Cytohesin-1 Controls the Activation of Rhoa and Modulates Integrin-Dependent Adhesion and Migration of Dendritic Cells
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Inhibition of Midkine Alleviates Experimental Autoimmune Encephalomyelitis Through the Expansion of Regulatory T Cell Population
Inhibition of midkine alleviates experimental autoimmune encephalomyelitis through the expansion of regulatory T cell population Jinyan Wang*, Hideyuki Takeuchi*†, Yoshifumi Sonobe*, Shijie Jin*, Tetsuya Mizuno*, Shin Miyakawa‡, Masatoshi Fujiwara‡, Yoshikazu Nakamura§¶, Takuma Katoʈ, Hisako Muramatsu**, Takashi Muramatsu**††, and Akio Suzumura*† *Department of Neuroimmunology, Research Institute of Environmental Medicine, Nagoya University, Furo-cho, Chikusa-ku, Nagoya 464-8601, Japan; ‡RIBOMIC, Inc., 3-15-5-601 Shirokanedai, Minato-ku, Tokyo 108-0071, Japan; §Department of Basic Medical Sciences, Institute of Medical Science, University of Tokyo, Shirokanedai, Minato-ku, Tokyo 108-8639, Japan; ¶Core Research Evolutional Science and Technology, Japan Science and Technology Agency, Toyonaka, Osaka 560-8531, Japan; ʈDepartment of Bioregulation, Mie University Graduate School of Medicine, Tsu, Mie 514-8507, Japan; **Department of Biochemistry, Nagoya University Graduate School of Medicine, Tsurumai-cho, Showa-ku, Nagoya 466-8550, Japan; and ††Department of Health Science, Faculty of Psychological and Physical Sciences, Aichi Gakuin University, Nisshin, Aichi 470-0195, Japan Edited by Ethan Shevach, National Institutes of Health, Bethesda, MD, and accepted by the Editorial Board January 20, 2008 (received for review October 12, 2007) CD4؉CD25؉ regulatory T (Treg) cells are crucial mediators of nity, and abnormalities in Treg cell function may contribute to the autoimmune tolerance. The factors that regulate Treg cells, how- development of -
Immunomodulation and Generation of Tolerogenic Dendritic Cells by Probiotic Bacteria in Patients with Inflammatory Bowel Disease
International Journal of Molecular Sciences Article Immunomodulation and Generation of Tolerogenic Dendritic Cells by Probiotic Bacteria in Patients with Inflammatory Bowel Disease 1, 2, 1 Shaghayegh Baradaran Ghavami y, Abbas Yadegar y , Hamid Asadzadeh Aghdaei , Dario Sorrentino 3,4,*, Maryam Farmani 1 , Adil Shamim Mir 5, Masoumeh Azimirad 2 , Hedieh Balaii 6, Shabnam Shahrokh 6 and Mohammad Reza Zali 6 1 Basic and Molecular Epidemiology of Gastrointestinal Disorders Research Center, Research Institute for Gastroenterology and Liver Diseases, Shahid Beheshti University of Medical Sciences, Tehran 1985717413, Iran; [email protected] (S.B.G.); [email protected] (H.A.A.); [email protected] (M.F.) 2 Foodborne and Waterborne Diseases Research Center, Research Institute for Gastroenterology and Liver Diseases, Shahid Beheshti University of Medical Sciences, Tehran 1985717413, Iran; [email protected] (A.Y.); [email protected] (M.A.) 3 IBD Center, Division of Gastroenterology, Virginia Tech Carilion School of Medicine, Roanoke, VA 24016, USA 4 Department of Clinical and Experimental Medical Sciences, University of Udine School of Medicine, 33100 Udine, Italy 5 Department of Internal Medicine, Roanoke Memorial Hospital, Carilion Clinic, VA 24014, USA; [email protected] 6 Gastroenterology and Liver Diseases Research Center, Research Institute for Gastroenterology and Liver Diseases, Shahid Beheshti University of Medical Sciences, Tehran 1985717413, Iran; [email protected] (H.B.); [email protected] (S.S.); [email protected] (M.R.Z.) * Correspondence: [email protected] These authors equally contributed to this study. y Received: 7 August 2020; Accepted: 27 August 2020; Published: 29 August 2020 Abstract: In inflammatory bowel diseases (IBD), the therapeutic benefit and mucosal healing from specific probiotics may relate to the modulation of dendritic cells (DCs). -
Galectin-4 Interaction with CD14 Triggers the Differentiation of Monocytes Into Macrophage-Like Cells Via the MAPK Signaling Pathway
Immune Netw. 2019 Jun;19(3):e17 https://doi.org/10.4110/in.2019.19.e17 pISSN 1598-2629·eISSN 2092-6685 Original Article Galectin-4 Interaction with CD14 Triggers the Differentiation of Monocytes into Macrophage-like Cells via the MAPK Signaling Pathway So-Hee Hong 1,2,3,4,5, Jun-Seop Shin 1,2,3,5, Hyunwoo Chung 1,2,4,5, Chung-Gyu Park 1,2,3,4,5,* 1Xenotransplantation Research Center, Seoul National University College of Medicine, Seoul 03080, Korea 2Institute of Endemic Diseases, Seoul National University College of Medicine, Seoul 03080, Korea 3Cancer Research Institute, Seoul National University College of Medicine, Seoul 03080, Korea 4Department of Biomedical Sciences, Seoul National University College of Medicine, Seoul 03080, Korea 5Department of Microbiology and Immunology, Seoul National University College of Medicine, Seoul 03080, Korea Received: Jan 28, 2019 ABSTRACT Revised: May 13, 2019 Accepted: May 19, 2019 Galectin-4 (Gal-4) is a β-galactoside-binding protein mostly expressed in the gastrointestinal *Correspondence to tract of animals. Although intensive functional studies have been done for other galectin Chung-Gyu Park isoforms, the immunoregulatory function of Gal-4 still remains ambiguous. Here, we Department of Microbiology and Immunology, Seoul National University College of Medicine, demonstrated that Gal-4 could bind to CD14 on monocytes and induce their differentiation 103 Daehak-ro, Jongno-gu, Seoul 03080, into macrophage-like cells through the MAPK signaling pathway. Gal-4 induced the phenotypic Korea. changes on monocytes by altering the expression of various surface molecules, and induced E-mail: [email protected] functional changes such as increased cytokine production and matrix metalloproteinase expression and reduced phagocytic capacity. -
Supplementary Table 1: Adhesion Genes Data Set
Supplementary Table 1: Adhesion genes data set PROBE Entrez Gene ID Celera Gene ID Gene_Symbol Gene_Name 160832 1 hCG201364.3 A1BG alpha-1-B glycoprotein 223658 1 hCG201364.3 A1BG alpha-1-B glycoprotein 212988 102 hCG40040.3 ADAM10 ADAM metallopeptidase domain 10 133411 4185 hCG28232.2 ADAM11 ADAM metallopeptidase domain 11 110695 8038 hCG40937.4 ADAM12 ADAM metallopeptidase domain 12 (meltrin alpha) 195222 8038 hCG40937.4 ADAM12 ADAM metallopeptidase domain 12 (meltrin alpha) 165344 8751 hCG20021.3 ADAM15 ADAM metallopeptidase domain 15 (metargidin) 189065 6868 null ADAM17 ADAM metallopeptidase domain 17 (tumor necrosis factor, alpha, converting enzyme) 108119 8728 hCG15398.4 ADAM19 ADAM metallopeptidase domain 19 (meltrin beta) 117763 8748 hCG20675.3 ADAM20 ADAM metallopeptidase domain 20 126448 8747 hCG1785634.2 ADAM21 ADAM metallopeptidase domain 21 208981 8747 hCG1785634.2|hCG2042897 ADAM21 ADAM metallopeptidase domain 21 180903 53616 hCG17212.4 ADAM22 ADAM metallopeptidase domain 22 177272 8745 hCG1811623.1 ADAM23 ADAM metallopeptidase domain 23 102384 10863 hCG1818505.1 ADAM28 ADAM metallopeptidase domain 28 119968 11086 hCG1786734.2 ADAM29 ADAM metallopeptidase domain 29 205542 11085 hCG1997196.1 ADAM30 ADAM metallopeptidase domain 30 148417 80332 hCG39255.4 ADAM33 ADAM metallopeptidase domain 33 140492 8756 hCG1789002.2 ADAM7 ADAM metallopeptidase domain 7 122603 101 hCG1816947.1 ADAM8 ADAM metallopeptidase domain 8 183965 8754 hCG1996391 ADAM9 ADAM metallopeptidase domain 9 (meltrin gamma) 129974 27299 hCG15447.3 ADAMDEC1 ADAM-like, -
B Cell Checkpoints in Autoimmune Rheumatic Diseases
REVIEWS B cell checkpoints in autoimmune rheumatic diseases Samuel J. S. Rubin1,2,3, Michelle S. Bloom1,2,3 and William H. Robinson1,2,3* Abstract | B cells have important functions in the pathogenesis of autoimmune diseases, including autoimmune rheumatic diseases. In addition to producing autoantibodies, B cells contribute to autoimmunity by serving as professional antigen- presenting cells (APCs), producing cytokines, and through additional mechanisms. B cell activation and effector functions are regulated by immune checkpoints, including both activating and inhibitory checkpoint receptors that contribute to the regulation of B cell tolerance, activation, antigen presentation, T cell help, class switching, antibody production and cytokine production. The various activating checkpoint receptors include B cell activating receptors that engage with cognate receptors on T cells or other cells, as well as Toll-like receptors that can provide dual stimulation to B cells via co- engagement with the B cell receptor. Furthermore, various inhibitory checkpoint receptors, including B cell inhibitory receptors, have important functions in regulating B cell development, activation and effector functions. Therapeutically targeting B cell checkpoints represents a promising strategy for the treatment of a variety of autoimmune rheumatic diseases. Antibody- dependent B cells are multifunctional lymphocytes that contribute that serve as precursors to and thereby give rise to acti- cell- mediated cytotoxicity to the pathogenesis of autoimmune diseases -
The Immunological Synapse and CD28-CD80 Interactions Shannon K
© 2001 Nature Publishing Group http://immunol.nature.com ARTICLES The immunological synapse and CD28-CD80 interactions Shannon K. Bromley1,Andrea Iaboni2, Simon J. Davis2,Adrian Whitty3, Jonathan M. Green4, Andrey S. Shaw1,ArthurWeiss5 and Michael L. Dustin5,6 Published online: 19 November 2001, DOI: 10.1038/ni737 According to the two-signal model of T cell activation, costimulatory molecules augment T cell receptor (TCR) signaling, whereas adhesion molecules enhance TCR–MHC-peptide recognition.The structure and binding properties of CD28 imply that it may perform both functions, blurring the distinction between adhesion and costimulatory molecules. Our results show that CD28 on naïve T cells does not support adhesion and has little or no capacity for directly enhancing TCR–MHC- peptide interactions. Instead of being dependent on costimulatory signaling, we propose that a key function of the immunological synapse is to generate a cellular microenvironment that favors the interactions of potent secondary signaling molecules, such as CD28. The T cell receptor (TCR) interaction with complexes of peptide and as CD2 and CD48, which suggests that CD28 might have a dual role as major histocompatibility complex (pMHC) is central to the T cell an adhesion and a signaling molecule4. Coengagement of CD28 with response. However, efficient T cell activation also requires the partici- the TCR has a number of effects on T cell activation; these include pation of additional cell-surface receptors that engage nonpolymorphic increasing sensitivity to TCR stimulation and increasing the survival of ligands on antigen-presenting cells (APCs). Some of these molecules T cells after stimulation5. CD80-transfected APCs have been used to are involved in the “physical embrace” between T cells and APCs and assess the temporal relationship of TCR and CD28 signaling, as initiat- are characterized as adhesion molecules. -
Anti-CD18 / LFA1 Beta Antibody (ARG41484)
Product datasheet [email protected] ARG41484 Package: 100 μl anti-CD18 / LFA1 beta antibody Store at: -20°C Summary Product Description Rabbit Polyclonal antibody recognizes CD18 / LFA1 beta Tested Reactivity Hu, Ms, Rat Tested Application ICC/IF, IHC-P, WB Host Rabbit Clonality Polyclonal Isotype IgG Target Name CD18 / LFA1 beta Antigen Species Human Immunogen Recombinant protein of Human CD18 / LFA1 beta. Conjugation Un-conjugated Alternate Names MF17; LAD; CD antigen CD18; MFI7; MAC-1; Cell surface adhesion glycoproteins LFA-1/CR3/p150,95 subunit beta; LCAMB; Integrin beta-2; Complement receptor C3 subunit beta; LFA-1; CD18 Application Instructions Application table Application Dilution ICC/IF 1:50 - 1:200 IHC-P 1:50 - 1:200 WB 1:500 - 1:2000 Application Note * The dilutions indicate recommended starting dilutions and the optimal dilutions or concentrations should be determined by the scientist. Positive Control Mouse thymus Calculated Mw 85 kDa Observed Size ~ 98 kDa Properties Form Liquid Purification Affinity purified. Buffer PBS (pH 7.3), 0.02% Sodium azide and 50% Glycerol. Preservative 0.02% Sodium azide Stabilizer 50% Glycerol Storage instruction For continuous use, store undiluted antibody at 2-8°C for up to a week. For long-term storage, aliquot and store at -20°C. Storage in frost free freezers is not recommended. Avoid repeated freeze/thaw www.arigobio.com 1/3 cycles. Suggest spin the vial prior to opening. The antibody solution should be gently mixed before use. Note For laboratory research only, not for drug, diagnostic or other use. Bioinformation Gene Symbol ITGB2 Gene Full Name integrin, beta 2 (complement component 3 receptor 3 and 4 subunit) Background This gene encodes an integrin beta chain, which combines with multiple different alpha chains to form different integrin heterodimers. -
Induces Antigen Presentation in B Cells Cell-Activating Factor of The
B Cell Maturation Antigen, the Receptor for a Proliferation-Inducing Ligand and B Cell-Activating Factor of the TNF Family, Induces Antigen Presentation in B Cells This information is current as of September 27, 2021. Min Yang, Hidenori Hase, Diana Legarda-Addison, Leena Varughese, Brian Seed and Adrian T. Ting J Immunol 2005; 175:2814-2824; ; doi: 10.4049/jimmunol.175.5.2814 http://www.jimmunol.org/content/175/5/2814 Downloaded from References This article cites 54 articles, 36 of which you can access for free at: http://www.jimmunol.org/content/175/5/2814.full#ref-list-1 http://www.jimmunol.org/ Why The JI? Submit online. • Rapid Reviews! 30 days* from submission to initial decision • No Triage! Every submission reviewed by practicing scientists • Fast Publication! 4 weeks from acceptance to publication by guest on September 27, 2021 *average Subscription Information about subscribing to The Journal of Immunology is online at: http://jimmunol.org/subscription Permissions Submit copyright permission requests at: http://www.aai.org/About/Publications/JI/copyright.html Email Alerts Receive free email-alerts when new articles cite this article. Sign up at: http://jimmunol.org/alerts The Journal of Immunology is published twice each month by The American Association of Immunologists, Inc., 1451 Rockville Pike, Suite 650, Rockville, MD 20852 Copyright © 2005 by The American Association of Immunologists All rights reserved. Print ISSN: 0022-1767 Online ISSN: 1550-6606. The Journal of Immunology B Cell Maturation Antigen, the Receptor for a Proliferation-Inducing Ligand and B Cell-Activating Factor of the TNF Family, Induces Antigen Presentation in B Cells1 Min Yang,* Hidenori Hase,* Diana Legarda-Addison,* Leena Varughese,* Brian Seed,† and Adrian T. -
Atpase, Na+/K+ Transporting, Alpha 3 Polypeptide Homologous to 3'UTR
HUGO ID Name Nalm-6 TOM-1 Reh Karpas-422 DoHH -2 SU-DHL-5 Namalwa DG-75 Ramos Raji BEL EHEB BONNA-12 L-428 DEL BCP-1 BC-3 BCBL-1 JSC-1 PEL-SY HBL-6 DS-1 RPMI-8226 NCI-H929 L-363 SK-MM-2 ATP1A3 ATPase, Na+/K+ transporting, alpha 3 polypeptide CD24 homologous to 3'UTR of human CD24 gene ABCC5 multidrug resistance-associated protein (MRP5) CD72 CD72 antigen TCL1A Tcell leukemia/lymphoma 1 ITGB2 Integrin, beta 2 (antigen CD18 (p95)) ? nuclear ribonucleoprotein particle (hnRNP) SGT1 suppressor of G2 allele of skp1 homolog DNMT 1 DNA (cytosine-5-)-methyltransferase 1 GALE UDP-Galactose 4 epimerase (GALE) HADHSC L-3-hydroxyacyl-CoA dehydrogenase LIG4 DNA ligase IV LIG1 Ligase I, DNA, ATP-dependent CEBPG CCAA T/enhancer binding protein (C/EBP), gamma DCK Deoxycytidine kinase TCEA1 TRANSCRIPTION ELONGATION FACTOR S-II TCN 1 TRANSCOBALAMIN I PRECURSOR POLA2 DNA polymerase alpha subunit CCNG2 cyclin G2 RNPC1 Finkel-Biskis-Reilly murine sarcoma virus; Human seb4D RNPC1 Finkel-Biskis-Reilly murine sarcoma virus; Human seb4D DGKD Diacylglycerol kinase delta KIAA0220 Polycystic kidney disease protein 1 KIAA0220 calcium-dependent group X phospholipase A2 KIAA0220 calcium-dependent group X phospholipase A2 ALDH5A1 NAD+-dependent succinate-semialdehyde dehydrogenase CCNG2 Polycystic kidney disease 1 (autosomal dominant) PDCD4 nuclear antigen H731-like protein SSH3BP1 eps8 binding protein e3B1 MAP4K2 B lymphocyte serine/threonine protein kinase (GC kinase) MAPRE2 novel T-cell activation protein ZNFN1A Ikaros/LyF-1 homolog (hIk-1) FLJ22624 clone 23799 KIAA0355 -
Rabbit Anti-Phospho-CD18-SL10462R-FITC
SunLong Biotech Co.,LTD Tel: 0086-571- 56623320 Fax:0086-571- 56623318 E-mail:[email protected] www.sunlongbiotech.com Rabbit Anti-Phospho-CD18 SL10462R-FITC Product Name: Anti-Phospho-CD18 (Thr758)/FITC Chinese Name: FITC标记的磷酸化整合素β2/Integrin β2抗体 CD18 (Phospho Thr758); CD18 (Phospho-Thr758); CD18 (Phospho T758); p-CD18 (T758); p-CD18 (Thr758); Integrin beta 2; 95 subunit beta; CD 18; CD18; Cell surface adhesion glycoprotein LFA 1/CR3/P150,959 beta subunit precursor); Cell surface adhesion glycoproteins LFA 1/CR3/p150,95 subunit beta; Cell surface adhesion glycoproteins LFA-1/CR3/p150; Complement receptor C3 beta subunit; Complement Alias: receptor C3 subunit beta; Integrin beta chain beta 2; Integrin beta-2; Integrin, beta 2 (complement component 3 receptor 3 and 4 subunit); ITB2_HUMAN; ITGB2; LAD; LCAMB; Leukocyte associated antigens CD18/11A, CD18/11B, CD18/11C; Leukocyte cell adhesion molecule CD18; LFA 1; LFA1; Lymphocyte function associated antigen 1; MAC 1; MAC1; MF17; MFI7; OTTHUMP00000115278; OTTHUMP00000115279; OTTHUMP00000115280; OTTHUMP00000115281; OTTHUMP00000115282. Organism Species: Rabbit Clonality: Polyclonal React Species: Human,Mouse,Rat,Chicken,Dog,Pig,Cow,Horse,Rabbit,Sheep,Guinea Pig, Flow-Cyt=1:50-200ICC=1:50-200IF=1:50-200www.sunlongbiotech.com Applications: not yet tested in other applications. optimal dilutions/concentrations should be determined by the end user. Molecular weight: 82kDa Form: Lyophilized or Liquid Concentration: 1mg/ml KLH conjugated synthesised phosphopeptide derived from human CD18 around the immunogen: phosphorylation site of Thr758 Lsotype: IgG Purification: affinity purified by Protein A Storage Buffer: 0.01M TBS(pH7.4) with 1% BSA, 0.03% Proclin300 and 50% Glycerol. Store at -20 °C for one year. -
Immuno-Oncology Panel 4 (Direct-MRM MS, Pending)
Immuno-Oncology panel 4 (direct-MRM MS, pending) (397 analytes pending validation) Gene Symbol Target protein name UniProt ID (& link) Modification* *blanks mean the assay detects the ABCE1 ATP-binding cassette sub-family E member 1 P61221 non-modified peptide sequence ABCE1 ATP-binding cassette sub-family E member 1 P61221 ABI1 Abl interactor 1 Q8IZP0 ABI1 Abl interactor 1 Q8IZP0 AKT1 RAC-alpha serine/threonine-protein kinase P31749 AKT1 RAC-alpha serine/threonine-protein kinase P31749 ANXA1 Annexin A1 P04083 ANXA4 annexin A4 P09525 ANXA5 Annexin A5 P08758 ANXA5 Annexin A5 P08758 ANXA6 annexin A6 P08133 B2M Beta-2-microglobulin P61769 B2M Beta-2-microglobulin P61769 BCAP31 B-cell receptor-associated protein 31 P51572 BCAP31 B-cell receptor-associated protein 31 P51572 BCL2 Apoptosis regulator Bcl-2 P10415 BCL2L1 Bcl-2-like protein 1 Q07817 BCL2L11 Bcl-2-like protein 11 O43521 BCL2L11 Bcl-2-like protein 11 O43521 BCL2L2 Bcl-2-like protein 2 Q92843 BCL2L2 Bcl-2-like protein 2 Q92843 BCL3 B-cell lymphoma 3 protein P20749 BCL3 B-cell lymphoma 3 protein P20749 BID BH3-interacting domain death agonist P55957 BID BH3-interacting domain death agonist P55957 BNIP3L BCL2/adenovirus E1B 19 kDa protein-interacting protein 3-like O60238 BNIP3L BCL2/adenovirus E1B 19 kDa protein-interacting protein 3-like O60238 BPGM Bisphosphoglycerate mutase P07738 BPGM Bisphosphoglycerate mutase P07738 BST2 Bone marrow stromal antigen 2 Q10589 BST2 Bone marrow stromal antigen 2 Q10589 C1QA Complement C1q subcomponent subunit A P02745 C1QA Complement C1q subcomponent -
Induce EBV-Transformed B Cell Apoptosis Through the Fas/Fasl Pathway
INTERNATIONAL JOURNAL OF ONCOLOGY 43: 1531-1540, 2013 CD80 (B7.1) and CD86 (B7.2) induce EBV-transformed B cell apoptosis through the Fas/FasL pathway GA BIN PARK1, YEONG SEOK KIM1, HYUN-KYUNG LEE2, DAE-HO CHO3, DAEJIN KIM1 and DAE YOUNG HUR1 1Department of Anatomy and Research Center for Tumor Immunology, Inje University College of Medicine; 2Department of Internal Medicine, Inje University Busan Paik Hospital, Busan 614-735; 3Department of Life Science, Sookmyung Women's University, Yongsan-gu, Yongsan-ku, Seoul 140-742, Republic of Korea Received July 7, 2013; Accepted August 16, 2013 DOI: 10.3892/ijo.2013.2091 Abstract. CD80 and CD86 expression is strongly regulated resting human B lymphocytes with EBV results in immor- in B cells and is induced by various stimuli (e.g., cytokines, talization of infected B cells, yielding lymphoblastoid cells, ligation of MHC class II and CD40 ligand). Epstein-Barr virus which are characterized by continuous growth and resistance (EBV) infection activates B lymphocytes and transforms them to various apoptotic signals. Moreover, lymphoblastoid cells into lymphoblastoid cells. However, the role of CD80 and CD86 have a phenotype related to that of activated B-lymphoblasts. in EBV infection of B cells remains unclear. Here, we observed However, despite clarification of the role of some viral proteins, that cross-linking of CD80 and CD86 in EBV-transformed such as latent membrane protein (LMP), in EBV-related resis- B cells induced apoptosis through caspase-dependent release tance, the molecular mechanisms of resistance to apoptosis are of apoptosis-related molecules, cytochrome c and apoptosis- not yet fully understood (2,3).