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Smith Hidde p 대한타이어공업협회 1984 타이어 고무 Vol.111 No.-
본자료는 UN산하기구인 아시아ㆍ태평양 경제사회위원회(ESCAP: Economic and Social Commission for Asia and Pacific)의 요청에 따라 1978년, 네덜란드의 암스테르담 Free대학교 사회경제대학 Hidde P.Smith 교수팀이 네덜란드 정부의 지원으로 2000년까지의 천연고무의 수급 및 가격문제를 분석 전망한 것이다. 따라서 본고에서는 고무제품업계에 다소라도 기여될 수 있는 다음과 같은 주요내용만을 발췌요약하였다.
Kim, Jihee,Huh, Jiwon,Hwang, Misun,Kwon, Eun-Hye,Jung, Da-Jung,Brinkmann, Melanie M.,Jang, Myoung Ho,Ploegh, Hidde L.,Kim, You-Me The American Association of Immunologists, Inc. 2013 JOURNAL OF IMMUNOLOGY Vol.190 No.10
<P>TLRs are divided into two groups based on their subcellular localization patterns. TLR1, 2, 4, 5, and 6 are expressed on the cell surface, whereas the nucleotide-sensing TLRs, such as TLR3, 7, 8, and 9 stay mainly inside cells. The polytopic membrane protein UNC93B1 physically interacts with the nucleotide-sensing TLRs and delivers them from the endoplasmic reticulum to endolysosomes, where the TLRs recognize their ligands and initiate signaling. In cells with nonfunctional UNC93B1, the nucleic acid–sensing TLRs fail to exit the endoplasmic reticulum and consequently do not signal. However, the detailed molecular mechanisms that underlie the UNC93B1-mediated TLR trafficking remain to be clarified. All nucleotide-sensing TLRs contain acidic amino acid residues in the juxtamembrane region between the leucine-rich repeat domain and the transmembrane segment. We show that the D812 and E813 residues of TLR9 and the D699 and E704 residues of TLR3 help to determine the interaction of these TLRs with UNC93B1. Mutation of the acidic residues in TLR3 and TLR9 prevents UNC93B1 binding, as well as impairs TLR trafficking and renders the mutant receptors incapable of transmitting signals. Therefore, the acidic residues in the juxtamembrane region of the nucleotide-sensing TLRs have important functional roles.</P>
Granulin Is a Soluble Cofactor for Toll-like Receptor 9 Signaling
Park, Boyoun,Buti, Ludovico,Lee, Sungwook,Matsuwaki, Takashi,Spooner, Eric,Brinkmann, Melanie ,M.,Nishihara, Masugi,Ploegh, Hidde ,L. Elsevier 2011 Immunity Vol.34 No.4
<P><B>Summary</B></P><P>Toll-like receptor (TLR) signaling plays a critical role in innate and adaptive immune responses and must be tightly controlled. TLR4 uses LPS binding protein, MD-2, and CD14 as accessories to respond to LPS. We therefore investigated the presence of an analagous soluble cofactor that might assist in the recruitment of CpG oligonucleotides (CpG-ODNs) to TLR9. We report the identification of granulin as an essential secreted cofactor that potentiates TLR9-driven responses to CpG-ODNs. Granulin, an unusual cysteine-rich protein, bound to CpG-ODNs and interacted with TLR9. Macrophages from granulin-deficient mice showed not only impaired delivery of CpG-ODNs to endolysosomal compartments, but also decreased interaction of TLR9 with CpG-ODNs. As a consequence, granulin-deficient macrophages showed reduced responses to stimulation with CpG-ODNs, a trait corrected by provision of exogenous granulin. Thus, we propose that granulin contributes to innate immunity as a critical soluble cofactor for TLR9 signaling.</P> <P><B>Highlights</B></P><P>► Granulin binds TLR9 and CpG oligonucleotides ► Granulin is sufficient for intracellular localization of CpG-ODNs ► Granulin is a critical cofactor in enabling TLR9 signal transduction</P>