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Original Research

Identification of CD245 as myosin 18A, a receptor for surfactant A: A novel pathway for activating human NK lymphocytes

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Article: e1127493 | Received 16 Sep 2015, Accepted 25 Nov 2015, Published online: 04 May 2016

References

  • Rosenberg EB, Herberman RB, Levine PH, Halterman RH, McCoy JL, Wunderlich JR. Lymphocyte cytotoxicity reactions to leukemia-associated antigens in identical twins. Int J Cancer 1972; 9(3):648-58; PMID:4513057; http://dx.doi.org/10.1002/ijc.2910090323
  • Benson DM, Caligiuri MA. Killer immunoglobulin-like receptors and tumor immunity. Cancer Immunol Res 2014; 2(2):99-104; PMID:24592397; http://dx.doi.org/10.1158/2326-6066.CIR-13-0219
  • Moffett-King A. Natural killer cells and pregnancy. Nat Rev Immunol 2002; 2(9):656-63; PMID:12209134; http://dx.doi.org/10.1038/nri886
  • Lanier LL. Up on the tightrope: natural killer cell activation and inhibition. Nat Immunol 2008; 9(5):495-502; PMID:18425106; http://dx.doi.org/10.1038/ni1581
  • Le Bouteiller P, Barakonyi A, Giustiniani J, Lenfant F, Marie-Cardine A, Aguerre-Girr M, Rabot M, Hilgert I, Mami-Chouaib F, Tabiasco J et al. Engagement of CD160 receptor by HLA-C is a triggering mechanism used by circulating natural killer (NK) cells to mediate cytotoxicity. Proc Natl Acad Sci U S A 2002; 99(26):16963-8; PMID:12486241; http://dx.doi.org/10.1073/pnas.012681099
  • Bensussan A, Gluckman E, Marsafy S el, Schiavon V, Mansur IG, Dausset J, Boumsell L, Carosella E. BY55 monoclonal antibody delineates within human cord blood and bone marrow lymphocytes distinct cell subsets mediating cytotoxic activity. Proc Natl Acad Sci U S A 1994; 91(19):9136-40; PMID:8090781; http://dx.doi.org/10.1073/pnas.91.19.9136
  • Melero I, Johnston JV, Shufford WW, Mittler RS, Chen L. NK1.1 cells express 4-1BB (CDw137) costimulatory molecule and are required for tumor immunity elicited by anti-4-1BB monoclonal antibodies. Cell Immunol 1998; 190(2):167-72; PMID:9878117; http://dx.doi.org/10.1006/cimm.1998.1396
  • Lin W, Voskens CJ, Zhang X, Schindler DG, Wood A, Burch E, Wei Y, Chen L, Tian G, Tamada K et al. Fc-dependent expression of CD137 on human NK cells: insights into «agonistic» effects of anti-CD137 monoclonal antibodies. Blood 2008; 112(3):699-707; PMID:18519814; http://dx.doi.org/10.1182/blood-2007-11-122465
  • Kohrt HE, Colevas AD, Houot R, Weiskopf K, Goldstein MJ, Lund P, Mueller A, Sagiv-Barfi I, Marabelle A, Lira R et al. Targeting CD137 enhances the efficacy of cetuximab. J Clin Invest 2014; 124(6):2668-82; PMID:24837434; http://dx.doi.org/10.1172/JCI73014
  • Kohrt HE, Houot R, Weiskopf K, Goldstein MJ, Scheeren F, Czerwinski D, Colevas AD, Weng WK, Clarke MF, Carlson RW et al. Stimulation of natural killer cells with a CD137-specific antibody enhances trastuzumab efficacy in xenotransplant models of breast cancer. J Clin Invest 2012; 122(3):1066-75; PMID:22326955; http://dx.doi.org/10.1172/JCI61226
  • Kohrt HE, Houot R, Goldstein MJ, Weiskopf K, Alizadeh AA, Brody J, Müller A, Pachynski R, Czerwinski D, Coutre S et al. CD137 stimulation enhances the antilymphoma activity of anti-CD20 antibodies. Blood 2011; 117(8):2423-32; PMID:21193697; http://dx.doi.org/10.1182/blood-2010-08-301945
  • Marie-Cardine A, Boumsell L, Bensussan A. The T-cell panel DY12 and DY35 mAbs define a novel receptor associated with protein tyrosine phosphatase activity in the leukeamic cell line YT indi. In: Leucocyte Typing VII. Oxford University Press. D Mason; 2002, Oxford University press, New York, USA. Edition D Mason. p. 688.
  • Giustiniani J, Marie-Cardine A, Bensussan A. A soluble form of the MHC class I-specific CD160 receptor is released from human activated NK lymphocytes and inhibits cell-mediated cytotoxicity. J Immunol 2007; 178(3):1293-300; PMID:17237375; http://dx.doi.org/10.4049/jimmunol.178.3.1293
  • Dufresne-Martin G, Lemay J-F, Lavigne P, Klarskov K. Peptide mass fingerprinting by matrix-assisted laser desorption ionization mass spectrometry of proteins detected by immunostaining on nitrocellulose. Proteomics 2005; 5(1):55-66; PMID:15602772; http://dx.doi.org/10.1002/pmic.200400902
  • Mansur I-G, Schiavon V, Giustiniani J, Bagot M, Bensussan A, Marie-Cardine A. Engagement of IL-1 receptor accessory protein (IL-1RAcP) with the monoclonal antibody AY19 provides co-activating signals and prolongs the CD2-induced proliferation of peripheral blood lymphocytes. Immunol Lett 2011; 139(1–2):52-7; PMID:21600927; http://dx.doi.org/10.1016/j.imlet.2011.04.015
  • Mori K, Furusawa T, Okubo T, Inoue T, Ikawa S, Yanai N, Mori KJ, Obinata M. Genome structure and differential expression of two isoforms of a novel PDZ-containing myosin (MysPDZ) (Myo18A). J Biochem (Tokyo) 2003; 133(4):405-13; PMID:12761286; http://dx.doi.org/10.1093/jb/mvg053
  • Yang C-H, Szeliga J, Jordan J, Faske S, Sever-Chroneos Z, Dorsett B, Christian RE, Settlage RE, Shabanowitz J, Hunt DF et al. Identification of the surfactant protein A receptor 210 as the unconventional myosin 18A. J Biol Chem 2005; 280(41):34447-57; PMID:16087679; http://dx.doi.org/10.1074/jbc.M505229200
  • Haagsman HP, Hawgood S, Sargeant T, Buckley D, White RT, Drickamer K, Benson BJ. The major lung surfactant protein, SP 28-36, is a calcium-dependent, carbohydrate-binding protein. J Biol Chem 1987; 262(29):13877-80; PMID:2820982
  • Mitsuhashi A, Goto H, Kuramoto T, Tabata S, Yukishige S, Abe S, Hanibuchi M, Kakiuchi S, Saijo A, Aono Y et al. Surfactant protein A suppresses lung cancer progression by regulating the polarization of tumor-associated macrophages. Am J Pathol 2013; 182(5):1843-53; PMID:23499372; http://dx.doi.org/10.1016/j.ajpath.2013.01.030
  • Cerwenka A, Lanier LL. Natural killer cells, viruses and cancer. Nat Rev Immunol 2001; 1(1):41-9; PMID:11905813; http://dx.doi.org/10.1038/35095564
  • McNeely TB, Coonrod JD. Aggregation and opsonization of type A but not type B Hemophilus influenzae by surfactant protein A. Am J Respir Cell Mol Biol 1994; 11(1):114-22; PMID:8018334; http://dx.doi.org/10.1165/ajrcmb.11.1.8018334
  • Pollok KE, Kim YJ, Hurtado J, Zhou Z, Kim KK, Kwon BS. 4-1BB T-cell antigen binds to mature B cells and macrophages, and costimulates anti-mu-primed splenic B cells. Eur J Immunol 1994; 24(2):367-74; PMID:8299685; http://dx.doi.org/10.1002/eji.1830240215
  • Zhao S, Zhang H, Xing Y, Natkunam Y. CD137 ligand is expressed in primary and secondary lymphoid follicles and in B-cell lymphomas: diagnostic and therapeutic implications. Am J Surg Pathol 2013; 37(2):250-8; PMID:23095505; http://dx.doi.org/10.1097/PAS.0b013e318268c6ea
  • Davis DM, Chiu I, Fassett M, Cohen GB, Mandelboim O, Strominger JL. The human natural killer cell immune synapse. Proc Natl Acad Sci U S A 1999; 96(26):15062-7; PMID:10611338; http://dx.doi.org/10.1073/pnas.96.26.15062
  • Rak GD, Mace EM, Banerjee PP, Svitkina T, Orange JS. Natural killer cell lytic granule secretion occurs through a pervasive actin network at the immune synapse. PLoS Biol 2011; 9(9):e1001151; PMID:21931536; http://dx.doi.org/10.1371/journal.pbio.1001151
  • Brown ACN, Oddos S, Dobbie IM, Alakoskela J-M, Parton RM, Eissmann P, Neil MA, Dunsby C, French PM, Davis I et al. Remodelling of cortical actin where lytic granules dock at natural killer cell immune synapses revealed by super-resolution microscopy. PLoS Biol 2011; 9(9):e1001152; PMID:21931537; http://dx.doi.org/10.1371/journal.pbio.1001152
  • Hsu R-M, Tsai M-H, Hsieh Y-J, Lyu P-C, Yu J-S. Identification of MYO18A as a novel interacting partner of the PAK2/betaPIX/GIT1 complex and its potential function in modulating epithelial cell migration. Mol Biol Cell 2010; 21(2):287-301; PMID:19923322; http://dx.doi.org/10.1091/mbc.E09-03-0232
  • Burshtyn DN, Scharenberg AM, Wagtmann N, Rajagopalan S, Berrada K, Yi T, Kinet JP, Long EO. Recruitment of tyrosine phosphatase HCP by the killer cell inhibitor receptor. Immunity 1996; 4(1):77-85; PMID:8574854; http://dx.doi.org/10.1016/S1074-7613(00)80300-3
  • Stebbins CC, Watzl C, Billadeau DD, Leibson PJ, Burshtyn DN, Long EO. Vav1 dephosphorylation by the tyrosine phosphatase SHP-1 as a mechanism for inhibition of cellular cytotoxicity. Mol Cell Biol 2003; 23(17):6291-9; PMID:12917349; http://dx.doi.org/10.1128/MCB.23.17.6291-6299.2003
  • Mahmood S, Kanwar N, Tran J, Zhang M-L, Kung SKP. SHP-1 phosphatase is a critical regulator in preventing natural killer cell self-killing. PloS One 2012; 7(8):e44244; PMID:22952938; http://dx.doi.org/10.1371/journal.pone.0044244
  • Purdy AK, Campbell KS. SHP-2 expression negatively regulates NK cell function. J Immunol 2009; 183(11):7234-43; PMID:19915046; http://dx.doi.org/10.4049/jimmunol.0900088
  • Dippold HC, Ng MM, Farber-Katz SE, Lee S-K, Kerr ML, Peterman MC, Sim R, Wiharto PA, Galbraith KA, Madhavarapu S et al. GOLPH3 bridges phosphatidylinositol-4- phosphate and actomyosin to stretch and shape the Golgi to promote budding. Cell 2009; 139(2):337-51; PMID:19837035; http://dx.doi.org/10.1016/j.cell.2009.07.052
  • Samten B, Townsend JC, Sever-Chroneos Z, Pasquinelli V, Barnes PF, Chroneos ZC. An antibody against the surfactant protein A (SP-A)-binding domain of the SP-A receptor inhibits T cell-mediated immune responses to Mycobacterium tuberculosis. J Leukoc Biol 2008; 84(1):115-23; PMID:18443188; http://dx.doi.org/10.1189/jlb.1207835
  • Mitra S, Beach C, Feng G-S, Plattner R. SHP-2 is a novel target of Abl kinases during cell proliferation. J Cell Sci 2008; 121(20):3335-46; PMID:18827006; http://dx.doi.org/10.1242/jcs.035691
  • MacGillivray M, Herrera-Abreu MT, Chow C-W, Shek C, Wang Q, Vachon E, Feng GS, Siminovitch KA, McCulloch CA, Downey GP. The protein tyrosine phosphatase SHP-2 regulates interleukin-1-induced ERK activation in fibroblasts. J Biol Chem 2003; 278(29):27190-8; PMID:12721296; http://dx.doi.org/10.1074/jbc.M213083200
  • Andzelm MM, Chen X, Krzewski K, Orange JS, Strominger JL. Myosin IIA is required for cytolytic granule exocytosis in human NK cells. J Exp Med 2007; 204(10):2285-91; PMID:17875677; http://dx.doi.org/10.1084/jem.20071143
  • Hsu R-M, Hsieh Y-J, Yang T-H, Chiang Y-C, Kan C-Y, Lin Y-T, Chen JT, Yu JS. Binding of the extreme carboxyl-terminus of PAK-interacting exchange factor β (βPIX) to myosin 18A (MYO18A) is required for epithelial cell migration. Biochim Biophys Acta 2014; 1843(11):2513-27; PMID:25014165; http://dx.doi.org/10.1016/j.bbamcr.2014.06.023
  • Furusawa T, Ikawa S, Yanai N, Obinata M. Isolation of a novel PDZ-containing myosin from hematopoietic supportive bone marrow stromal cell lines. Biochem Biophys Res Commun 2000; 270(1):67-75; PMID:10733906; http://dx.doi.org/10.1006/bbrc.2000.2377
  • Nakano T, Tani M, Nishioka M, Kohno T, Otsuka A, Ohwada S, Yokota J. Genetic and epigenetic alterations of the candidate tumor-suppressor gene MYO18B, on chromosome arm 22q, in colorectal cancer. Genes Chromosomes Cancer 2005; 43(2):162-71; PMID:15751041; http://dx.doi.org/10.1002/gcc.20180
  • Nishioka M, Kohno T, Tani M, Yanaihara N, Tomizawa Y, Otsuka A, Sasaki S, Kobayashi K, Niki T, Maeshima A et al. MYO18B, a candidate tumor suppressor gene at chromosome 22q12.1, deleted, mutated, and methylated in human lung cancer. Proc Natl Acad Sci U S A 2002; 99(19):12269-74; PMID:12209013; http://dx.doi.org/10.1073/pnas.192445899
  • Taft MH, Behrmann E, Munske-Weidemann L-C, Thiel C, Raunser S, Manstein DJ. Functional characterization of human myosin-18A and its interaction with F-actin and GOLPH3. J Biol Chem 2013; 288(42):30029-41; PMID:23990465; http://dx.doi.org/10.1074/jbc.M113.497180
  • Farber-Katz SE, Dippold HC, Buschman MD, Peterman MC, Xing M, Noakes CJ, Tat J, Ng MM, Rahajeng J, Cowan DM et al. DNA damage triggers Golgi dispersal via DNA-PK and GOLPH3. Cell 2014; 156(3):413-27; PMID:24485452; http://dx.doi.org/10.1016/j.cell.2013.12.023
  • Kuroki Y, Tsutahara S, Shijubo N, Takahashi H, Shiratori M, Hattori A, Honda Y, Abe S, Akino T. Elevated levels of lung surfactant protein A in sera from patients with idiopathic pulmonary fibrosis and pulmonary alveolar proteinosis. Am Rev Respir Dis 1993; 147(3):723-9; PMID:8442609; http://dx.doi.org/10.1164/ajrccm/147.3.723
  • Rubio S, Lacaze-Masmonteil T, Chailley-Heu B, Kahn A, Bourbon JR, Ducroc R. Pulmonary surfactant protein A (SP-A) is expressed by epithelial cells of small and large intestine. J Biol Chem 1995; 270(20):12162-9; PMID:7744866; http://dx.doi.org/10.1074/jbc.270.20.12162
  • Aiad HAS, El-Farargy SM, Soliman MM, El-Wahed Gaber MA, El-Aziz Othman SA. Immunohistochemical staining of surfactant proteins A and B in skin of psoriatic patients before and after narrow-band UVB phototherapy. Am J Clin Dermatol 2012; 13(5):341-8; PMID:22621659; http://dx.doi.org/10.2165/11630720-000000000-00000
  • Cunningham D, Humblet Y, Siena S, Khayat D, Bleiberg H, Santoro A, Bets D, Mueser M, Harstrick A, Verslype C et al. Cetuximab monotherapy and cetuximab plus irinotecan in irinotecan-refractory metastatic colorectal cancer. N Engl J Med 2004; 351(4):337-45; PMID:15269313; http://dx.doi.org/10.1056/NEJMoa033025

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