doi:10.1016/j.cell.2007.09.008. PMID 17889651.
  6. ↑ de Kivit S, Tobin MC, Forsyth CB, Keshavarzian A, Landay AL (2014). "Regulation of Intestinal Immune Responses through TLR Activation: Implications for Pro- and Prebiotics". Frontiers in Immunology. 5: 60. doi:10.3389/fimmu.2014.00060. PMC 3927311. PMID 24600450.
  7. ↑ Takeuchi O, Sato S, Horiuchi T, Hoshino K, Takeda K, Dong Z, Modlin RL, Akira S (Jul 2002). "Cutting edge: role of Toll-like receptor 1 in mediating immune response to microbial lipoproteins". J. Immunol. 169 (1): 10–4. doi:10.4049/jimmunol.169.1.10. PMID 12077222.

External links

This article incorporates text from the United States National Library of Medicine ([2]), which is in the public domain.


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