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1. A new class of membrane-bound chemokine with a CX3C motif

Author

T J Schall, Gary Hardiman, W Wang, Devora L. Rossi, Albert Zlotnik, J F Bazan, K Soo, Kevin B. Bacon, and David R. Greaves

Subjects
DNA, Complementary, Molecular Sequence Data, C-C chemokine receptor type 6, Biology, Hybrid Cells, Cell Line, Chemokine receptor, CXCL10, Humans, Tissue Distribution, Amino Acid Sequence, RNA, Messenger, Cloning, Molecular, CCL13, CXCL16, Multidisciplinary, Chemokine CX3CL1, Chromosome Mapping, Membrane Proteins, Chemokines, CX3C, Cell biology, CXCL2, Biochemistry, XCL2, Chemokines, CCL21, Protein Binding
Abstract

Chemokines direct the trafficking of white blood cells in immune surveillance, playing a key role in inflammatory and infectious diseases such as AIDS. All chemokines studied so far are secreted proteins of relative molecular mass approximately 7K-15K and fall into three families that are defined by a cysteine signature motif: CXC, CC and C (refs 3, 6, 7), where C is a cysteine and X any amino-acid residue. We report here the identification and characterization of a fourth human chemokine type, derived from non-haemopoietic cells and bearing a new CX3C fingerprint. Unlike other chemokine types, the polypeptide chain of the human CX3C chemokine is predicted to be part of a 373-amino-acid protein that carries the chemokine domain on top of an extended mucin-like stalk. This molecule can exist in two forms: either membrane-anchored or as a shed 95K glycoprotein. The soluble CX3C chemokine has potent chemoattractant activity for T cells and monocytes, and the cell-surface-bound protein, which is induced on activated primary endothelial cells, promotes strong adhesion of those leukocytes. The structure, biochemical features, tissue distribution and chromosomal localization of CX3C chemokine all indicate that it represents a unique class of chemokine that may constitute part of the molecular control of leukocyte traffic at the endothelium.

Published
2016

2. EXPERIMENTAL THERAPEUTICS AND PHARMACOLOGY

Author

C. Aaberg-Jessen, L. Fogh, B. Halle, V. Jensen, N. Brunner, B. W. Kristensen, T. Abe, Y. Momii, J. Watanabe, I. Morisaki, A. Natsume, T. Wakabayashi, M. Fujiki, B. Aldaz, A. W. M. Fabius, J. Silber, G. Harinath, T. A. Chan, J. T. Huse, S. Anai, T. Hide, H. Nakamura, K. Makino, S. Yano, J.-i. Kuratsu, I. V. Balyasnikova, M. S. Prasol, D. K. Kanoija, K. S. Aboody, M. S. Lesniak, T. Barone, C. Burkhart, A. Purmal, A. Gudkov, K. Gurova, R. Plunkett, K. Barton, K. Misuraca, F. Cordero, E. Dobrikova, H. Min, M. Gromeier, D. Kirsch, O. Becher, L. B. Pont, J. Kloezeman, M. van den Bent, R. Kanaar, A. Kremer, S. Swagemakers, P. French, C. Dirven, M. Lamfers, S. Leenstra, R. Balvers, A. Kleijn, S. Lawler, X. Gong, A. Andres, J. Hanson, J. Delashaw, D. Bota, C.-C. Chen, N.-W. Yao, W.-J. Chuang, C. Chang, P.-Y. Chen, C.-Y. Huang, K.-C. Wei, Y. Cheng, Q. Dai, R. Morshed, Y. Han, B. Auffinger, D. Wainwright, L. Zhang, A. Tobias, E. Rincon, B. Thaci, A. Ahmed, C. He, M. Lesniak, Y. A. Choi, H. Pandya, D. M. Gibo, I. Fokt, W. Priebe, W. Debinski, Y. Chornenkyy, S. Agnihotri, P. Buczkowicz, P. Rakopoulos, A. Morrison, M. Barszczyk, C. Hawkins, S. Chung, S. Decollogne, P. Luk, H. Shen, W. Ha, B. Day, B. Stringer, P. Hogg, P. Dilda, K. McDonald, S. Moore, M. Hayden-Gephart, J. Bergen, Y. Su, H. Rayburn, M. Edwards, M. Scott, J. Cochran, A. Das, A. K. Varma, G. C. Wallace, Y. N. Dixon-Mah, W. A. Vandergrift, P. Giglio, S. K. Ray, S. J. Patel, N. L. Banik, T. Dasgupta, A. Olow, X. Yang, S. Mueller, M. Prados, C. D. James, D. Haas-Kogan, N. D. Dave, P. B. Desai, G. A. Gudelsky, L. M. L. Chow, K. LaSance, X. Qi, J. Driscoll, K. Ebsworth, M. J. Walters, L. S. Ertl, Y. Wang, R. D. Berahovic, J. McMahon, J. P. Powers, J. C. Jaen, T. J. Schall, Z. Eroglu, J. Portnow, A. Sacramento, E. Garcia, A. Raubitschek, T. Synold, S. Esaki, S. Rabkin, R. Martuza, H. Wakimoto, S. Ferluga, C. L. Tome, H. E. Forde, I. A. Netland, L. Sleire, B. Skeie, P. O. Enger, D. Goplen, M. Giladi, A. Tichon, R. Schneiderman, Y. Porat, M. Munster, M. Dishon, U. Weinberg, E. Kirson, Y. Wasserman, Y. Palti, D. Gramatzki, M. Staudinger, K. Frei, M. Peipp, M. Weller, C. Grasso, L. Liu, N. Berlow, L. Davis, M. Fouladi, A. Gajjar, E. Huang, E. Hulleman, M. Hutt, C. Keller, X.-N. Li, P. Meltzer, M. Quezado, M. Quist, E. Raabe, P. Spellman, N. Truffaux, D. van Vurden, N. Wang, K. Warren, R. Pal, J. Grill, M. Monje, A. L. Green, S. Ramkissoon, D. McCauley, K. Jones, J. A. Perry, L. Ramkissoon, C. Maire, S. Shacham, K. L. Ligon, A. L. Kung, K. Zielinska-Chomej, V. Grozman, J. Tu, K. Viktorsson, R. Lewensohn, S. Gupta, A. Mladek, K. Bakken, B. Carlson, F. Boakye-Agyeman, S. Kizilbash, M. Schroeder, J. Reid, J. Sarkaria, P. Hadaczek, T. Ozawa, L. Soroceanu, Y. Yoshida, L. Matlaf, E. Singer, E. Fiallos, C. S. Cobbs, R. Hashizume, M. Tom, Y. Ihara, R. Santos, J. D. L. Torre, E. Lepe, T. Waldman, D. James, X. Huang, L. Yu-Jen, N. Gupta, D. Solomon, Z. Zhang, T. Hayashi, K. Adachi, S. Nagahisa, M. Hasegawa, Y. Hirose, M. H. Gephart, Y. S. Su, S. Hingtgen, R. Kasmieh, I. Nesterenko, J.-L. Figueiredo, R. Dash, D. Sarkar, P. Fisher, K. Shah, E. Horne, P. Diaz, N. Stella, C. Huang, H. Yang, K. Wei, T. Huang, J. Hlavaty, D. Ostertag, F. L. Espinoza, B. Martin, H. Petznek, M. Rodriguez-Aguirre, C. Ibanez, N. Kasahara, W. Gunzburg, H. Gruber, D. Pertschuk, D. Jolly, J. Robbins, B. Hurwitz, J. Y. Yoo, C. Bolyard, J.-G. Yu, J. Wojton, J. Zhang, Z. Bailey, D. Eaves, T. Cripe, M. Old, B. Kaur, L. Serwer, N. Le Moan, S. Ng, N. Butowski, A. Krtolica, S. P. L. Cary, T. Johns, S. Greenall, J. Donoghue, T. Adams, G. Karpel-Massler, M.-A. Westhoff, R. E. Kast, A. Dwucet, C. R. Wirtz, K.-M. Debatin, M.-E. Halatsch, N. Merkur, F. Kievit, Z. Stephen, K. Wang, D. Kolstoe, R. Ellenbogen, M. Zhang, G. Kitange, E. Haefner, K. Knubel, B. M. Pernu, A. Sufit, A. M. Pierce, S. K. Nelson, A. K. Keating, S. S. Jensen, J. Lachowicz, M. Demeule, A. Regina, S. Tripathy, J.-C. Curry, T. Nguyen, J.-P. Castaigne, T. Davis, A. Davis, K. Tanaka, T. Keating, J. Getz, G. T. Kapp, J. M. Romero, S. Lee, S. Ramisetti, B. Slagle-Webb, A. Sharma, J. Connor, W.-S. Lee, M. Kluk, J. C. Aster, K. Ligon, S. Sun, D. Lee, A. S. W. Ho, J. K. S. Pu, Z.-q. Zhang, N. P. Lee, P. J. R. Day, G. K. K. Leung, Z. Liu, X. Liu, A. B. Madhankumar, P. Miller, B. Webb, J. R. Connor, Q. X. Yang, M. Lobo, S. Green, M. Schabel, Y. Gillespie, R. Woltjer, M. Pike, Y.-J. Lu, H. A. Luchman, O. Stechishin, S. Nguyen, J. G. Cairncross, S. Weiss, X. Lun, J. C. Wells, X. Hao, N. Grinshtein, D. Kaplan, A. Luchman, D. Senger, S. Robbins, A. Madhankumar, E. Rizk, R. Payne, A. Park, M. Pang, K. Harbaugh, A. Wilisch-Neumann, D. Pachow, E. Kirches, C. Mawrin, S. McDonell, J. Liang, Y. Piao, N. Nguyen, A. Yung, R. Verhaak, E. Sulman, C. Stephan, F. Lang, J. de Groot, Y. Mizobuchi, T. Okazaki, T. Kageji, K. Kuwayama, K. T. Kitazato, H. Mure, K. Hara, R. Morigaki, K. Matsuzaki, K. Nakajima, S. Nagahiro, S. Kumala, M. Heravi, S. Devic, T. Muanza, K. H. Knubel, A. Neuwelt, Y. J. Wu, A. Donson, R. Vibhakar, S. Venkatamaran, V. Amani, E. Neuwelt, L. Rapkin, N. Foreman, F. Ibrahim, P. New, K. Cui, H. Zhao, D. Chow, W. Stephen, K. Nozue-Okada, M. Nagane, K. L. McDonald, D. Ogawa, E. Chiocca, J. Godlewski, A. Patel, N. Pasupuleti, F. Gorin, A. Valenzuela, L. Leon, K. Carraway, C. Ramachandran, S. Nair, K.-W. Quirrin, Z. Khatib, E. Escalon, S. Melnick, A. Phillips, E. Boghaert, K. Vaidya, P. Ansell, D. Shalinsky, Y. Zhang, M. Voorbach, S. Mudd, K. Holen, R. Humerickhouse, E. Reilly, S. Parab, O. Diago, T. Ryken, S. Agarwal, M. Al-Keilani, M. Alqudah, Z. Sibenaller, M. Assemolt, K. Sai, W.-y. Li, W.-p. Li, Z.-p. Chen, R. Saito, Y. Sonoda, M. Kanamori, Y. Yamashita, T. Kumabe, T. Tominaga, G. Sarkar, G. Curran, R. Jenkins, R. Scharnweber, Y. Kato, J. Lin, R. Everson, H. Soto, C. Kruse, L. Liau, R. Prins, S. Semenkow, Q. Chu, C. Eberhart, R. Sengupta, J. Marassa, D. Piwnica-Worms, J. Rubin, R. Shai, T. Pismenyuk, I. Moshe, T. Fisher, S. Freedman, A. Simon, N. Amariglio, G. Rechavi, A. Toren, M. Yalon, Y. Shimazu, K. Kurozumi, T. Ichikawa, K. Fujii, M. Onishi, J. Ishida, T. Oka, M. Watanabe, Y. Nasu, H. Kumon, I. Date, R. W. Sirianni, R. L. McCall, J. Spoor, M. van der Kaaij, M. Geurtjens, O. Veiseh, C. Fang, M. Leung, G. Strohbehn, K.-K. Atsina, T. Patel, J. Piepmeier, J. Zhou, W. M. Saltzman, M. Takahashi, G. Valdes, A. Inagaki, S. Kamijima, K. Hiraoka, E. Micewicz, W. H. McBride, K. S. Iwamoto, H. E. Gruber, J. M. Robbins, D. J. Jolly, C. McCully, J. Bacher, T. Thomas, R. Murphy, E. Steffen-Smith, R. McAllister, D. Pastakia, B. Widemann, P. Chen, M. Hua, H. Liu, E. C. Woolf, M. G. Abdelwahab, K. E. Fenton, Q. Liu, G. Turner, M. C. Preul, A. C. Scheck, W. Shen, D. Brown, H. Pedersen, S. Hariono, T.-W. Yao, A. Sidhu, W. A. Weiss, T. P. Nicolaides, and T. Olusanya

Subjects
Cancer Research, Abstracts, Oncology, business.industry, Medicine, Neurology (clinical), Pharmacology, business
Published
2013

3. RANTES induces tyrosine kinase activity of stably complexed p125FAK and ZAP-70 in human T cells

Author

Hans Yssel, J B Bolen, T J Schall, M C Szabo, and K B Bacon

Subjects
T cell, T-Lymphocytes, Immunology, PTK2, Receptors, Antigen, T-Cell, Focal adhesion, chemistry.chemical_compound, medicine, Cell Adhesion, Immunology and Allergy, Humans, Phosphorylation, Chemokine CCL5, Paxillin, ZAP-70 Protein-Tyrosine Kinase, biology, Tyrosine phosphorylation, Articles, Protein-Tyrosine Kinases, Phosphoproteins, Molecular biology, Receptor, Insulin, Enzyme Activation, Cytoskeletal Proteins, medicine.anatomical_structure, chemistry, Focal Adhesion Kinase 1, Focal Adhesion Protein-Tyrosine Kinases, biology.protein, Signal transduction, Tyrosine kinase, Cell Adhesion Molecules
Abstract

The chemokine RANTES is a chemoattractant and activating factor for T lymphocytes. Investigation of the signal transduction mechanisms induced by RANTES in T cells revealed tyrosine phosphorylation of multiple protein species with prominent bands at 70-85 and 120-130 kD. Immunoprecipitation and Western analyses revealed that a protein of 125 kD was identical to the focal adhesion kinase (FAK) pp125FAK. RANTES stimulated phosphorylation of FAK as early as 30 seconds and immunoblots using antiphosphotyrosine monoclonal antibodies revealed that there was consistent phosphorylation of a 68-70 kD species in the pp125FAK immunoprecipitates. Immunoblotting and kinase assays showed this to be two separate proteins, the tyrosine kinase zeta-associated protein (ZAP) 70, and the focal adhesion protein paxillin. These results indicate a potentially important role for RANTES in the generation of T cell focal adhesions and subsequent cell activation via a molecular complex containing FAK, ZAP-70, and paxillin.

Published
1996

4. Engagement of major histocompatibility complex class II molecules by superantigen induces inflammatory cytokine gene expression in human rheumatoid fibroblast-like synoviocytes

Author

T. J. Schall, Shaun R. McColl, Walid Mourad, and Khalil Mehindate

Subjects
Staphylococcus aureus, Interferon Inducers, medicine.medical_treatment, Immunology, Gene Expression, Enzyme-Linked Immunosorbent Assay, Major histocompatibility complex, Arthritis, Rheumatoid, Enterotoxins, Synovial Fluid, Superantigen, medicine, Immunology and Allergy, Humans, Interferon gamma, Northern blot, RNA, Messenger, Interleukin 6, MHC class II, Interferon inducer, biology, Articles, HLA-DR Antigens, Fibroblasts, Blotting, Northern, Molecular biology, Cytokine, biology.protein, Cytokines, medicine.drug
Abstract

Cells in the rheumatoid synovium express high levels of major histocompatibility complex (MHC) class II molecules in vivo. We have therefore examined the ability of engagement of MHC class II molecules by the superantigen Staphylococcal enterotoxin A (SEA) to activate interleukin 6 (IL-6) and IL-8 gene expression in type B synoviocytes isolated from patients with rheumatoid arthritis. SEA had a minimal or undetectable effect on the expression of either gene in resting synoviocytes, as determined by Northern blot and specific enzyme-linked immunosorbent assay. However, induction of MHC class II molecule expression after treatment of synoviocytes with interferon gamma (IFN-gamma) enabled the cells to respond to SEA in a dose-dependent manner, resulting in an increase in both the level of steady-state mRNA for IL-6 and IL-8, and the release of these cytokines into the supernatant. IFN-gamma by itself had no effect on the expression of either cytokine. Pretreatment of the cells with the transcription inhibitor actinomycin D prevented the increase in cytokine mRNA induced by SEA, whereas cycloheximide superinduced mRNA for both cytokines after stimulation by SEA. Taken together, these results indicate that signaling through MHC class II molecules may represent a novel mechanism by which inflammatory cytokine production is regulated in type B rheumatoid synoviocytes, and potentially provides insight into the manner by which superantigens may initiate and/or propagate autoimmune diseases.

Published
1992

5. Characterization of the Rhesus Cytomegalovirus US28 Locus

Author

D. J. Dairaghi, Peter A. Barry, T. L. Schmidt, Mark E. T. Penfold, and T. J. Schall

Subjects
Human cytomegalovirus, Chemokine, Viral pathogenesis, Immunology, Molecular Sequence Data, Biology, Microbiology, Immediate early protein, Immediate-Early Proteins, Open Reading Frames, Viral Proteins, Viral entry, Virology, medicine, Animals, Humans, Amino Acid Sequence, ORFS, Tropism, Glycoproteins, Chromosome Mapping, Membrane Proteins, medicine.disease, Macaca mulatta, Open reading frame, Insect Science, biology.protein, Pathogenesis and Immunity, Calcium, Receptors, Chemokine
Abstract

Human cytomegalovirus (CMV) US28 (and the related open reading frame [ORF] US27) are G-protein-coupled receptor homologs believed to play a role in viral pathogenesis. In vitro, US28 has been shown to bind and internalize ligands, as well as activate intracellular signaling in response to certain chemokines, and to initiate the migration of smooth muscle cells to chemokine gradients. To assess the role of US28 in vivo, we examined the rhesus model and sequenced and characterized the rhesus CMV US28 locus. We found that rhesus CMV carries five tandem homologs of US28, all widely divergent from US28 and from each other. By reverse transcription-PCR and Northern analysis, we demonstrated expression of these ORFs in infected cells. With stable cell lines expressing these ORFs, we analyzed the homolog's binding and signaling characteristics across a wide range of chemokines and found one (RhUS28.5) to have a ligand binding profile similar to that of US28. In addition, we localized US28 and the rhesus CMV homolog RhUS28.5 to the envelope of infectious virions, suggesting a role in viral entry or cell tropism.

Published
2003

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