A Monoclonal Antibody to the Surface Membrane of Human Platelets Which Inhibits Ristocetin- and Collagen-induced Platelet Aggregation Reacts with H1 Histones of Cell Nuclei

Overview

Journal Clin Exp Immunol

Publisher Oxford University Press

Specialty Allergy & Immunology

Date 1987 Aug 1

PMID 3308229

Citations 1

Authors

L Cosgrove

F Alderuccio

B H Toh

J Pedersen

A Holliday

I McKenzie

Affiliations

Soon will be listed here.

Abstract

A murine monoclonal antibody HuPIA3, produced by immunization with human platelet membranes, reacted by radioimmunoassay with platelets, and inhibited ristocetin- and collagen-induced platelet aggregation and release of 14C-serotonin. The antibody also inhibited ristocetin-induced aggregation of washed, formaldehyde-fixed platelets by von Willebrand factor. On cultures of human and rodent fibroblasts, and on frozen sections of rabbit liver and rat kidney, the antibody gave a diffuse, homogenous immunofluorescence staining of cell nuclei which could be abolished by treatment with 0.1 M HC1 or 2 M NaCl and restored by reconstitution with histones, suggesting a reaction with nuclear histones. Absorption of the antibody with histones abolished nuclear staining and abrogated the inhibitory effect of the antibody on ristocetin- and collagen-induced platelet aggregation and 14C-serotonin release. Conversely, absorption with platelets removed antibody reactivity for platelets and for cell nuclei. In addition, the antibody reacted with H1 histones by radioimmunoassay, and immunoblotting studies showed that the antibody reacted with a protein of 199,000 daltons on platelets and with H1 histones (31,000 dalton and 32,000 dalton). These observations suggest that the antibody recognizes epitopes found on surface molecules of platelets as well as on H1 histones of cell nuclei.

Citing Articles

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Hackstadt T, Baehr W, Ying Y Proc Natl Acad Sci U S A. 1991; 88(9):3937-41.

PMID: 2023942 PMC: 51568. DOI: 10.1073/pnas.88.9.3937.

References

Laemmli U . Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970; 227(5259):680-5. DOI: 10.1038/227680a0. View

Warley A, Cook G . The isolation and characterization of plasma membranes from normal and leukaemic cells of mice. Biochim Biophys Acta. 1973; 323(1):55-68. DOI: 10.1016/0005-2736(73)90431-8. View

Kaplan K, Nachman R . The interaction of platelets and concanavalin A. Thromb Res. 1975; 7(6):847-59. DOI: 10.1016/0049-3848(75)90088-2. View

Tan E, Robinson J, Robitaille P . Studies on antibodies to histones by immunofluorescence. Scand J Immunol. 1976; 5(6-7):811-8. DOI: 10.1111/j.1365-3083.1976.tb03030.x. View

Kao K, Pizzo S, McKee P . Demonstration and characterization of specific binding sites for factor VIII/von Willebrand factor on human platelets. J Clin Invest. 1979; 63(4):656-64. PMC: 372000. DOI: 10.1172/JCI109348. View

Towbin H, Staehelin T, Gordon J . Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci U S A. 1979; 76(9):4350-4. PMC: 411572. DOI: 10.1073/pnas.76.9.4350. View

Agnello V, Arbetter A, Ibanez de Kasep G, Powell R, Tan E, Joslin F . Evidence for a subset of rheumatoid factors that cross-react with DNA-histone and have a distinct cross-idiotype. J Exp Med. 1980; 151(6):1514-27. PMC: 2185879. DOI: 10.1084/jem.151.6.1514. View

Adolph K . Organization of chromosomes in HeLa cells: isolation of histone-depleted nuclei and nuclear scaffolds. J Cell Sci. 1980; 42:291-304. DOI: 10.1242/jcs.42.1.291. View

McEver R, Baenziger N, MAJERUS P . Isolation and quantitation of the platelet membrane glycoprotein deficient in thrombasthenia using a monoclonal hybridoma antibody. J Clin Invest. 1980; 66(6):1311-8. PMC: 371616. DOI: 10.1172/JCI109983. View

10.

Rekvig O, Hannestad K . Human autoantibodies that react with both cell nuclei and plasma membranes display specificity for the octamer of histones H2A, H2B, H3, and H4 in high salt. J Exp Med. 1980; 152(6):1720-33. PMC: 2186031. DOI: 10.1084/jem.152.6.1720. View

11.

Hogarth P, Edwards J, McKenzie I, Goding J, Liew F . Monoclonal antibodies to the murine Ly-2.1 cell surface antigen. Immunology. 1982; 46(1):135-44. PMC: 1555340. View

12.

Coller B, Peerschke E, Scudder L, Sullivan C . Studies with a murine monoclonal antibody that abolishes ristocetin-induced binding of von Willebrand factor to platelets: additional evidence in support of GPIb as a platelet receptor for von Willebrand factor. Blood. 1983; 61(1):99-110. View

13.

Kenneally D, Lolait S, Toh B . Fibroblast monolayers as substrates for the demonstration and analysis of anti-nuclear autoantibodies. J Clin Lab Immunol. 1983; 10(1):47-51. View

14.

Thurlow P, Barlow B, CONNELLAN J, McKenzie I . Detection of glycoprotein IIb and IIIa by monoclonal antibodies. Br J Haematol. 1983; 55(1):123-34. DOI: 10.1111/j.1365-2141.1983.tb01230.x. View

15.

Hardin J, Thomas J . Antibodies to histones in systemic lupus erythematosus: localization of prominent autoantigens on histones H1 and H2B. Proc Natl Acad Sci U S A. 1983; 80(24):7410-4. PMC: 389960. DOI: 10.1073/pnas.80.24.7410. View

16.

Andre-Schwartz J, Datta S, Shoenfeld Y, Isenberg D, Stollar B, Schwartz R . Binding of cytoskeletal proteins by monoclonal anti-DNA lupus autoantibodies. Clin Immunol Immunopathol. 1984; 31(2):261-71. DOI: 10.1016/0090-1229(84)90246-0. View

17.

Rubin R, Balderas R, Tan E, Dixon F, Theofilopoulos A . Multiple autoantigen binding capabilities of mouse monoclonal antibodies selected for rheumatoid factor activity. J Exp Med. 1984; 159(5):1429-40. PMC: 2187302. DOI: 10.1084/jem.159.5.1429. View

18.

Chiang T, Kang A, Dale J, Beachey E . Immunochemical studies of the purified human platelet receptor for the alpha 1(I)-chain of chick skin collagen. J Immunol. 1984; 133(2):872-6. View

19.

Krippner H, Springer B, Merle S, Pirlet K . Antibodies to histones of the IgG and IgM class in systemic lupus erythematosus. Clin Exp Immunol. 1984; 58(1):49-56. PMC: 1576959. View

20.

Jacob L, Lety M, Louvard D, Bach J . Binding of a monoclonal anti-DNA autoantibody to identical protein(s) present at the surface of several human cell types involved in lupus pathogenesis. J Clin Invest. 1985; 75(1):315-7. PMC: 423443. DOI: 10.1172/JCI111692. View