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Surface Plasmon Resonance Sensing on Naturally Derived Membranes: A Remyelination-Promoting Human Antibody Binds Myelin with Extraordinary Affinity.
Vala, Milan; Jordan, Luke R; Warrington, Arthur E; Maher, L James; Rodriguez, Moses; Wittenberg, Nathan J; Oh, Sang-Hyun.
Afiliación
  • Vala M; Department of Electrical and Computer Engineering , University of Minnesota , Minneapolis , Minnesota 55455 , United States.
  • Jordan LR; Department of Electrical and Computer Engineering , University of Minnesota , Minneapolis , Minnesota 55455 , United States.
  • Warrington AE; Department of Chemistry, Lehigh University , Bethlehem , Pennsylvania 18015 , United States.
  • Maher LJ; Departments of Neurology and Immunology , Mayo Clinic , Rochester , Minnesota 55905 , United States.
  • Rodriguez M; Department of Biochemistry and Molecular Biology , Mayo Clinic , Rochester , Minnesota 55905 , United States.
  • Wittenberg NJ; Departments of Neurology and Immunology , Mayo Clinic , Rochester , Minnesota 55905 , United States.
  • Oh SH; Department of Electrical and Computer Engineering , University of Minnesota , Minneapolis , Minnesota 55455 , United States.
Anal Chem ; 90(21): 12567-12573, 2018 11 06.
Article en En | MEDLINE | ID: mdl-30231202
rHIgM22 is a recombinant human monoclonal IgM designed to promote remyelination, and it is currently in Phase I clinical trials in patients with multiple sclerosis (MS). In animal models of demyelination, a single low dose of rHIgM22 stimulates oligodendrocyte maturation, induces remyelination, preserves axons, and slows the decline of locomotor deficits. Natural autoantibodies like rHIgM22 typically bind to multiple antigens with weak affinity. rHIgM22 binds to oligodendrocytes and myelin. Because the antigens for rHIgM22 is prevalent within and exclusive to central nervous system (CNS) myelin, we used CNS myelin particles in combination with surface plasmon resonance to determine the kinetic and affinity constants for the interaction of rHIgM22 to myelin. We found that both the serum and recombinant forms of the antibody bind to myelin with very small dissociation constants in the 100 pM range, which is highly unusual for natural autoantibodies. The extraordinary affinity between rHIgM22 and myelin may explain why such a low effective dose can stimulate CNS repair in animal models of demyelination and underlie the accumulation of rHIgM22 in the CSF in treated MS patients by targeting myelin.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Inmunoglobulina M / Anticuerpos Monoclonales / Vaina de Mielina Límite: Animals / Humans Idioma: En Revista: Anal Chem Año: 2018 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos
Texto completo
Añadir a Mi BVS
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Inmunoglobulina M / Anticuerpos Monoclonales / Vaina de Mielina Límite: Animals / Humans Idioma: En Revista: Anal Chem Año: 2018 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos