Our study group has been examining the role of p38 MAPK signaling pathway on number microbial interactions during periodontal disease. This review intends to talk about the significance of the potential and the p38 MAPK pathway to govern this pathway Syk inhibition for therapeutic applications in vivo. From the time the initial description of Toll like receptors in the mid late 90s, the field of natural immunity has been greatly stimulated and the implications of these receptors on the regulation of host response has been intensively studied. Importantly, the functions of TLRs in inflammation and immune response have been extended, therefore it is now known these receptors not merely understand numerous microbial associated molecular patterns to stimulate innate immune response, but they may also bind to endogenous compounds based on damaged tissue and have a task in inflammation and adaptive immune response. The TLR family currently consists of more than 13 people, each effective at realizing different PAMPs. These receptors are expressed by immune cells such as neutrophils, macrophages and dendritic cells as well PF299804 molecular weight as by low immune resident cells, such as periodontal fibroblasts and gingival epithelial cells. In periodontal tissues, expression of TLR2 and TLR4 has been positively correlated with inflammation, in addition to in intestinal inflammation. On another hand, reduced expression of TLR mRNA in the oral mucosa of periodontitis patients has been noted, nevertheless concomitantly with increased infiltration of the mucosa with TLRpositive inflammatory cells. This has been regarded by the writers as a possible consequence of the repeated Eumycetoma and extended problem of this tissue with PAMPs and an effort of the host to reestablish tissue homeostasis, as in a immune tolerance mechanism. TLRs are single move transmembrane proteins with an N terminal offering leucine rich repeats that are accountable for the recognition of their ligands and with a C terminal cytoplasmic domain that’s very similar to the cytoplasmic region of the interleukin 1 receptor. Nucleotide oligomerization domain proteins are cytosolic proteins that also have leucine loaded repeats and were initially referred to as intracellular TLRs that understand PAMPs connected with bacteria entering the cytosol, nevertheless these proteins have also demonstrated an ability to regulate various signaling pathways, including p38 MAPK and NF?B. Our study chk2 inhibitor group has observed that Nod1 and Nod2 are expected for transcriptional activation of RANKL mediated by TLR2 and TLR4 signaling, however only Nod1 becomes necessary for expression of RANKL mRNA induced by IL 1 receptor signaling. This shows the complexity of TLR signaling and the cross talk to other signaling pathways involved because the cytosolic domains of TLRs and IL 1 receptor are similar.