Development and characterization of monoclonal antibodies specific for amylin

Hybridoma. 1996 Oct;15(5):379-86. doi: 10.1089/hyb.1996.15.379.

Abstract

Highly selective monoclonal antibodies to the peptide hormone human amylin have been produced and characterized. These antibodies are produced by hybridomas resulting from the fusions of BALB/c-derived myelomas and splenocytes from either inbred or outbred mouse strains. Certain of these antibodies recognize epitopes at the amino-terminus or the amidated carboxy-terminus, as well as conformational epitopes within the central region of the 37 amino acid peptide. Several of these antibodies show less than 0.1% cross-reactivity with related peptide hormones such as calcitonin and calcitonin gene-related peptide (CGRP) and have apparent affinities in the low nanomolar range. Antibody pairs were selected for use in two-site assays for the direct measurement of endogenous amylin and the synthetic human amylin analogue, pramlintide (25, 28, 29 tripro-human amylin), which is presently under clinical investigation for improving glucose control in patients with both Type I and Type II diabetes treated with insulin.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Amyloid / immunology*
  • Animals
  • Antibodies, Monoclonal / biosynthesis
  • Antibodies, Monoclonal / chemistry*
  • Antibody Specificity*
  • Binding, Competitive
  • Cell Fusion / immunology
  • Cross Reactions
  • Epitope Mapping
  • Humans
  • Immunization
  • Islet Amyloid Polypeptide
  • Mice
  • Mice, Inbred A
  • Mice, Inbred BALB C
  • Molecular Sequence Data
  • Radioimmunoassay

Substances

  • Amyloid
  • Antibodies, Monoclonal
  • Islet Amyloid Polypeptide