Characterization and Specificity of a High Titre Polyclonal Goat Anti-murine IL-1 Antibody

Overview

Journal Immunology

Specialty Allergy & Immunology

Date 1986 Dec 1

PMID 3492439

Citations 2

Authors

M E Scheetz

D G Carlson

J L Bobbitt

L D Butler

S H Zuckerman

Affiliations

Soon will be listed here.

Abstract

The immunization of goats with an HPLC-purified IL-1 preparation derived from the supernatants of LPS-induced P388D1 cultures has resulted in the derivation of a high titre antiserum specific for murine IL-1. This antiserum exhibits a 50% inhibition of an IL-1-dependent thymocyte costimulation assay at a reciprocal dilution of 30,000 and antibody activity is still detected at 100,000-fold dilution. The goat anti-murine IL-1 serum is specific for murine IL-1 synthesized by several murine macrophage cell lines and does not neutralize human, rabbit or porcine (catabolin) IL-1. The antiserum also inhibits antigen-induced proliferation of the D10.G4 helper T-cell line. In addition to the reaction against IL-1, the antiserum also detects three additional peptides with molecular weights between 20,000 and 30,000.

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References

Koren H, Handwerger B, Wunderlich J . Identification of macrophage-like characteristics in a cultured murine tumor line. J Immunol. 1975; 114(2 pt 2):894-7. View

Kock A, Danner M, Stadler B, Luger T . Characterization of a monoclonal antibody directed against the biologically active site of human interleukin 1. J Exp Med. 1986; 163(2):463-8. PMC: 2188039. DOI: 10.1084/jem.163.2.463. View

Ralph P, Moore M, Nilsson K . Lysozyme synthesis by established human and murine histiocytic lymphoma cell lines. J Exp Med. 1976; 143(6):1528-33. PMC: 2190228. DOI: 10.1084/jem.143.6.1528. View

Dinarello C, Renfer L, Wolff S . Human leukocytic pyrogen: purification and development of a radioimmunoassay. Proc Natl Acad Sci U S A. 1977; 74(10):4624-7. PMC: 431999. DOI: 10.1073/pnas.74.10.4624. 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

Murphy P, Simon P, Willoughby W . Endogenous pyrogens made by rabbit peritoneal exudate cells are identical with lymphocyte-activating factors made by rabbit alveolar macrophages. J Immunol. 1980; 124(5):2498-501. View

Mizel S, Mizel D . Purification to apparent homogeneity of murine interleukin 1. J Immunol. 1981; 126(3):834-7. View

Lachman L, Page S, METZGAR R . Purification of human interleukin 1. J Supramol Struct. 1980; 13(4):457-66. DOI: 10.1002/jss.400130405. View

Sztein M, Vogel S, Sipe J, Murphy P, Mizel S, Oppenheim J . The role of macrophages in the acute-phase response: SAA inducer is closely related to lymphocyte activating factor and endogenous pyrogen. Cell Immunol. 1981; 63(1):164-76. DOI: 10.1016/0008-8749(81)90037-x. View

10.

Murphy P, Cebula T, Levin J, Windle B . Rabbit macrophages secrete two biochemically and immunologically distinct endogenous pyrogens. Infect Immun. 1981; 34(1):177-83. PMC: 350840. DOI: 10.1128/iai.34.1.177-183.1981. View

11.

Mizel S, Dukovich M, Rothstein J . Preparation of goat antibodies against interleukin 1: use of an immunoadsorbent to purify interleukin 1. J Immunol. 1983; 131(4):1834-7. View

12.

Dinarello C . Interleukin-1. Rev Infect Dis. 1984; 6(1):51-95. DOI: 10.1093/clinids/6.1.51. View

13.

Kimball E, Pickeral S, Oppenheim J, Rossio J . Interleukin 1 activity in normal human urine. J Immunol. 1984; 133(1):256-60. View

14.

Dinarello C, CLOWES Jr G, Gordon A, SARAVIS C, Wolff S . Cleavage of human interleukin 1: isolation of a peptide fragment from plasma of febrile humans and activated monocytes. J Immunol. 1984; 133(3):1332-8. View

15.

Kaye J, Gillis S, Mizel S, Shevach E, Malek T, Dinarello C . Growth of a cloned helper T cell line induced by a monoclonal antibody specific for the antigen receptor: interleukin 1 is required for the expression of receptors for interleukin 2. J Immunol. 1984; 133(3):1339-45. View

16.

Giri J, Lomedico P, Mizel S . Studies on the synthesis and secretion of interleukin 1. I. A 33,000 molecular weight precursor for interleukin 1. J Immunol. 1985; 134(1):343-9. View

17.

Lomedico P, Gubler U, Hellmann C, Dukovich M, Giri J, Pan Y . Cloning and expression of murine interleukin-1 cDNA in Escherichia coli. Nature. 1984; 312(5993):458-62. DOI: 10.1038/312458a0. View

18.

Auron P, Webb A, Rosenwasser L, Mucci S, Rich A, Wolff S . Nucleotide sequence of human monocyte interleukin 1 precursor cDNA. Proc Natl Acad Sci U S A. 1984; 81(24):7907-11. PMC: 392262. DOI: 10.1073/pnas.81.24.7907. View

19.

March C, Mosley B, Larsen A, Cerretti D, Braedt G, Price V . Cloning, sequence and expression of two distinct human interleukin-1 complementary DNAs. Nature. 1985; 315(6021):641-7. DOI: 10.1038/315641a0. View

20.

Cameron P, Limjuco G, Rodkey J, Bennett C, Schmidt J . Amino acid sequence analysis of human interleukin 1 (IL-1). Evidence for biochemically distinct forms of IL-1. J Exp Med. 1985; 162(3):790-801. PMC: 2187801. DOI: 10.1084/jem.162.3.790. View