Is the Catalytic Activity of Bence Jones Proteins an Autoimmune Effector Mechanism in Multiple Myeloma?
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book series (CONTIM)
On Friday, October 30, 1845, W. MacIntire, physician to the Metropolitan Convalescent Institution and to the Western General Dispensary, St. Marylebone, was called to see a patient who had been treated by T. Watson for several months (1,2). Since the patient had a history of edema, Maclntire examined the urine and noted the peculiar physical properties of the urinary protein (precipitation with heating at 40–60°C, disappearance with boiling, and reappearance with cooling). He wrote: “I was at first inclined to think that some mistake had occurred, but on repeated trials with other specimens, and closely watching their course, the results were always found to be the same” (2). Watson had evidently not examined the urine when the patient had been under his care, but was present when Maclntire performed urinalysis. In those days, it was customary for the specialist services to be provided by practicing physicians and surgeons. Urine specimens were sent to Henry Bence Jones, physician to St. George’s Hospital and professor of forensic medicine of the Medical College associated with the Hospital. Jones was then 31 yr old, but had already established a reputation as a chemical pathologist. He confirmed the Maclntire results and examined the protein in some detail. The patient died six weeks later, and an autopsy was performed by Shaw, surgeon to the Middlesex Hospital, in the presence of Watson, Jones, Ridge, and Maclntire, none of whom thought that the peculiar urinary protein was related to the disease, mollities ossium, later called multiple myeloma (2).
KeywordsMultiple Myeloma Light Chain Free Light Chain Catalytic Antibody Urinary Trypsin Inhibitor
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Clamp, J. R. (1967) Some aspects of the first recorded case of multiple myeloma. Lancet
, 1354–1356.PubMedCrossRefGoogle Scholar
MacIntire, W. (1850) Case of mollities and fragilitas ossium, accompanied with urine strongly charged with animal matter. Med. Chir. Trans.
, 211–232.Google Scholar
Jones, B. H. (1847) Papers on chemical pathology; prefaced by the Gulstonian Lectures, read at the Royal College of Physicians, 1846. Lancet
, 88–92.CrossRefGoogle Scholar
Peeters, H. (chairman) and 21 other participants (1961) Round table conference: New methods and recent results in protide chemistry. Protides Biol. Fluids
, 359–370.Google Scholar
Migita, S. (1965) The story of Bence Jones protein (in Japanese). Kyudai Iho
, 205–209.Google Scholar
Edelman, G. M. and Gaily, J. A. (1962) The nature of Bence Jones proteins: chemical similarities to polypeptide chains of myeloma globulins and normal γ-globu-lins. J. Exp. Med.
, 207–227.PubMedCrossRefGoogle Scholar
Erhan, S., and Greller, L. D. (1974) Do immunoglobulins have proteolytic activity? Nature
, 353–355.PubMedCrossRefGoogle Scholar
Mei, S., Mody, R., Ekulund, S. H., and Paul, S. (1991) Vasoactive intestinal peptide hydrolysis by antibody light chains. J. Biol. Chem.
, 15571–15574.PubMedGoogle Scholar
Gao, Q.-S., Sun, M., Tyutyukova, S., Webster, D., Rees, A., Tranibtabim A., et al. (1994) Molecular cloning of a proteolytic antibody light chain. J. Biol. Chem.
, 32389–32393.PubMedGoogle Scholar
Sun, M., Gao, Q.-S., Li, L., and Paul, S. (1994) Proteolytic activity of an antibody light chain. J. Immunol.
, 5121–5126.PubMedGoogle Scholar
Paul, S., Li, L., Kalga, R., Wilkins-Stevens, P., Stevens, F. J., and Solomon, A. (1995) Natural catalytic antibodies: peptide-hydrolyzing activities of Bence Jones proteins and VL fragment. J. Biol. Chem.
, 15257–15262.PubMedCrossRefGoogle Scholar
Matsuura, K., Yamamoto, K., and Sinohara, H. (1994) Amidase activity of human Bence Jones proteins. Biochem. Biophys. Res. Commun.
, 57–62.PubMedCrossRefGoogle Scholar
Matsuura, K. and Sinohara, H. (1996) Catalytic cleavage of vasopressin by human Bence Jones proteins at the arginylglycinamide bond. Biol. Chem.
, 587–589.PubMedGoogle Scholar
Selby, P. and Gore, M. (1995) Myeloma and other plasma cell malignancies, in Oxford Textbook of Oncology
(Peckham, M., Pinego, H., and Veronesi, U., eds.) vol. 1, pp. 1852–1878.Google Scholar
Buxbaum, J. (1992) Mechanisms of disease: Monoclonal immunoglobulin deposition. Hematol. Oncol. Clin. N. Am.
, 323–346.Google Scholar
Pascali, E. and Pezzoli, A. (1988) The clinical spectrum of pure Bence Jones pro-teinuria. Cancer
, 2408–2415.PubMedCrossRefGoogle Scholar
Lerner, R. A., Benkovic, S. J., and Schultz, P. G. (1991) At the crossroads of chemistry and immunology: catalytic antibodies. Science
, 659–667.PubMedCrossRefGoogle Scholar
Paul, S. (1996) Natural catalytic antibodies. Mol. Biotechnol.
, 197–207.PubMedCrossRefGoogle Scholar
Li, L., Paul, S., Tyutyukova, S., Kazatchkine, M., and Kaveri, S. (1995) Catalytic activity of anti-thyroglobulin antibodies. J. Immunol.
, 3328–3332.PubMedGoogle Scholar
Paul, S., Volle, D. J., Beach, C. M., Johnson, D. R., Powell, M. J., and Massey, R. J. (1989) Catalytic hydrolysis of vasoactive intestinal peptide by human auto-antibody. Science
, 1158–1162.PubMedCrossRefGoogle Scholar
Pauling, L. (1946) Molecular architecture and biological reactions. Chem. Eng. News
, 1375–1377.CrossRefGoogle Scholar
Shuster, A. M., Gololobov, G. V., Kvashuk, O. A., Bogomolova, A. E., Smirnov, I. V., and Gabibov, A.G. (1992) DNA hydrolyzing autoantibodies. Science
, 665–667.PubMedCrossRefGoogle Scholar
Yanase, K., Smith, R. M., Cizman, B., Foster, M. H., Peachey, L. D., Jarett, L., et al. (1994) A subgroup of murine monoclonal antideoxyribonucleic acid antibodies traverse the cytoplasm and enter the nucleus in a time-and temperature-dependent manner. Lab. Invest.
, 52–60.PubMedGoogle Scholar
Levinson, S. S. and Keren, D. F. (1994) Free light chains of immunoglobulins: clinical laboratory analysis. Clin. Chem.
, 1869–1878.PubMedGoogle Scholar
Ioannidis, R. A., Joshua, D. E., Warburton, P. T., Francis, S. E., Brown, R. D., Gibson, J., et al. (1989) Multiple myeloma: evidence that light chains play an immunoregulatory role in B-cell regulation. Hematol. Pathol.
, 169–175.PubMedGoogle Scholar
Maack, T., Johnson, V., Kau, S. T., Figueiredo, J., and Sigulem, D. (1979) Renal filtration, transport, and metabolism of low-molecular-weight proteins: a review. Kidney Int.
, 251–270.PubMedCrossRefGoogle Scholar
Carone, F. A., Peterson, D. R., Oparil, S., and Pullman, T. N. (1979) Renal tubular transport and catabolism of proteins and peptides. Kidney Int.
, 271–278.PubMedCrossRefGoogle Scholar
Solomon, A., Weiss, D. H., and Kattine, A. A. (1991) Nephrotoxic potential of Bence Jones proteins. N. Engl. J. Med.
, 1845–1851.PubMedCrossRefGoogle Scholar
Dammacco, F. and Waidenstrom, J. (1968) Serum and urine light chain levels in benign monoclonal gammopathies, multiple myeloma and Waidenstrom’s macro-globulinemia. Clin. Exp. Immunol.
, 911–921.PubMedGoogle Scholar
Nelson, M., Brown, R. D., Gibson, J., and Joshua, D. E. (1992) Measurement of free kappa and lambda chains in serum and the significance of their ratio in patients with multiple myeloma. Br. J. Haematol.
, 223–230.PubMedCrossRefGoogle Scholar
Sanders, P. W. (1994) Pathogenesis and treatment of myeloma kidney. J. Lab. Clin. Med.
, 484–488.PubMedGoogle Scholar
Kyle, R. A. and Gertz, M. A. (1995) Primary systemic amyloidosis: clinical and laboratory features in 474 cases. Semin. Hematol.
, 45–59.PubMedGoogle Scholar
Shirahama, T., Miura, K., Ju, S.-T., Kisilevsky, R., Grays, E., and Cohen, A. S. (1990) Amyloid enhancing factor-loaded macrophages in amyloid fibril formation. Lab. Invest.
, 61–68.PubMedGoogle Scholar
Preud’homme, J.-L., Aucouturier, P., Touchard, G., Striker, L., Khamlichi, A. A., Rocca, A., et al. (1994) Monoclonal immunoglobulin deposition disease (Randall type). Relationship with structural abnormalities of immunoglobulin chains. Kidney Int.
, 965–972.CrossRefGoogle Scholar
Huang, Z.-Q., Kirk, K. A., Connelly, K. G., and Sanders, P. W. (1993) Bence Jones proteins bind to a common peptide segment of Tamm-Horsfall glycoprotein to promote heterotypic aggregation. J. Clin. Invest.
, 2975–2983.PubMedCrossRefGoogle Scholar
De Fronzo, R. A., Cooke, C. R., Wright, J. R., and Humphrey, R. L. (1978) Renal function in patients with multiple myeloma. Medicine
, 151–166.Google Scholar
Yokota, N., Yamamoto, Y., Kitamura, K., Kuroki, N., Hisanaga, S., Fujimoto, S., et al. (1991) Renal tubular lesions induced by human Bence Jones protein in the rat: N-acetyl-b-D-glucosaminidase as a sensitive marker. J. Exp. Pathol.
, 255–262.Google Scholar
Fang, L. S. T. (1985) Light-chain nephropathy. Kidney Int.
, 582–592.PubMedCrossRefGoogle Scholar
Ollerenshaw, S., Jarvis, D., Woolcock, A., Sullivan, C., and Scheibner, T. (1989) Absence of immunoreactive vasoactive intestinal polypeptide in tissue from the lungs of patients with asthma. N. Engl. J. Med.
, 1244–1248.PubMedCrossRefGoogle Scholar
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