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Creating the Costliest Orphan: The Orphan Drug Act in the Development of Ceredase™

Published online by Cambridge University Press:  10 March 2009

Dana P. Goldman ,
Ann E. Clarke  and
Alan M. Garber
Dana P. Goldman
Affiliation:
Stanford University
Ann E. Clarke
Affiliation:
Stanford University
Alan M. Garber
Affiliation:
Palo Alto Department of Veterans Affairs Medical Center and Stanford University
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Abstract

The FDA recently approved Ceredase™, a new treatment for Gaucher's disease, under the provisions of the Orphan Drug Act. Ceredase™ is unusually expensive, but there are no satisfactory alternative therapies. It appears likely that Ceredase™would not have become available without the protection of the Orphan Drug Act, but its expense and the lack of information about its long-term effects on health raise questions about whether the ODA provides appropriate incentives to develop cost-effective technologies.

Type
Special Section: Orphan Technologies
Information
International Journal of Technology Assessment in Health Care , Volume 8 , Issue 4 , Fall 1992 , pp. 583 - 597
Copyright
Copyright © Cambridge University Press 1992

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References

REFERENCES

1.Aerts, J. M. F. G., Donker-Koopman, W. E., Murray, G. J., et al. A procedure for the rapid purification in high yields of human glucocerebrosidase using immunoaffinity chromatography with monoclonal antibodies. Analytic Biochemistry, 1986, 154, 655–63.CrossRefGoogle ScholarPubMed
2.Barranger, J. A., & Ginns, E. I. Glucosylceramide lipidosis: Gaucher disease. In Scriver, C. R., Beaudet, A. L., Sly, W. S., & Valle, D. (eds.), The metabolic basis of inherited disease, 6th ed.New York: McGraw-Hill, 1989, 1677–98.Google Scholar
3.Barton, N. W., Brady, R. O., Dambrosia, J. M., et al. Replacement therapy for inherited enzyme deficiency—Macrophage targeted glucocerebrosidase for Gaucher’s disease. New England Journal of Medicine, 1991, 324, 1464–70.CrossRefGoogle ScholarPubMed
4.Barton, N. W., Furbish, F. S., Murray, G. J., et al. Therapeutic response to intravenous infusions of glucocerebrosidase in a patient with Gaucher disease. Proceedings of the National Academy of Sciences U.S.A., 1990, 87, 1913–16.CrossRefGoogle Scholar
5.Belchelz, P. E., Crawley, J. C. W., Braidman, I. P., & Gregoriadis, G.Treatment of Gaucher’s disease with liposome-entrapped glucocerebrosidase: β-glucosidase. Lancet, 1977, ii, 116–17.CrossRefGoogle Scholar
6.Beutler, E.Gaucher disease. Blood Reviews, 1988, 2, 59–70.CrossRefGoogle ScholarPubMed
7.Beutler, E. Monocyte and macrophage disorders: Lipid storage disorders. In Williams, W. J., Beutler, E., Erslev, A. J., & Lichtman, M. A. (eds.), Hematology, 4th ed. New York: McGraw-Hill, 1990, 886–94.Google Scholar
8.Beutler, E.Gaucher’s disease. New England Journal of Medicine, 1991, 325, 1354–60.Google ScholarPubMed
9.Beutler, E., Dale, G. L., Guinto, E., & Kuhl, W.Enzyme replacement therapy in Gaucher’s disease: Preliminary clinical trial of a new enzyme preparation. Proceedings of the National Academy of Sciences U.S.A., 1977, 74, 4620–23.CrossRefGoogle ScholarPubMed
10.Beutler, E., Dale, G. L., & Kuhl, W. Replacement therapy in Gaucher disease. In Desnick, R. J. (ed.), Enzyme replacement therapy in genetic diseases: 2. New York: Alan R. Liss, Inc., 1980, 369–81.Google Scholar
11.Beutler, E., Kay, A., Saven, A., et al. Enzyme replacement therapy for Gaucher disease. Blood, 1991, 78, 1183–89.CrossRefGoogle ScholarPubMed
12.Brady, R. O., & Barranger, J. A. Glucosylceramide lipidosis: Gaucher's disease. In Stanbury, J. B., Wyngaarden, J. B., Fredrickson, D. S., Goldstein, J. L., & Brown, M. S. (eds.), The metabolic basis of inherited disease, 5th ed.New York: McGraw-Hill, 1983, 842–56.Google Scholar
13.Brady, R. O., Barranger, J.A., Furbish, F. S., et al. Prospects for enzyme replacement therapy in Gaucher disease. In Desnick, R. J., Gatt, S., & Grabowski, G. A. (eds.), Gaucher disease: A century of delineation and research. New York: Alan R. Liss, Inc., 1982, 669–80.Google Scholar
14.Brady, R. O., Barranger, J. A., Gal, A. E., et al. Status of enzyme replacement therapy for Gaucher disease. In Desnick, R. J. (ed.), Enzyme therapy in genetic diseases: 2. New York: Alan R. Liss, Inc., 1980, 361–68.Google Scholar
15.Brady, R. O., Pentchev, P. G., Gal, A. E., et al. Replacement therapy for inherited enzyme deficiency. Use of purified glucocerebrosidase in Gaucher's disease. New England Journal of Medicine, 1974, 291, 989–93.CrossRefGoogle ScholarPubMed
16.Choy, F. Y. M.Purification of human placental glucocerebrosidase using a two-step high performance hydrophobic and gel permeation column chromatography method. Analytic Biochemistry, 1986, 156, 515–20.CrossRefGoogle ScholarPubMed
17.Comanor, W. S.The political economy of the pharmaceutical industry. Journal of Economic Literature, 1986, 24, 1178–17.Google ScholarPubMed
18.Dale, G. L., & Beutler, E.Enzyme replacement therapy in Gaucher's disease: A rapid high yield method for purification of glucocerebrosidase. Proceedings of the National Academy of Sciences U.S.A., 1976, 73, 4672–74.CrossRefGoogle ScholarPubMed
19.Dale, G. L., Beutler, E., Fournier, P., et al. Large scale purification of glucocerebrosidase from human placentas. In Desnick, R J. (ed.), Enzyme therapy in genetic diseases. 2. New York: Alan R. Liss, Inc., 1980, 33–41.Google Scholar
20.Doebber, T. W., Wu, M. S., Bugianesi, R. L., et al. Enhanced macrophage uptake of synthetically glycosylated human placental glucocerebrosidase. Journal of Biological Chemistry 1982, 257, 2193–99.CrossRefGoogle Scholar
21.Erikson, E., Groth, G. C, Mansson, J. E., et al. Clinical and biochemical outcome of marrow transplantation for Gaucher disease of the Norrbottnian type. Ada Paediatrica Scandanavica, 1990, 79, 680–85.CrossRefGoogle ScholarPubMed
22.Eyal, N., Wilder, S., & Horowitz, M.Prevalent and rare mutations among Gaucher patients. Gene, 1990, 96, 277–83.CrossRefGoogle ScholarPubMed
23.Furbish, F. S., Blair, H. E., Shiloach, J., et al. Enzyme replacement therapy in Gaucher's disease: Large-scale purification of glucocerebrosidase suitable for human administration. Proceedings of the National Academy of Sciences U.S.A., 1977, 74, 3560–63.CrossRefGoogle ScholarPubMed
24.Furbish, F. S., Steer, C. J., Krett, N. L., & Barranger, J. A.Uptake and distribution of placental glucocerebrosidase in rat hepatic cells and effects of sequential deglycosylation. Biochimica et Biophysica Ada, 1981, 673, 425–34.CrossRefGoogle ScholarPubMed
25.Grabowski, G. A., & Dagan, A.Human lysosomal β-glucosidase: Purification by affinity chromatography. Analytic Biochemistry, 1984, 141, 267–79.CrossRefGoogle ScholarPubMed
26.Gregoriadis, G., Neerunjun, D., Meade, T. W., et al. Experiences after long-term treatment of a Type 1 Gaucher disease patient with liposome-entrapped glucocerebroside: β-glucosidase. In Desnick, R. J. (ed.), Enzyme therapy in genetic diseases. 2. New York: Alan R. Liss, Inc., 1980, 383–92.Google Scholar
27.Groth, C. G., Collste, H., Dreborg, S., et al. Attempt at enzyme replacement by organ transplantation; renal transplantation in Gaucher disease. Transplantation Proceedings, 1979, 11, 1218–19.Google ScholarPubMed
28.Groth, C. G., Dreborg, S., Oeckerman, P. A., et al. Splenic transplantation in a case of Gaucher's disease. Lancet, 1971, 1260–64.CrossRefGoogle Scholar
29.Hobbs, J. R., Shaw, P. J., Hugh-Jones, K., et al. Beneficial effect of pretransplant splencetomy on displacement bone marrow transplantation for Gaucher's syndrome. Lancet, 1987, ii, 1111-15.CrossRefGoogle Scholar
30.Kirkpatrick, D. V., Barrios, N. J., Shapira, E., & Humbert, J. R.Treatment of enzyme storage disease with matched and partially matched bone marrow transplantation: The Tulane marrow transplant group experience. Blood, 1990, 76(suppl. 1), AZ184.Google Scholar
31.Kleinschmidt, T., Christomanou, H., & Braunitzer, G.Complete amino-acid sequence and carbohydrate content of the naturally occurring glucosylceramide activator protein (Al activator) absent from a new human Gaucher disease variant. Biological Chemistry HoppeSeyler, 1987, 368, 1571–78.Google Scholar
32.Krivit, W. Lysosomal storage diseases. In Hoffman, R., Benz, E. J., Shattil, S. J., Furie, B., & Cohen, H. J. (eds.), Hematology. Basic principles and practice. New York: Churchill Livingstone, 1991, 617–20.Google Scholar
33.Krivit, W. Bone marrow transplantation as treatment for storage diseases: Background review and specific application to Gaucher's disease. Japanese Journal of Inborn Errors of Metabolism, in press.Google Scholar
34.Latham, T. E., Theophilus, B. D. M., Grabowski, G. A., & Smith, F. I.Heterogeneity of mutations in the acid-glucosidase gene of Gaucher disease patients. DNA and Cell Biology, 1991, 10, 15–21.CrossRefGoogle Scholar
35.Ludman, M. D., Lipton, J., Sadhev, I., et al. Gaucher disease: Bone marrow transplantation in rapidly progressive disease. American Journal of Human Genetics, 1988, (suppl.), A237.Google Scholar
36.Matoth, Y., Chazan, S., Cnaan, A., et al. Frequency of carriers of chronic (type 1) Gaucher disease in Ashkenazi Jews. American Journal of Medical Genetics, 1987, 27, 561–65.Google ScholarPubMed
37.Maugh, T. H., II. Study finds a second genetic link to illness. Los Angeles Times, 12 1991.Google Scholar
38.Murray, G. J., Howard, K. D., Richards, S. M., et al. Gaucher's disease: Lack of antibody response in 12 patients following repeated intravenous infusions of mannose terminal glucocerebrosidase. Journal of Immunological Methods, 1991, 137, 113–20.CrossRefGoogle ScholarPubMed
39.Murray, G. J., Youle, R. J., Gandy, S. E., et al. Purification of ß-glucocerebrosidase by preparative-scale high-performance liquid chromatography: The use of ethylene glycol containing buffers for chromatography of hydrophobic glycoprotein enzymes. Analytic Biochemistry, 1985, 147, 301–10.CrossRefGoogle Scholar
40.Pentchev, P. G., Brady, R. O., Hibbert, S. R., et al. Isolation and characterization of glucocerebrosidase from human placental tissue. Journal of Biological Chemistry, 1973, 248, 5256–61.CrossRefGoogle ScholarPubMed
41. Personal communication with Norman Barton, MD, PhD, Developmental and Metabolic Branch, National Institute of Neurological Disorders and Stroke, U.S. National Institutes of Health.Google Scholar
42. Personal communication with Ernest Beutler, MD, Department of Molecular and Experimental Medicine, Scripps Research Institute, La Jolla, CA.Google Scholar
43. Personal communication with Gregory Grabowski, MD, Department of Genetics and Molecular Biology, Mt. Sinai Medical Center, NY.Google Scholar
44. Personal communication with Glenn Molyneaux, MD, Assistant Medical Director, Blue Shield of California.Google Scholar
45. Personal communication with John Short, MD, Executive Secretary, U.S. Food and Drug Administration Endocrinologic and Metabolic Drugs Advisory Committee.Google Scholar
46. Personal communication with Alison Taunton-Rigby, PhD, Vice President Therapeutics, Genzyme Corporation.Google Scholar
47. Personal communication with Peter Vaccari, Office of Orphan Product Development, U.S. Food and Drug Administration.Google Scholar
48.Rappeport, J. M., Barranger, J. A., & Ginns, E. I.Bone marrow transplantation in Gaucher disease. Birth Defects, 1986, 22, 101–09.Google ScholarPubMed
49. Report by Barton, Norman MD, PhD in Proceedings from the Endocrinologic and Metabolic Advisory Committee, 10 22, 1990, 135–248.Google Scholar
50.Ringden, O., Groth, C. G., Aschan, J., et al. Bone marrow transplantation for metabolic disorders at Huddinge hospital. Transplantation Proceedings, 1990, 22, 198–202.Google ScholarPubMed
51.Russell, L. B.Some of the tough decisions required by a national health plan. Science, 1989, 240, 892–96.CrossRefGoogle Scholar
52.Securities and Exchange Commission. 10-K filings on behalf of Genzyme Corporation, 1987–1990.Google Scholar
53.Stahl, P. D., Rodman, J. S., Miller, M. J., & Schlesinger, P. H.Evidence for receptor-mediated binding of glycoproteins, glycoconjugates, and lysosomal glycosidases by alveolar macrophages. Proceedings of the National Academy of Sciences U.S.A. 1978, 75, 1399–403.CrossRefGoogle ScholarPubMed
54.Starer, F., Sargent, J. D., & Hobbs, J. R.Regression of the radiological changes of Gaucher's disease following bone marrow transplantation. British Journal of Radiology, 1987, 60, 1189–95.CrossRefGoogle ScholarPubMed
55.Strasberg, P. M., Lowden, J. A., & Mahuran, D.Purification of glucosylceramidase by affinity chromatography. Canadian Journal of Biochemistry, 1982, 60, 1025–31.CrossRefGoogle ScholarPubMed
56.Tsuji, S., Choudary, P. V., Martin, B. M., et al. A mutation in the human glucocerebrosidase gene in neuronopathic Gaucher's disease. New England Journal of Medicine, 1987, 316, 570–75.CrossRefGoogle ScholarPubMed
57.Tsuji, S., Martin, B. M., Barranger, J. A., et al. Genetic heterogeneity in type 1 Gaucher disease: Multiple genotypes in Ashkenazic and non-Ashkenazic individuals. Proceedings of the National Academy of Sciences, U.S.A., 1988, 85, 2349–52.CrossRefGoogle ScholarPubMed
58. United States Congressional Office of Technology Assessment Report on the Pharmaceutical Industry. In press.Google Scholar
59.Zimran, A., Gelbert, T., Westwood, B., et al. High frequency of the common Jewish mutation for Type 1 Gaucher disease among the Ashkenazi Jewish population. Blood, 1990, 76 (suppl.), A199.Google Scholar
60.Zimran, A., Gelbart, T., Westwood, B., et al. High frequency of the Gaucher disease mutation at nucleotide 1226 among Ashkenazi Jews. American Journal of Human Genetics, 1991, 49, 855-59.Google ScholarPubMed
61.Zimran, A., Gross, E., West, C., et al. Prediction of severity of Gaucher's disease by identification of mutations at DNA level. Lancet, 1989, ii, 349–52.CrossRefGoogle Scholar