Toll-like receptor 2 (TLR2), often designated as CD282 (cluster of differentiation 282) is a type I transmembrane protein belong to the large homologous family of Toll-like receptors. TLR2 acts as functional receptor for both Gram-positive and Gram-negative. Like all other members of the TLR family, TLR2 is composed of an extracellular domain containing multiple leucine rich repeats (LRRs), a transmembrane region and a cytoplasmic tail TIR domain containing conserved. TLR2 maps to chromosome 4q31-32 and encodes a putative 784 amino acid protein with 19 N-terminal LLRs and a calculated molecular weight of 84 kDa (1, 2, 3). The comparison of the amino acid sequence revealed that TLR2, TLR1, TLR6 and TLR form a subfamily, which probably diverged from a common ancestral gene. In humans, TLR10 is also a member of this subfamily TLR2. Among all TLRs, TLR1 and TLR6 have the highest overall identity of the amino acid sequence that is 66% and a similar genomic structure and therefore are assumed to be products of the evolution of gene duplication.
In vivo transcripts for TLR2 is observed suggesting that the mRNA is alternatively spliced. TLR2 mRNA expression is observed in the brain, heart, lung, spleen, and tissues and is higher in PBLs, specifically those of myelomonocytic origin. In vitro PMA-differentiated THP-1, TLR2 is more important autocrine-stimulated IL-6 and TNF-α, IL-1β and IL-10. Moreover, the TLR2 mRNA expression is elevated after exposure to both Gram-positive and Gram-negative. The increased expression of TLR2 on monocytes and granulocytes in the exposure to Gram-negative bacteria is very modest. Furthermore, TLR2 appears to be regulated in mononuclear cells in disorders such as chronic obstructive pulmonary disease, infections with influenza virus, and sepsis
TLR2 act as signal transducers for various bacterial components, including lipoproteins derivative of M. TB burgdorfei Borrelia, Treponema, Mycoplasma fermentans pallidium. In addition, TLR2 mediates responses cell to a variety of infectious pathogens and their products, including yeast cells walls, whole mycobacteria, mycobacterial ara-lipoarabinomannan, whole Gram-positive bacteria, Trypanosoma cruzi (peptidoglycan PGN), Treponema glycolipid anchor glycophosphatidylinositol. TLR2 forms heterodimers with TLR1, TLR6 and possibly TLR10, where each complex is particularly sensitive to TLR2 subsets of pathogen-associated molecular partners patterns (PAMPs). There is evidence that TLR6 and TLR2 function together to detect Gram-positive bacteria, PGN and zymose, whereas TLR2 functions by alone or with different TLR TLR6 to detect bacterial lipopeptides. Recent studies have suggested that, like TLR4, TLR2 complex requires CD14 and MD-2 for the detection of PAMPs and signaling. (4, 5) Upon recognition of ligands, recruits both TLR2 TIR domain containing the classification TIRAP adapter and signaling adapter MyD88 and initiates the MyD88-dependent pathway. The MyD88-dependent pathway activates the nuclear factor (NF)-kB, protein activator-1 (AP-1) and interferon regulatory factor 5 (IRF5), which induce the expression inflammatory cytokines such as IL-6, IL-12 and TNFa. (6)
In addition to the detection of patterns I, TLR2 complexes are also capable of auto detecting patterns changed, as shown by the necrotic cells. Furthermore, recent studies indicate that TLR2 is recruited to phagosomes and may be directly involved in the internalization of microbial products in cells.
Reference:
1. Rock, FL et al. (1998) Proc. Natl. Acad. Sci USA 95:588.
2. Chaudhary, PM et al. (1998) Blood 91:4020.
3. Dunne, A. & LAJ O'Neill (2003) Sci STKE 2003: RE3.
lang = "DE"> 4. Modlin, RL (2002) Ann. Allergy Asthma Immunol. 88:543.
5. J Endotoxin Res 2000, 6 (5) :401-5
6. Annual Review of Biochemistry Vol 76: 447-480 (Published July 2007)
AccessPort with bad intake (NON FUNCTIONAL)
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