Osteopontin and allergic disease: pathophysiology and implications for diagnostics and therapy

References

• Pirquet CV. Allergie. Münch Med. Wochenschr.30, 1457–1458 (1906).
   Google Scholar
• Rajan TV. The Gell–Coombs classification of hypersensitivity reactions: a re-interpretation. Trends Immunol.24(7), 376–379 (2003).
   PubMed Web of Science ®Google Scholar
• Weck AD. A short history of allergological diseases and concepts. In: Allergy. Kay B (Ed). Blackwell, Oxford, UK, 3–22 (1997).
   Google Scholar
• Gell P, Coombs RRA. The classification of allergic reactions underlying disease. In: Clinical Aspects of Immunology. Coombs RRA, Gell PGH (Eds). Blackwell Science, Oxford, UK (1963).
   Google Scholar
• Descotes J, Choquet-Kastylevsky G. Gell and Coombs’s classification: is it still valid? Toxicology158(1–2), 43–49 (2001).
   PubMed Web of Science ®Google Scholar
• Akdis CA, Akdis M, Bieber T et al. Diagnosis and treatment of atopic dermatitis in children and adults: European Academy of Allergology and Clinical Immunology/American Academy of Allergy, Asthma and Immunology/PRACTALL Consensus Report. J. Allergy Clin. Immunol.118(1), 152–169 (2006).
   PubMed Web of Science ®Google Scholar
• Frew AJ. Advances in environmental and occupational diseases 2004. J. Allergy Clin. Immunol.115(6), 1197–1202 (2005).
   PubMed Web of Science ®Google Scholar
• Karlberg AT, Bergstrom MA, Borje A, Luthman K, Nilsson JL. Allergic contact dermatitis – formation, structural requirements, and reactivity of skin sensitizers. Chem. Res. Toxicol.21(1), 53–69 (2008).
   PubMed Web of Science ®Google Scholar
• Traidl-Hoffmann C, Jakob T, Behrendt H. Determinants of allergenicity. J. Allergy Clin. Immunol.123(3), 558–566 (2009).
   PubMed Web of Science ®Google Scholar
• Weidinger S, Gieger C, Rodriguez E et al. Genome-wide scan on total serum IgE levels identifies FCER1A as novel susceptibility locus. PLoS Genet.4(8), e1000166 (2008).
   Web of Science ®Google Scholar
• Cavani A, Girolomoni G. Immune Mechanisms in Allergic Contact Dermatitis. RG Landies Company, Georgetown, TX, USA (2005).
   Google Scholar
• Frosch PJ MT, Lepoittevin JP. Contact dermatitis (3rd Edition). Springer, Berlin, Germany (2007).
   Google Scholar
• Ale IS, Maibacht HA. Diagnostic approach in allergic and irritant contact dermatitis. Expert Rev. Clin. Immunol.6(2), 291–310 (2010).
   Web of Science ®Google Scholar
• Fisher LW, Fedarko NS. Six genes expressed in bones and teeth encode the current members of the SIBLING family of proteins. Connect. Tissue Res.44(Suppl. 1), 33–40 (2003).
   PubMed Web of Science ®Google Scholar
• Fisher LW, Torchia DA, Fohr B, Young MF, Fedarko NS. Flexible structures of SIBLING proteins, bone sialoprotein, and osteopontin. Biochem. Biophys. Res. Commun.280(2), 460–465 (2001).
   PubMed Web of Science ®Google Scholar
• Yamaguchi Y, Hanashima S, Yagi H et al. NMR characterization of intramolecular interaction of osteopontin, an intrinsically disordered protein with cryptic integrin-binding motifs. Biochem. Biophys. Res. Commun.393(3), 487–491 (2010).
   Google Scholar
• Buback F, Renkl AC, Schulz G, Weiss JM. Osteopontin and the skin: multiple emerging roles in cutaneous biology and pathology. Exp. Dermatol.18(9), 750–759 (2009).
   PubMedGoogle Scholar
• O’Regan A. The role of osteopontin in lung disease. Cytokine Growth Factor Rev.14(6), 479–488 (2003).
   PubMed Web of Science ®Google Scholar
• Sodek J, Batista Da Silva AP, Zohar R. Osteopontin and mucosal protection. J. Dent. Res.85(5), 404–415 (2006).
   PubMedGoogle Scholar
• Wang KX, Denhardt DT. Osteopontin: role in immune regulation and stress responses. Cytokine Growth Factor Rev.19(5–6), 333–345 (2008).
   PubMed Web of Science ®Google Scholar
• Cantor H, Shinohara ML. Regulation of T-helper-cell lineage development by osteopontin: the inside story. Nat. Rev. Immunol.9(2), 137–141 (2009).
   PubMed Web of Science ®Google Scholar
• Shinohara ML, Kim HJ, Kim JH, Garcia VA, Cantor H. Alternative translation of osteopontin generates intracellular and secreted isoforms that mediate distinct biological activities in dendritic cells. Proc. Natl Acad. Sci. USA105(20), 7235–7239 (2008).
   PubMedGoogle Scholar
• Ashkar S, Weber GF, Panoutsakopoulou V et al. Eta-1 (osteopontin): an early component of type-1 (cell-mediated) immunity. Science287(5454), 860–864 (2000).
   PubMed Web of Science ®Google Scholar
• O’Regan AW, Nau GJ, Chupp GL, Berman JS. Osteopontin (Eta-1) in cell-mediated immunity: teaching an old dog new tricks. Immunol. Today21(10), 475–478 (2000).
   PubMedGoogle Scholar
• Weiss JM, Renkl AC, Maier CS et al. Osteopontin is involved in the initiation of cutaneous contact hypersensitivity by inducing Langerhans and dendritic cell migration to lymph nodes. J. Exp. Med.194(9), 1219–1229 (2001).
   Google Scholar
• Kohan M, Bader R, Puxeddu I, Levi-Schaffer F, Breuer R, Berkman N. Enhanced osteopontin expression in a murine model of allergen-induced airway remodelling. Clin. Exp. Allergy37(10), 1444–1454 (2007).
   Google Scholar
• Lu X, Zhang XH, Wang H et al. Expression of osteopontin in chronic rhinosinusitis with and without nasal polyps. Allergy64(1), 104–111 (2009).
   PubMed Web of Science ®Google Scholar
• Xanthou G, Alissafi T, Semitekolou M et al. Osteopontin has a crucial role in allergic airway disease through regulation of dendritic cell subsets. Nat. Med.13(5), 570–578 (2007).
   PubMed Web of Science ®Google Scholar
• Fet V, Dickinson ME, Hogan BL. Localization of the mouse gene for secreted phosphoprotein 1 (Spp-1) (2ar, osteopontin, bone sialoprotein 1, 44-kDa bone phosphoprotein, tumor-secreted phosphoprotein) to chromosome 5, closely linked to Ric (Rickettsia resistance). Genomics5(2), 375–377 (1989).
   Google Scholar
• Patarca R, Freeman GJ, Singh RP et al. Structural and functional studies of the early T lymphocyte activation 1 (Eta-1) gene. Definition of a novel T cell-dependent response associated with genetic resistance to bacterial infection. J. Exp. Med.170(1), 145–161 (1989).
   PubMed Web of Science ®Google Scholar
• Young MF, Kerr JM, Termine JD et al. cDNA cloning, mRNA distribution and heterogeneity, chromosomal location, and RFLP analysis of human osteopontin (OPN). Genomics7(4), 491–502 (1990).
   PubMed Web of Science ®Google Scholar
• Craig AM, Denhardt DT. The murine gene encoding secreted phosphoprotein 1 (osteopontin): promoter structure, activity, and induction in vivo by estrogen and progesterone. Gene100, 163–171 (1991).
   PubMed Web of Science ®Google Scholar
• Hijiya N, Setoguchi M, Matsuura K, Higuchi Y, Akizuki S, Yamamoto S. Cloning and characterization of the human osteopontin gene and its promoter. Biochem. J.303(Pt 1), 255–262 (1994).
   PubMed Web of Science ®Google Scholar
• Saitoh Y, Kuratsu J, Takeshima H, Yamamoto S, Ushio Y. Expression of osteopontin in human glioma. Its correlation with the malignancy. Lab. Invest.72(1), 55–63 (1995).
   PubMed Web of Science ®Google Scholar
• Tanaka K, Morimoto J, Kon S et al. Effect of osteopontin alleles on β-glucan-induced granuloma formation in the mouse liver. Am. J. Pathol.164(2), 567–575 (2004).
   PubMed Web of Science ®Google Scholar
• Oldberg A, Franzen A, Heinegard D. Cloning and sequence analysis of rat bone sialoprotein (osteopontin) cDNA reveals an Arg-Gly-Asp cell-binding sequence. Proc. Natl Acad. Sci. USA83(23), 8819–8823 (1986).
   PubMed Web of Science ®Google Scholar
• Craig AM, Smith JH, Denhardt DT. Osteopontin, a transformation-associated cell adhesion phosphoprotein, is induced by 12-O-tetradecanoylphorbol 13-acetate in mouse epidermis. J. Biol. Chem.264(16), 9682–9689 (1989).
   PubMed Web of Science ®Google Scholar
• Kiefer MC, Bauer DM, Barr PJ. The cDNA and derived amino acid sequence for human osteopontin. Nucleic Acids Res.17(8), 3306 (1989).
   Google Scholar
• Wrana JL, Zhang Q, Sodek J. Full length cDNA sequence of porcine secreted phosphoprotein-I (SPP-I, osteopontin). Nucleic Acids Res.17(23), 10119 (1989).
   Google Scholar
• Tezuka K, Sato T, Kamioka H et al. Identification of osteopontin in isolated rabbit osteoclasts. Biochem. Biophys. Res. Commun.186(2), 911–917 (1992).
   PubMed Web of Science ®Google Scholar
• Kerr JM, Fisher LW, Termine JD, Young MF. The cDNA cloning and RNA distribution of bovine osteopontin. Gene108(2), 237–243 (1991).
   PubMed Web of Science ®Google Scholar
• Senger DR, Asch BB, Smith BD, Perruzzi CA, Dvorak HF. A secreted phosphoprotein marker for neoplastic transformation of both epithelial and fibroblastic cells. Nature302(5910), 714–715 (1983).
   PubMed Web of Science ®Google Scholar
• Franzen A, Heinegard D. Isolation and characterization of two sialoproteins present only in bone calcified matrix. Biochem. J.232(3), 715–724 (1985).
   PubMed Web of Science ®Google Scholar
• Smith JH, Denhardt DT. Molecular cloning of a tumor promoter-inducible mRNA found in JB6 mouse epidermal cells: induction is stable at high, but not at low, cell densities. J. Cell Biochem.34(1), 13–22 (1987).
   PubMed Web of Science ®Google Scholar
• Prince CW. Secondary structure predictions for rat osteopontin. Connect. Tissue Res.21(1–4), 15–20 (1989).
   PubMed Web of Science ®Google Scholar
• Sodek J, Ganss B, McKee MD. Osteopontin. Crit. Rev. Oral Biol. Med.11(3), 279–303 (2000).
   PubMedGoogle Scholar
• Kazanecki CC, Uzwiak DJ, Denhardt DT. Control of osteopontin signaling and function by post-translational phosphorylation and protein folding. J. Cell Biochem.102(4), 912–924 (2007).
   PubMed Web of Science ®Google Scholar
• Yokosaki Y, Tanaka K, Higashikawa F, Yamashita K, Eboshida A. Distinct structural requirements for binding of the integrins αvβ6, αvβ3, αvβ5, α5β1 and α9β1 to osteopontin. Matrix Biol.24(6), 418–427 (2005).
   PubMed Web of Science ®Google Scholar
• Barry ST, Ludbrook SB, Murrison E, Horgan CM. Analysis of the α4β1 integrin–osteopontin interaction. Exp. Cell Res.258(2), 342–351 (2000).
   Google Scholar
• Smith LL, Cheung HK, Ling LE et al. Osteopontin N-terminal domain contains a cryptic adhesive sequence recognized by α9β1 integrin. J. Biol. Chem.271(45), 28485–28491 (1996).
   PubMed Web of Science ®Google Scholar
• Grassinger J, Haylock DN, Storan MJ et al. Thrombin-cleaved osteopontin regulates hemopoietic stem and progenitor cell functions through interactions with α9β1 and α4β1 integrins. Blood114(1), 49–59 (2009).
   PubMedGoogle Scholar
• Hasegawa M, Nakoshi Y, Iino T et al. Thrombin-cleaved osteopontin in synovial fluid of subjects with rheumatoid arthritis. J. Rheumatol.36(2), 240–245 (2009).
   Google Scholar
• Khan SA, Cook AC, Kappil M et al. Enhanced cell surface CD44 variant (v6, v9) expression by osteopontin in breast cancer epithelial cells facilitates tumor cell migration: novel post-transcriptional, post-translational regulation. Clin. Exp. Metastasis22(8), 663–673 (2005).
   Google Scholar
• Weber GF, Ashkar S, Glimcher MJ, Cantor H. Receptor-ligand interaction between CD44 and osteopontin (Eta-1). Science271(5248), 509–512 (1996).
   PubMed Web of Science ®Google Scholar
• Katagiri YU, Sleeman J, Fujii H et al. CD44 variants but not CD44s cooperate with β1-containing integrins to permit cells to bind to osteopontin independently of arginine-glycine-aspartic acid, thereby stimulating cell motility and chemotaxis. Cancer Res.59(1), 219–226 (1999).
   PubMed Web of Science ®Google Scholar
• Lin YH, Huang CJ, Chao JR et al. Coupling of osteopontin and its cell surface receptor CD44 to the cell survival response elicited by interleukin-3 or granulocyte-macrophage colony-stimulating factor. Mol. Cell Biol.20(8), 2734–2742 (2000).
   PubMedGoogle Scholar
• Senger DR, Ledbetter SR, Claffey KP, Papadopoulos-Sergiou A, Peruzzi CA, Detmar M. Stimulation of endothelial cell migration by vascular permeability factor/vascular endothelial growth factor through cooperative mechanisms involving the αvβ3 integrin, osteopontin, and thrombin. Am. J. Pathol.149(1), 293–305 (1996).
   PubMed Web of Science ®Google Scholar
• Denhardt DT, Noda M, O’Regan AW, Pavlin D, Berman JS. Osteopontin as a means to cope with environmental insults: regulation of inflammation, tissue remodeling, and cell survival. J. Clin. Invest.107(9), 1055–1061 (2001).
   PubMed Web of Science ®Google Scholar
• Zohar R, Suzuki N, Suzuki K et al. Intracellular osteopontin is an integral component of the CD44-ERM complex involved in cell migration. J. Cell Physiol.184(1), 118–130 (2000).
   PubMed Web of Science ®Google Scholar
• Kon S, Ikesue M, Kimura C et al. Syndecan-4 protects against osteopontin-mediated acute hepatic injury by masking functional domains of osteopontin. J. Exp. Med.205(1), 25–33 (2008).
   Google Scholar
• Keykhosravani M, Doherty-Kirby A, Zhang C et al. Comprehensive identification of post-translational modifications of rat bone osteopontin by mass spectrometry. Biochemistry44(18), 6990–7003 (2005).
   PubMed Web of Science ®Google Scholar
• Christensen B, Nielsen MS, Haselmann KF, Petersen TE, Sorensen ES. Post-translationally modified residues of native human osteopontin are located in clusters: identification of 36 phosphorylation and five O-glycosylation sites and their biological implications. Biochem. J.390(Pt 1), 285–292 (2005).
   PubMed Web of Science ®Google Scholar
• Crawford HC, Matrisian LM, Liaw L. Distinct roles of osteopontin in host defense activity and tumor survival during squamous cell carcinoma progression in vivo. Cancer Res.58(22), 5206–5215 (1998).
   PubMed Web of Science ®Google Scholar
• Weber GF, Zawaideh S, Hikita S, Kumar VA, Cantor H, Ashkar S. Phosphorylation-dependent interaction of osteopontin with its receptors regulates macrophage migration and activation. J. Leukoc. Biol.72(4), 752–761 (2002).
   PubMed Web of Science ®Google Scholar
• Sorensen ES, Petersen TE. Phosphorylation, glycosylation, and transglutaminase sites in bovine osteopontin. Ann. NY Acad. Sci.760, 363–366 (1995).
   PubMed Web of Science ®Google Scholar
• Sorensen ES, Hojrup P, Petersen TE. Posttranslational modifications of bovine osteopontin: identification of twenty-eight phosphorylation and three O-glycosylation sites. Protein Sci.4(10), 2040–2049 (1995).
   PubMed Web of Science ®Google Scholar
• Shanmugam V, Chackalaparampil I, Kundu GC, Mukherjee AB, Mukherjee BB. Altered sialylation of osteopontin prevents its receptor-mediated binding on the surface of oncogenically transformed tsB77 cells. Biochemistry36(19), 5729–5738 (1997).
   Google Scholar
• Kaartinen MT, Pirhonen A, Linnala-Kankkunen A, Maenpaa PH. Cross-linking of osteopontin by tissue transglutaminase increases its collagen binding properties. J. Biol. Chem.274(3), 1729–1735 (1999).
   PubMed Web of Science ®Google Scholar
• Higashikawa F, Eboshida A, Yokosaki Y. Enhanced biological activity of polymeric osteopontin. FEBS Lett.581(14), 2697–2701 (2007).
   PubMed Web of Science ®Google Scholar
• Lorand L, Graham RM. Transglutaminases: crosslinking enzymes with pleiotropic functions. Nat. Rev. Mol. Cell Biol.4(2), 140–156 (2003).
   PubMed Web of Science ®Google Scholar
• Beninati S, Senger DR, Cordella-Miele E et al. Osteopontin: its transglutaminase-catalyzed posttranslational modifications and crosslinking to fibronectin. J. Biochem.115(4), 675–682 (1994).
   PubMed Web of Science ®Google Scholar
• Coca AF, Cooke RA. On the classification of the phenomena of hypersensitiveness. J. Immunol.8, 163–182 (1923).
   Google Scholar
• Allergy (2nd Edition). Holgate ST, Church MK, Lichtenstein LM (Eds). Mosby, London, UK (2001).
   Google Scholar
• Girolomoni G, Gisondi P, Ottaviani C, Cavani A. Immunoregulation of allergic contact dermatitis. J. Dermatol.31(4), 264–270 (2004).
   PubMedGoogle Scholar
• Martin SF, Jakob T. From innate to adaptive immune responses in contact hypersensitivity. Curr. Opin. Allergy Clin. Immunol.8(4), 289–293 (2008).
   PubMed Web of Science ®Google Scholar
• Ho IC, Glimcher LH. Transcription: tantalizing times for T cells. Cell109(Suppl.), S109–S120 (2002).
   PubMed Web of Science ®Google Scholar
• Akira S, Takeda K, Kaisho T. Toll-like receptors: critical proteins linking innate and acquired immunity. Nat. Immunol.2(8), 675–680 (2001).
   PubMed Web of Science ®Google Scholar
• Manetti R, Parronchi P, Giudizi MG et al. Natural killer cell stimulatory factor (interleukin 12 [IL-12]) induces T helper type 1 (Th1)-specific immune responses and inhibits the development of IL-4-producing Th cells. J. Exp. Med.177(4), 1199–1204 (1993).
   PubMed Web of Science ®Google Scholar
• Manetti R, Annunziato F, Gianno V et al. Th1 and Th2 cells in HIV infection. Chem. Immunol.63, 138–157 (1996).
   Google Scholar
• Parronchi P, De Carli M, Manetti R et al. IL-4 and IFN (α and γ) exert opposite regulatory effects on the development of cytolytic potential by Th1 or Th2 human T cell clones. J. Immunol.149(9), 2977–2983 (1992).
   PubMed Web of Science ®Google Scholar
• Hochrein H, Shortman K, Vremec D, Scott B, Hertzog P, O’Keeffe M. Differential production of IL-12, IFN-α, and IFN-γ by mouse dendritic cell subsets. J. Immunol.166(9), 5448–5455 (2001).
   PubMed Web of Science ®Google Scholar
• He R, Geha RS. Thymic stromal lymphopoietin. Ann. NY Acad. Sci.1183, 13–24 (2010).
   PubMed Web of Science ®Google Scholar
• Grogan JL, Mohrs M, Harmon B, Lacy DA, Sedat JW, Locksley RM. Early transcription and silencing of cytokine genes underlie polarization of T helper cell subsets. Immunity14(3), 205–215 (2001).
   PubMed Web of Science ®Google Scholar
• Mullen AC, High FA, Hutchins AS et al. Role of T-bet in commitment of TH1 cells before IL-12-dependent selection. Science292(5523), 1907–1910 (2001).
   PubMed Web of Science ®Google Scholar
• Afkarian M, Sedy JR, Yang J et al. T-bet is a STAT1-induced regulator of IL-12R expression in naive CD4+ T cells. Nat. Immunol.3(6), 549–557 (2002).
   PubMed Web of Science ®Google Scholar
• Lighvani AA, Frucht DM, Jankovic D et al. T-bet is rapidly induced by interferon-γ in lymphoid and myeloid cells. Proc. Natl Acad. Sci. USA98(26), 15137–15142 (2001).
   PubMed Web of Science ®Google Scholar
• Amsen D, Blander JM, Lee GR, TanigakiK, Honjo T, Flavell RA. Instruction of distinct CD4 T helper cell fates by different notch ligands on antigen-presenting cells. Cell117(4), 515–526 (2004).
   PubMed Web of Science ®Google Scholar
• Amsen D, Antov A, Jankovic D et al. Direct regulation of Gata3 expression determines the T helper differentiation potential of Notch. Immunity27(1), 89–99 (2007).
   PubMed Web of Science ®Google Scholar
• Liotta F, Frosali F, Querci V et al. Human immature myeloid dendritic cells trigger a TH2-polarizing program via Jagged-1/Notch interaction. J. Allergy Clin. Immunol.121(4), 1000–1005.e8 (2008).
   PubMed Web of Science ®Google Scholar
• Fallon PG, Ballantyne SJ, Mangan NE et al. Identification of an interleukin (IL)-25-dependent cell population that provides IL-4, IL-5, and IL-13 at the onset of helminth expulsion. J. Exp. Med.203(4), 1105–1116 (2006).
   PubMed Web of Science ®Google Scholar
• Schmitz J, Thiel A, Kuhn R et al. Induction of interleukin 4 (IL-4) expression in T helper (Th) cells is not dependent on IL-4 from non-Th cells. J. Exp. Med.179(4), 1349–1353 (1994).
   PubMed Web of Science ®Google Scholar
• Ouyang W, Lohning M, Gao Z et al. Stat6-independent GATA-3 autoactivation directs IL-4-independent Th2 development and commitment. Immunity12(1), 27–37 (2000).
   PubMed Web of Science ®Google Scholar
• Zhu J, Yamane H, Cote-Sierra J, Guo L, Paul WE. GATA-3 promotes Th2 responses through three different mechanisms: induction of Th2 cytokine production, selective growth of Th2 cells and inhibition of Th1 cell-specific factors. Cell Res.16(1), 3–10 (2006).
   PubMed Web of Science ®Google Scholar
• Bettelli E, Carrier Y, Gao W et al. Reciprocal developmental pathways for the generation of pathogenic effector TH17 and regulatory T cells. Nature441(7090), 235–238 (2006).
   PubMed Web of Science ®Google Scholar
• Ivanov, II, McKenzie BS, Zhou L et al. The orphan nuclear receptor RORγt directs the differentiation program of proinflammatory IL-17+ T helper cells. Cell126(6), 1121–1133 (2006).
   PubMed Web of Science ®Google Scholar
• Louten J, Boniface K, de Waal Malefyt R. Development and function of TH17 cells in health and disease. J. Allergy Clin. Immunol.123(5), 1004–1011 (2009).
   PubMed Web of Science ®Google Scholar
• Fouser LA, Wright JF, Dunussi-Joannopoulos K, Collins M. Th17 cytokines and their emerging roles in inflammation and autoimmunity. Immunol. Rev.226, 87–102 (2008).
   PubMed Web of Science ®Google Scholar
• van Beelen AJ, Teunissen MB, Kapsenberg ML, de Jong EC. Interleukin-17 in inflammatory skin disorders. Curr. Opin. Allergy Clin. Immunol.7(5), 374–381 (2007).
   Google Scholar
• He R, Kim HY, Yoon J et al. Exaggerated IL-17 response to epicutaneous sensitization mediates airway inflammation in the absence of IL-4 and IL-13. J. Allergy Clin. Immunol.124(4), 761.e1–770.e1 (2009).
   Google Scholar
• Shinohara ML, Jansson M, Hwang ES, Werneck MB, Glimcher LH, Cantor H. T-bet-dependent expression of osteopontin contributes to T cell polarization. Proc. Natl Acad. Sci. USA102(47), 17101–17106 (2005).
   Google Scholar
• Zohar R, Lee W, Arora P, Cheifetz S, McCulloch C, Sodek J. Single cell analysis of intracellular osteopontin in osteogenic cultures of fetal rat calvarial cells. J. Cell Physiol.170(1), 88–100 (1997).
   Google Scholar
• Seier AM, Renkl AC, Schulz G et al. Antigen-specific induction of osteopontin contributes to the chronification of allergic contact dermatitis. Am. J. Pathol.176(1), 246–258 (2010).
   Google Scholar
• Shinohara ML, Lu L, Bu J et al. Osteopontin expression is essential for interferon-α production by plasmacytoid dendritic cells. Nat. Immunol.7(5), 498–506 (2006).
   PubMed Web of Science ®Google Scholar
• Maeno Y, Nakazawa S, Yamamoto N et al. Osteopontin participates in Th1-mediated host resistance against nonlethal malaria parasite Plasmodium chabaudi chabaudi infection in mice. Infect. Immun.74(4), 2423–2427 (2006).
   PubMed Web of Science ®Google Scholar
• Shinohara ML, Kim JH, Garcia VA, Cantor H. Engagement of the type I interferon receptor on dendritic cells inhibits T helper 17 cell development: role of intracellular osteopontin. Immunity29(1), 68–78 (2008).
   PubMed Web of Science ®Google Scholar
• Renkl AC, Wussler J, Ahrens T et al. Osteopontin functionally activates dendritic cells and induces their differentiation toward a Th1-polarizing phenotype. Blood106(3), 946–955 (2005).
   Google Scholar
• Murugaiyan G, Mittal A, Weiner HL. Increased osteopontin expression in dendritic cells amplifies IL-17 production by CD4+ T cells in experimental autoimmune encephalomyelitis and in multiple sclerosis. J. Immunol.181(11), 7480–7488 (2008).
   PubMed Web of Science ®Google Scholar
• Schulz G, Renkl AC, Seier A, Liaw L, Weiss JM. Regulated osteopontin expression by dendritic cells decisively affects their migratory capacity. J. Invest. Dermatol.128(10), 2541–2544 (2008).
   Google Scholar
• Alcorn JF, Crowe CR, Kolls JK. TH17 cells in asthma and COPD. Annu. Rev. Physiol.72, 495–516 (2010).
   PubMed Web of Science ®Google Scholar
• Metz M, Maurer M. Innate immunity and allergy in the skin. Curr. Opin. Immunol.21(6), 687–693 (2009).
   PubMed Web of Science ®Google Scholar
• Axtell RC, de Jong BA, Boniface K et al. T helper type 1 and 17 cells determine efficacy of interferon-β in multiple sclerosis and experimental encephalomyelitis. Nat. Med.16(4), 406–412 (2010).
   PubMed Web of Science ®Google Scholar
• Steinman L. Mixed results with modulation of TH-17 cells in human autoimmune diseases. Nat. Immunol.11(1), 41–44 (2010).
   PubMed Web of Science ®Google Scholar
• Leipe J, Grunke M, Dechant C et al. Th17 cells in autoimmune arthritis. Arthritis Rheum.62(10), 2876–2885 (2010).
   PubMed Web of Science ®Google Scholar
• Murugaiyan G, Mittal A, Weiner HL. Identification of an IL-27/osteopontin axis in dendritic cells and its modulation by IFN-γ limits IL-17-mediated autoimmune inflammation. Proc. Natl Acad. Sci. USA107(25), 11495–11500 (2010).
   PubMed Web of Science ®Google Scholar
• Yoshida H, Nakaya M, Miyazaki Y. Interleukin 27: a double-edged sword for offense and defense. J. Leukoc. Biol.86(6), 1295–1303 (2009).
   Google Scholar
• Pennino D, Eyerich K, Scarponi C et al. IL-17 amplifies human contact hypersensitivity by licensing hapten nonspecific Th1 cells to kill autologous keratinocytes. J. Immunol.184(9), 4880–4888 (2010).
   PubMed Web of Science ®Google Scholar
• Eder W, Ege MJ, von Mutius E. The asthma epidemic. N. Engl. J. Med.355(21), 2226–2235 (2006).
   PubMed Web of Science ®Google Scholar
• Meltzer EO. The prevalence and medical and economic impact of allergic rhinitis in the United States. J. Allergy Clin. Immunol.99(6 Pt 2), S805–S828 (1997).
   PubMed Web of Science ®Google Scholar
• Pawankar R, Bunnag C, Chen Y et al. Allergic rhinitis and its impact on asthma update (ARIA 2008) – western and Asian–Pacific perspective. Asian Pac. J. Allergy Immunol.27(4), 237–243 (2009).
   PubMed Web of Science ®Google Scholar
• Greenberger PA. Interactions between rhinitis and asthma. Allergy Asthma Proc.25(2), 89–93 (2004).
   Google Scholar
• Liu Y, Lu X, Yu HJ et al. The expression of osteopontin and its association with Clara cell 10 kDa protein in allergic rhinitis. Clin. Exp. Allergy40(11), 1632–1641 (2010).
   PubMed Web of Science ®Google Scholar
• Kurokawa M, Konno S, Matsukura S et al. Effects of corticosteroids on osteopontin expression in a murine model of allergic asthma. Int. Arch. Allergy Immunol.149(Suppl. 1), 7–13 (2009).
   Google Scholar
• Takahashi A, Kurokawa M, Konno S et al. Osteopontin is involved in migration of eosinophils in asthma. Clin. Exp. Allergy39(8), 1152–1159 (2009).
   Google Scholar
• Samitas K, Zervas E, Vittorakis S et al. Osteopontin expression and relation to disease severity in human asthma. Eur. Respir. J. DOI: 10.1183/09031936.00017810 (2010) (Epub ahead of print).
   Google Scholar
• Uchio E, Matsuura N, Kadonosono K, Ohno S, Uede T. Tear osteopontin levels in patients with allergic conjunctival diseases. Graefes Arch. Clin. Exp. Ophthalmol.240(11), 924–928 (2002).
   Google Scholar
• Chen LC, Zhang Z, Myers AC, Huang SK. Cutting edge: altered pulmonary eosinophilic inflammation in mice deficient for Clara cell secretory 10-kDa protein. J. Immunol.167(6), 3025–3028 (2001).
   PubMed Web of Science ®Google Scholar
• de Heer HJ, Hammad H, Soullie T et al. Essential role of lung plasmacytoid dendritic cells in preventing asthmatic reactions to harmless inhaled antigen. J. Exp. Med.200(1), 89–98 (2004).
   Google Scholar
• Kohl J, Baelder R, Lewkowich IP et al. A regulatory role for the C5a anaphylatoxin in type 2 immunity in asthma. J. Clin. Invest.116(3), 783–796 (2006).
   PubMed Web of Science ®Google Scholar
• Idzko M, Hammad H, van Nimwegen M et al. Local application of FTY720 to the lung abrogates experimental asthma by altering dendritic cell function. J. Clin. Invest.116(11), 2935–2944 (2006).
   PubMed Web of Science ®Google Scholar
• Ehrchen JM, Roebrock K, Foell D et al. Keratinocytes determine Th1 immunity during early experimental leishmaniasis. PLoS Pathog.6(4), e1000871 (2010).
   Google Scholar
• Mellman I, Turley SJ, Steinman RM. Antigen processing for amateurs and professionals. Trends Cell. Biol.8(6), 231–237 (1998).
   PubMed Web of Science ®Google Scholar
• Steinman RM, Hemmi H. Dendritic cells: translating innate to adaptive immunity. Curr. Top. Microbiol. Immunol.311, 17–58 (2006).
   PubMed Web of Science ®Google Scholar
• Barnes PJ. Immunology of asthma and chronic obstructive pulmonary disease. Nat. Rev. Immunol.8(3), 183–192 (2008).
   PubMed Web of Science ®Google Scholar
• Bousquet J, Jeffery PK, Busse WW, Johnson M, Vignola AM. Asthma. From bronchoconstriction to airways inflammation and remodeling. Am. J. Respir. Crit. Care Med.161(5), 1720–1745 (2000).
   PubMed Web of Science ®Google Scholar
• Cockcroft DW, Davis BE. Mechanisms of airway hyperresponsiveness. J. Allergy Clin. Immunol.118(3), 551–559; quiz 560–551 (2006).
   PubMed Web of Science ®Google Scholar
• Bergeron C, Al-Ramli W, Hamid Q. Remodeling in asthma. Proc. Am. Thorac. Soc.6(3), 301–305 (2009).
   PubMedGoogle Scholar
• Homer RJ, Elias JA. Consequences of long-term inflammation. Airway remodeling. Clin. Chest Med.21(2), 331–343, ix (2000).
   PubMedGoogle Scholar
• Shinagawa K, Kojima M. Mouse model of airway remodeling: strain differences. Am. J. Respir. Crit. Care Med.168(8), 959–967 (2003).
   PubMed Web of Science ®Google Scholar
• Tomasek JJ, Gabbiani G, Hinz B, Chaponnier C, Brown RA. Myofibroblasts and mechano-regulation of connective tissue remodelling. Nat. Rev. Mol. Cell Biol.3(5), 349–363 (2002).
   PubMed Web of Science ®Google Scholar
• Puxeddu I, Alian A, Piliponsky AM, Ribatti D, Panet A, Levi-Schaffer F. Human peripheral blood eosinophils induce angiogenesis. Int. J. Biochem. Cell Biol.37(3), 628–636 (2005).
   Google Scholar
• Berman JS, Serlin D, Li X et al. Altered bleomycin-induced lung fibrosis in osteopontin-deficient mice. Am. J. Physiol. Lung Cell Mol. Physiol.286(6), L1311–L1318 (2004).
   PubMed Web of Science ®Google Scholar
• Liaw L, Birk DE, Ballas CB, Whitsitt JS, Davidson JM, Hogan BL. Altered wound healing in mice lacking a functional osteopontin gene (spp1). J. Clin. Invest.101(7), 1468–1478 (1998).
   PubMed Web of Science ®Google Scholar
• Pardo A, Gibson K, Cisneros J et al. Up-regulation and profibrotic role of osteopontin in human idiopathic pulmonary fibrosis. PLoS Med.2(9), e251 (2005).
   PubMed Web of Science ®Google Scholar
• Kohan M, Breuer R, Berkman N. Osteopontin induces airway remodeling and lung fibroblast activation in a murine model of asthma. Am. J. Respir. Cell Mol. Biol.41(3), 290–296 (2009).
   PubMed Web of Science ®Google Scholar
• Rosenberg HF, Phipps S, Foster PS. Eosinophil trafficking in allergy and asthma. J. Allergy Clin. Immunol.119(6), 1303–1310; quiz 1311–1302 (2007).
   PubMed Web of Science ®Google Scholar
• Humbles AA, Lloyd CM, McMillan SJ et al. A critical role for eosinophils in allergic airways remodeling. Science305(5691), 1776–1779 (2004).
   PubMed Web of Science ®Google Scholar
• Puxeddu I, Berkman N, Ribatti D et al. Osteopontin is expressed and functional in human eosinophils. Allergy65(2), 168–174 (2010).
   Google Scholar
• Wardlaw AJ, Walsh GM, Symon FA. Adhesion interactions involved in eosinophil migration through vascular endothelium. Ann. NY Acad. Sci.796, 124–137 (1996).
   Google Scholar
• Wenzel SE, Schwartz LB, Langmack EL et al. Evidence that severe asthma can be divided pathologically into two inflammatory subtypes with distinct physiologic and clinical characteristics. Am. J. Respir. Crit. Care Med.160(3), 1001–1008 (1999).
   PubMed Web of Science ®Google Scholar
• Rothenberg ME, Hogan SP. The eosinophil. Annu. Rev. Immunol.24, 147–174 (2006).
   PubMed Web of Science ®Google Scholar
• Puxeddu I, Ribatti D, Crivellato E, Levi-Schaffer F. Mast cells and eosinophils: a novel link between inflammation and angiogenesis in allergic diseases. J. Allergy Clin. Immunol.116(3), 531–536 (2005).
   Google Scholar
• Nagasaka A, Matsue H, Matsushima H et al. Osteopontin is produced by mast cells and affects IgE-mediated degranulation and migration of mast cells. Eur.J. Immunol.38(2), 489–499 (2008).
   Google Scholar
• Flood-Page P, Menzies-Gow A, Phipps S et al. Anti-IL-5 treatment reduces deposition of ECM proteins in the bronchial subepithelial basement membrane of mild atopic asthmatics. J. Clin. Invest.112(7), 1029–1036 (2003).
   PubMed Web of Science ®Google Scholar
• Lee JJ, Dimina D, Macias MP et al. Defining a link with asthma in mice congenitally deficient in eosinophils. Science305(5691), 1773–1776 (2004).
   PubMed Web of Science ®Google Scholar
• Okayama Y, Kawakami T. Development, migration, and survival of mast cells. Immunol. Res.34(2), 97–115 (2006).
   PubMed Web of Science ®Google Scholar
• Stelekati E, Bahri R, D’Orlando O et al. Mast cell-mediated antigen presentation regulates CD8+ T cell effector functions. Immunity31(4), 665–676 (2009).
   PubMed Web of Science ®Google Scholar
• Ozdemir C. An immunological overview of allergen specific immunotherapy – subcutaneous and sublingual routes. Ther. Adv. Respir. Dis.3(5), 253–262 (2009).
   Google Scholar
• Larche M, Akdis CA, Valenta R. Immunological mechanisms of allergen-specific immunotherapy. Nat. Rev. Immunol.6(10), 761–771 (2006).
   PubMed Web of Science ®Google Scholar
• Konno S, Golden DB, Schroeder J, Hamilton RG, Lichtenstein LM, Huang SK. Increased expression of osteopontin is associated with long-term bee venom immunotherapy. J. Allergy Clin. Immunol.115(5), 1063–1067 (2005).
   Google Scholar
• Konno S, Hizawa N, Nishimura M, Huang SK. Osteopontin: a potential biomarker for successful bee venom immunotherapy and a potential molecule for inhibiting IgE-mediated allergic responses. Allergol. Int.55(4), 355–359 (2006).
   Google Scholar
• Diepgen TL, Coenraads PJ. The epidemiology of occupational contact dermatitis. Int. Arch. Occup. Environ. Health72(8), 496–506 (1999).
   PubMed Web of Science ®Google Scholar
• Thyssen JP, Menne T, Schnuch A et al. Acceptable risk of contact allergy in the general population assessed by CE-DUR – a method to detect and categorize contact allergy epidemics based on patient data. Regul. Toxicol. Pharmacol.54(2), 183–187 (2009).
   PubMed Web of Science ®Google Scholar
• Thyssen JP, Linneberg A, Menne T, Johansen JD. The epidemiology of contact allergy in the general population – prevalence and main findings. Contact Derm.57(5), 287–299 (2007).
   PubMed Web of Science ®Google Scholar
• Thyssen JP, Johansen JD, Menne T. Contact allergy epidemics and their controls. Contact Derm.56(4), 185–195 (2007).
   PubMed Web of Science ®Google Scholar
• Thyssen JP, Johansen JD, Linneberg A, Menne T. The epidemiology of hand eczema in the general population – prevalence and main findings. Contact Derm.62(2), 75–87 (2010).
   PubMed Web of Science ®Google Scholar
• Saint-Mezard P, Berard F, Dubois B, Kaiserlian D, Nicolas JF. The role of CD4+ and CD8+ T cells in contact hypersensitivity and allergic contact dermatitis. Eur. J. Dermatol.14(3), 131–138 (2004).
   PubMed Web of Science ®Google Scholar
• Cavani A, De Pita O, Girolomoni G. New aspects of the molecular basis of contact allergy. Curr. Opin. Allergy Clin. Immunol.7(5), 404–408 (2007).
   PubMed Web of Science ®Google Scholar
• Kimber I, Dearman RJ. Allergic contact dermatitis: the cellular effectors. Contact Derm.46(1), 1–5 (2002).
   PubMed Web of Science ®Google Scholar
• Hogan DJ, Dannaker CJ, Maibach HI. The prognosis of contact dermatitis. J. Am. Acad. Dermatol.23(2 Pt 1), 300–307 (1990).
   PubMed Web of Science ®Google Scholar
• Saint-Mezard P, Rosieres A, Krasteva M et al. Allergic contact dermatitis. Eur. J. Dermatol.14(5), 284–295 (2004).
   PubMed Web of Science ®Google Scholar
• Cavani A, Albanesi C, Traidl C, Sebastiani S, Girolomoni G. Effector and regulatory T cells in allergic contact dermatitis. Trends Immunol.22(3), 118–120 (2001).
   PubMed Web of Science ®Google Scholar
• Pichler BJ, Kneilling M, Haubner R et al. Imaging of delayed-type hypersensitivity reaction by PET and 18F-galacto-RGD. J. Nucl. Med.46(1), 184–189 (2005).
   PubMed Web of Science ®Google Scholar
• Weiss JM, Renkl AC, Sleeman J et al. CD44 variant isoforms are essential for the function of epidermal Langerhans cells and dendritic cells. Cell. Adhes. Commun.6(2–3), 157–160 (1998).
   PubMed Web of Science ®Google Scholar
• Hur EM, Youssef S, Haws ME, Zhang SY, Sobel RA, Steinman L. Osteopontin-induced relapse and progression of autoimmune brain disease through enhanced survival of activated T cells. Nat. Immunol.8(1), 74–83 (2007).
   PubMed Web of Science ®Google Scholar