tapasin

出典: meddic

タパシン TAPBP

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出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2012/04/06 03:37:03」(JST)

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英文文献

  • Expression of tapasin in rainbow trout tissues and cell lines and up regulation in a monocyte/macrophage cell line (RTS11) by a viral mimic and viral infection.
  • Sever L1, Vo NT1, Bols NC1, Dixon B2.Author information 1Department of Biology, University of Waterloo, 200 University Ave W., Waterloo, Ontario N2L 3G1, Canada.2Department of Biology, University of Waterloo, 200 University Ave W., Waterloo, Ontario N2L 3G1, Canada. Electronic address: bdixon@uwaterloo.ca.AbstractTapasin is a transmembrane glycoprotein that acts as a bridge between the transporter associated with antigen processing and the MHC class I receptor in mammals. Through the development of antibody against trout tapasin, this report demonstrates the detection of trout tapasin as a N-glycosylated 48kDa protein. Tissue and cell line distribution revealed that tapasin protein is expressed mainly in immune system organs and in rainbow trout epithelial cell lines from gill (RTgill-W1), liver (RTL-W1), and intestine (RTgutGC). An additional 20kDa band was observed in tissues and cell lines, and appeared to be most prominent in RTgutGC but was absent in peripheral blood leukocytes. Tapasin 48kDa protein was most strongly expressed in RTS11 (monocyte/macrophage cell line) and its regulation following dsRNA stimulation was explored. Upon poly I:C treatment and Chum Salmon Reovirus (CSV) infection, tapasin protein expression was upregulated up to 3.5 fold and 3 fold respectively, in parallel with increased expression of the glycosylated MH class I heavy chain, whereas the expression of the 20kDa form remained unchanged. Overall this work demonstrates the induction of tapasin protein by dsRNA stimulation, which implies its possible conserved regulation during viral infection in teleost cells.
  • Developmental and comparative immunology.Dev Comp Immunol.2013 Dec 7;44(1):86-93. doi: 10.1016/j.dci.2013.11.019. [Epub ahead of print]
  • Tapasin is a transmembrane glycoprotein that acts as a bridge between the transporter associated with antigen processing and the MHC class I receptor in mammals. Through the development of antibody against trout tapasin, this report demonstrates the detection of trout tapasin as a N-glycosylated 48k
  • PMID 24321527
  • The binding of TAPBPR and Tapasin to MHC class I is mutually exclusive.
  • Hermann C, Strittmatter LM, Deane JE, Boyle LH.Author information Department of Pathology, Cambridge Institute of Medical Research, University of Cambridge, Cambridge CB2 0XY, United Kingdom.AbstractThe loading of peptide Ags onto MHC class I molecules is a highly controlled process in which the MHC class I-dedicated chaperone tapasin is a key player. We recently identified a tapasin-related molecule, TAPBPR, as an additional component in the MHC class I Ag-presentation pathway. In this study, we show that the amino acid residues important for tapasin to interact with MHC class I are highly conserved on TAPBPR. We identify specific residues in the N-terminal and C-terminal domains of TAPBPR involved in associating with MHC class I. Furthermore, we demonstrate that residues on MHC class I crucial for its association with tapasin, such as T134, are also essential for its interaction with TAPBPR. Taken together, the data indicate that TAPBPR and tapasin bind in a similar orientation to the same face of MHC class I. In the absence of tapasin, the association of MHC class I with TAPBPR is increased. However, in the absence of TAPBPR, the interaction between MHC class I and tapasin does not increase. In light of our findings, previous data determining the function of tapasin in the MHC class I Ag-processing and presentation pathway must be re-evaluated.
  • Journal of immunology (Baltimore, Md. : 1950).J Immunol.2013 Dec 1;191(11):5743-50. doi: 10.4049/jimmunol.1300929. Epub 2013 Oct 25.
  • The loading of peptide Ags onto MHC class I molecules is a highly controlled process in which the MHC class I-dedicated chaperone tapasin is a key player. We recently identified a tapasin-related molecule, TAPBPR, as an additional component in the MHC class I Ag-presentation pathway. In this study,
  • PMID 24163410
  • A mechanistic basis for the co-evolution of chicken tapasin and major histocompatibility complex class I (MHC I) proteins.
  • van Hateren A, Carter R, Bailey A, Kontouli N, Williams AP, Kaufman J, Elliott T.Author information From the Faculty of Medicine and Institute for Life Science, University of Southampton, Southampton SO16 6YD, United Kingdom.AbstractMHC class I molecules display peptides at the cell surface to cytotoxic T cells. The co-factor tapasin functions to ensure that MHC I becomes loaded with high affinity peptides. In most mammals, the tapasin gene appears to have little sequence diversity and few alleles and is located distal to several classical MHC I loci, so tapasin appears to function in a universal way to assist MHC I peptide loading. In contrast, the chicken tapasin gene is tightly linked to the single dominantly expressed MHC I locus and is highly polymorphic and moderately diverse in sequence. Therefore, tapasin-assisted loading of MHC I in chickens may occur in a haplotype-specific way, via the co-evolution of chicken tapasin and MHC I. Here we demonstrate a mechanistic basis for this co-evolution, revealing differences in the ability of two chicken MHC I alleles to bind and release peptides in the presence or absence of tapasin, where, as in mammals, efficient self-loading is negatively correlated with tapasin-assisted loading. We found that a polymorphic residue in the MHC I α3 domain thought to bind tapasin influenced both tapasin function and intrinsic peptide binding properties. Differences were also evident between the MHC alleles in their interactions with tapasin. Last, we show that a mismatched combination of tapasin and MHC alleles exhibit significantly impaired MHC I maturation in vivo and that polymorphic MHC residues thought to contact tapasin influence maturation efficiency. Collectively, this supports the possibility that tapasin and BF2 proteins have co-evolved, resulting in allele-specific peptide loading in vivo.
  • The Journal of biological chemistry.J Biol Chem.2013 Nov 8;288(45):32797-808. doi: 10.1074/jbc.M113.474031. Epub 2013 Sep 27.
  • MHC class I molecules display peptides at the cell surface to cytotoxic T cells. The co-factor tapasin functions to ensure that MHC I becomes loaded with high affinity peptides. In most mammals, the tapasin gene appears to have little sequence diversity and few alleles and is located distal to sever
  • PMID 24078633

和文文献

  • Human cytomegalovirus inhibits tapasin-dependent peptide loading and optimization of the MHC class I peptide cargo for immune evasion
  • The MHC-encoded class I molecule, H-2K^k, demonstrates distinct requirements of assembly factors for cell surface expression : roles of TAP, Tapasin and β_2-microglobulin

関連リンク

Tapasin Overview: Tapasin is a trans-membrane protein that is located within the endoplasmic reticulum (ER) . Its primary function is to assist in the binding of the MHC I protein with its antigen peptide fragment. It acts as an ...
Tapasin is normally found in stoichiometric amounts with TAP1/2 (Ortmann et al., 1997), which is expected under the predominate hypothesis that tapasin forms a complex with TAP1/2. Tapasin associates with the TAP1 protein of the ...

関連画像

Anti-TAPBP / Tapasin Antibody (aa307-356 putative model of the Peptide Loading  – eli kuinka tapasin Einsteininmhc class i docking with tapasin tapasin Tapasin is a type I transmembrane protein Tapasin

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