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Structural and biosynthetic features of the Mo5 human myeloid differentiation antigen
dc.contributor.authorGoldstein, Steven C.en_US
dc.contributor.authorTodd, Robert F. IIIen_US
dc.date.accessioned2010-04-01T15:06:31Z
dc.date.available2010-04-01T15:06:31Z
dc.date.issued1993-04en_US
dc.identifier.citationGoldstein, Steven C.; Todd, Robert F. (1993). "Structural and biosynthetic features of the Mo5 human myeloid differentiation antigen." Tissue Antigens 41(4): 214-218. <http://hdl.handle.net/2027.42/65573>en_US
dc.identifier.issn0001-2815en_US
dc.identifier.issn1399-0039en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/65573
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=8362416&dopt=citationen_US
dc.format.extent550328 bytes
dc.format.extent3110 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.publisherBlackwell Publishing Ltden_US
dc.rights1993 Blackwell Munksgaarden_US
dc.subject.otherAntigenen_US
dc.subject.otherBiosynthesisen_US
dc.subject.otherDifferentiationen_US
dc.subject.otherGlycoproteinen_US
dc.subject.otherMyeloiden_US
dc.subject.otherStructureen_US
dc.titleStructural and biosynthetic features of the Mo5 human myeloid differentiation antigenen_US
dc.typeArticleen_US
dc.rights.robotsIndexNoFollowen_US
dc.subject.hlbsecondlevelMicrobiology and Immunologyen_US
dc.subject.hlbtoplevelHealth Sciencesen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumSimpson Memorial Institute, Department of Internal Medicine, Division of Hematology and Oncology, The University of Michigan Medical School, Ann Arbor, MI, U.S.A.en_US
dc.identifier.pmid8362416en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/65573/1/j.1399-0039.1993.tb02007.x.pdf
dc.identifier.doi10.1111/j.1399-0039.1993.tb02007.xen_US
dc.identifier.sourceTissue Antigensen_US
dc.identifier.citedreferenceTodd RF III, Roach JA, Arnaout MA. The modulated expression of Mo5, a human myelomonocytic plasma membrane antigen. Blood 1985 : 65 : 964 – 73.en_US
dc.identifier.citedreferenceSundstrom C, Nilsson K. Establishment and characterization of a human histocytic lymphoma cell line (U-937). Int J Cancer 1976 : 17 : 565 – 77.en_US
dc.identifier.citedreferenceTsuchiya S, Kobayashi Y, Goto Y, et al. Induction of maturation in cultured human monocytic leukemia cells by a phorbol diester. Cancer Res 1982 : 42 : 1530 – 6.en_US
dc.identifier.citedreferenceCollins SJ, Gallo RC, Gallagher RE. Continous growth and differentiation of human myeloid leukemic cells in suspension culture. Nature 1977 : 270 : 347 – 9.en_US
dc.identifier.citedreferenceKoeffler HP, Golde DW. Acute myelogenous leukemia: A human cell line responsive to colony stimulating activity. Science 1978 : 200 : 1153 – 4.en_US
dc.identifier.citedreferenceFoon K, Todd RF III. Immunologic Classification of Leukemia and Lymphoma. Blood 1986 : 68 : 1 – 31.en_US
dc.identifier.citedreferenceHarlow E, Lane D. Antibody purification on Protein A columns. In : Antibodies - A Laboratory Manual. Cold Spring Harbor, 1988 : 310.en_US
dc.identifier.citedreferenceSchneider C, Newman RA, Sutherland DR, Asser U, Greaves MF. A one-step purification of membrane proteins using a high efficiency immunomatrix. J Biol Chem 1982 : 257 : 10766 – 9.en_US
dc.identifier.citedreferenceDana N, Styrt B, Griffin JD, Todd RF III, Klempner MS, Arnaout MA. Two functional domains in the phagocyte membrane glycoprotein Mol identified with monoclonal antibodies. J Immunol 1986 : 137 : 3259 – 63.en_US
dc.identifier.citedreferenceBiondi A, Rossing TH, Bennett J, Todd RF III. Surface membrane heterogeneity among mononuclear phagocytes. J Immunol 1984 : 132 : 1237 – 43.en_US
dc.identifier.citedreferenceRemold-O'Donnell E. Regulation of synthesis of macrophage adhesion molecule, a heterodimeric membrane glycoprotein. J Immunol 1988 : 140 : 1244 – 9.en_US
dc.identifier.citedreferenceLaemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970 : 227 : 680 – 5.en_US
dc.identifier.citedreferenceMorrison M. Lactoperoxidase-catalyzed iodination as a tool for investigation of proteins. Meth Enz 1980 : 70 : 214 – 20.en_US
dc.identifier.citedreferenceBadwey JA, Curnutte JT, Robinson JM, Berde CB, Karnovsky MJ, Karnovsky ML. Effects of free fatty acids on release of superoxide and on change of shape by human neutrophils. J Biol Chem 1984 : 259 : 7870 – 7.en_US
dc.identifier.citedreferenceArnaout MA, Spits H, Terhorst C, Pitt J, Todd RF III. Deficiency of leukocyte surface glycoprotein (LFA-1) in two patients with Mol deficiency. Effects of cell activation on Mol/LFA-1 surface expression in normal and deficient leukocytes. J Clin Invest 1984 : 74 : 1291 – 300.en_US
dc.identifier.citedreferenceGahmberg CG, Andersson LC. Identification and characterization of normal and malignant human blood leukocytes by surface glycoprotein patterns. Ann NY Acad Sci 1978 : 312 : 240 – 55.en_US
dc.identifier.citedreferenceMizukami IF, Vinjamuri SD, Trochelman RD, Todd RF III. A structural characterization of the Mo3 activation antigen expressed on the plasma membrane of human mononuclear phagocytes. J Immunol 1990 : 144 : 1841 – 8.en_US
dc.identifier.citedreferenceTarentino AL, Gomez CM, Plummer TH. Deglycosylation of asparagine-linked glycans by peptide: N-glycosidase F. Biochem 1985 : 24 : 4665 – 71.en_US
dc.identifier.citedreferenceKornfeld R, Kornfeld S. Assembly of asparagine-linked oligosaccharides. Annu Rev Biochem 1985 : 54 : 631 – 64.en_US
dc.identifier.citedreferenceMizukami IF, Vinjamuri SD, Perini F, Liu DY, Todd RF III. Purification, biochemical composition, and biosynthesis of the Mo3 activation antigen expressed on the plasma membrane of human mononuclear phagocytes. J Immunol 1991 : 147 : 1331 – 7.en_US
dc.identifier.citedreferenceRosse WF. Phosphatidylinositol-linked proteins and paroxysmal nocturnal hemoglobinuria. Blood 1990 : 75 : 1595 – 601.en_US
dc.identifier.citedreferenceJack RM, Fearon DT. Selective synthesis of mRNA and proteins by human peripheral blood neutrophils. J Immunol 1988 : 140 : 4286 – 93.en_US
dc.identifier.citedreferenceTiku K, Tiku ML, Skosey JL. Interleukin 1 production by human polymorphonuclear neutrophils. J Immunol 1986 : 136 : 3677 – 85.en_US
dc.identifier.citedreferenceCicco NA, Lindemann A, Content J, et al. Inducible production of interleukin-6 by human polymorphonuclear neutrophils: Role of GM-CSF and TNFΑ. Blood 1990 : 75 : 2049 – 52.en_US
dc.identifier.citedreferenceBazzoni F, Cassatella MA, Rossi F, Ceska M, Dewald B, Baggiolini M. Phagocytosing neutrophils produce and release high amounts of the neutrophilactivating peptide 1/IL-8. J Exp Med 1991 : 173 : 771 – 4.en_US
dc.identifier.citedreferenceLindemann A, Riedel D, Oster W, Ziegler-Heitbrock HW, Mertelsmann R, Herrmann F. Granulocyte-macrophage colony-stimulating factor induces cytokine secretion by human polymorphonuclear leukocytes. J Clin Invest 1989 : 83 : 1308 – 12.en_US
dc.identifier.citedreferenceShirafuji N, Matsuda S, Ogura H, et al. Granulocyte colony-stimulating factor stimulates human mature neutrophilic granulocytes to produce IFNΑ. Blood 1990 : 75 : 17 – 9.en_US
dc.identifier.citedreferenceKreis C, La Fleur M, Menard C, Paquin R, Beaulieu AD. Thrombospondin and fibronectin are synthesized by neutrophils in human inflammatory joint disease and in a rabbit model of in vivo neutrophil activation. J Immunol 1989 : 143 : 1961 – 8.en_US
dc.identifier.citedreferenceDuBois RM, Bernaudin JF, Paakko P, et al. Human neutrophils express the alpha 1-antitrypsin gene and produce alpha 1-antitrypsin. Blood 1991 : 77 : 2724 – 30.en_US
dc.identifier.citedreferenceKnapp W, Bettelheim P, Gadd S, et al. Leukocyte Typing IV. White Cell Differentiation Antigens. 1989. Oxford : Oxford University Press, 1989.en_US
dc.identifier.citedreferenceKuijpers TW, Tool ATJ, van der Schoot CE, et al. Membrane surface antigen expression on neutrophils: a reappraisal of the use of surface markers for neutrophil activation. Blood 1991 : 78 : 1105 – 11.en_US
dc.identifier.citedreferenceOld LJ, Stockert E, Boyse EA, Kim JH. Antigenic modulation. Loss of TL antigen from cells exposed to TL antibody. Study of the phenomenon in vitro. J Exp Med 1968 : 127 : 523 – 39.en_US
dc.identifier.citedreferenceHuizinga TWJ, van der Schoot CE, Jost C, et al. The PI-linked receptor FcRIII is released on stimulation of neutrophils. Nature 1988 : 333 : 667 – 9.en_US
dc.identifier.citedreferenceArnaout MA, Tood RF III, Dana N, Melamed J, Schlossman SF, Colten HR. Inhibition of phagocytosis of complement C3 or Immunoglobulin G-coated particles and of C3bi binding by monoclonal antibodies to a monocytegranulocyte membrane glycoprotein (Mo1). J Clin Invest 1983 : 72 : 171 – 9.en_US
dc.identifier.citedreferenceArnaout MA, Hakim RM, Todd RF III, Dana N, Colten HR. Increased expression of an adhesion-promoting surface glycoprotein in the granulocytopenia of hemodialysis. N Engl J Med 1985 : 312 : 457 – 62.en_US
dc.identifier.citedreferenceIsmail G, Morganroth ML, Todd RF III, Boxer LA. Prevention of pulmonary injury in isolated perfused rat lungs by activated human neutrophils preincubated with anti-Mo1 monoclonal antibody. Blood 1987 : 69 : 1167 – 74.en_US
dc.identifier.citedreferenceCassatella MC, Anegon I, Cuturi MC, Griskey P, Trinchieri G, Perussia B. FcΓR (CD 16) interaction with ligand induces Ca 2+ mobilization and phosphoinositide turnover in human natural killer cells. J Exp Med 1989 : 169 : 549 – 67.en_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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