Abstract

The studies described in this proposal are designed to further our understanding of the structure and function of antibody molecules, the relationship of immune complexes to human disease and the characterization of the major protein constituents of amyloid. The experiments dealing with antibody molecules and immunoglobulin variants produced by normal individuals as well as those with multiple myeloma and related plasma cell neoplasms are expected to shed insight into the genetic control of immunoglobulin structure and synthesis, to define the antibody combining sites and the expression of novel immunoglubulin genes. We wish to determine the factors involved in the production of rheumatoid factor cryoglobulins which result in an immune complex type of nephritis and vasculitis. Finally, we are attempting to classify from a clinical, immunohistologic and biochemical point of view a heterogeneous group of diseases characterized by the deposition of amyloid fibrils. Our approach is based on the theory that all types of amyloidosis occur in individuals who are genetically or otherwise defective in processing a soluble precursor which is a normal serum component.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of Arthritis, Diabetes, Digestive and Kidney Diseases (NIADDK)
Type
Research Project (R01)
Project #
5R01AM002594-28
Application #
3150693
Study Section
Allergy and Immunology Study Section (ALY)
Project Start
1978-09-01
Project End
1988-08-31
Budget Start
1985-09-01
Budget End
1986-08-31
Support Year
28
Fiscal Year
1985
Total Cost
Indirect Cost

  Institution

Name
New York University
Department
Type
Schools of Medicine
DUNS #
004514360
City
New York
State
NY
Country
United States
Zip Code
10012

  Publications

Picken, M M; Gallo, G R; Pruzanski, W et al. (1990) Biochemical characterization of amyloid derived from the variable region of the kappa light chain subgroup III. Arthritis Rheum 33:880-4
Picken, M M; Frangione, B; Barlogie, B et al. (1989) Light chain deposition disease derived from the kappa I light chain subgroup. Biochemical characterization. Am J Pathol 134:749-54
Castano, E M; Frangione, B (1988) Human amyloidosis, Alzheimer disease and related disorders. Lab Invest 58:122-32
Fong, S; Chen, P P; Crowley, J J et al. (1988) Idiotypic characteristics of rheumatoid factors. Scand J Rheumatol Suppl 75:58-65
Chen, P P; Fong, S; Goni, F et al. (1988) Cross-reacting idiotypes on cryoprecipitating rheumatoid factor. Springer Semin Immunopathol 10:35-55
Goni, F; Chuba, J; Buxbaum, J et al. (1988) A double monoclonal IgG1 kappa and IgG2 kappa in a single myeloma patient. Variation in clonal products and therapeutic responses. J Immunol 140:551-7
Mihaesco, E; Gendron, M C; Congy, N et al. (1988) Protein Rou. A human IgA hybrid. J Immunol 140:1236-8
Prelli, F; Pras, M; Frangione, B (1987) Degradation and deposition of amyloid AA fibrils are tissue specific. Biochemistry 26:8251-6
Picken, M M; Pelton, K; Frangione, B et al. (1987) Primary amyloidosis A. Immunohistochemical and biochemical characterization. Am J Pathol 129:536-42
Agnello, V; Goni, F; Barnes, J L et al. (1987) Human rheumatoid factor crossidiotypes. II. Primary structure-dependent crossreactive idiotype, PSL2-CRI, present on Wa monoclonal rheumatoid factors is present on Bla and other IgM kappa monoclonal autoantibodies. J Exp Med 165:263-7

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