TY - JOUR
T1 - Characterization of autoantibodies to vasoactive intestinal peptide in asthma
AU - Paul, Sudhir
AU - Said, Sami I.
AU - Thompson, Austin B.
AU - Volle, Deanna J.
AU - Agrawal, Devendra K.
AU - Foda, Hussein
AU - de la Rocha, Santiago
N1 - Funding Information:
The neuropeptide vasoactive intestinal peptide (VIP) is the likely physiological mediator of non- Address for correspondence: Dr. Sudhir Paul, Department of Pharmacology, University of Nebraska Medical Center, 42nd and Dewey Avenue, Omaha, NE 68105, U.S.A. Supported by NHBLI grants 35506 and 40348.
PY - 1989/7
Y1 - 1989/7
N2 - Vasoactive intestinal peptide (VIP) is a potent relaxant of the airway smooth muscle. In this study, VIP-binding autoantibodies were observed in the plasma of 18% asthma patients and 16% healthy subjects. Immunoprecipitation studies and chromatography on DEAE-cellulose and immobilized protein G indicated that the plasma VIP-binding activity was largely due to IgG antibodies. Saturation analysis of VIP binding by the plasma suggested the presence of one or two classes of autoantibodies, distinguished by their apparent equilibrium affinity constants (Ka). The autoantibodies from asthma patients exhibited a larger VIP-binding affinity compared to those from healthy subjects (Ka 7.8 × 109 M-1 and 0.13 × 109 M-1, respectively; P < 0.005). The antibodies were specific for VIP, judged by their poor reaction with peptides bearing partial sequence homology with VIP (peptide histidine isoleucine, growth hormone releasing factor and secretin). IgG prepared from the plasma of an antibody-positive asthma patient inhibited the saturable binding of 125I-VIP by receptors in guinea pig lung membranes (by 39-59%; P < 0.001). These observations are consistent with a role for the VIP autoantibodies in the airway hyperresponsiveness of asthma.
AB - Vasoactive intestinal peptide (VIP) is a potent relaxant of the airway smooth muscle. In this study, VIP-binding autoantibodies were observed in the plasma of 18% asthma patients and 16% healthy subjects. Immunoprecipitation studies and chromatography on DEAE-cellulose and immobilized protein G indicated that the plasma VIP-binding activity was largely due to IgG antibodies. Saturation analysis of VIP binding by the plasma suggested the presence of one or two classes of autoantibodies, distinguished by their apparent equilibrium affinity constants (Ka). The autoantibodies from asthma patients exhibited a larger VIP-binding affinity compared to those from healthy subjects (Ka 7.8 × 109 M-1 and 0.13 × 109 M-1, respectively; P < 0.005). The antibodies were specific for VIP, judged by their poor reaction with peptides bearing partial sequence homology with VIP (peptide histidine isoleucine, growth hormone releasing factor and secretin). IgG prepared from the plasma of an antibody-positive asthma patient inhibited the saturable binding of 125I-VIP by receptors in guinea pig lung membranes (by 39-59%; P < 0.001). These observations are consistent with a role for the VIP autoantibodies in the airway hyperresponsiveness of asthma.
KW - Antibody affinity
KW - Asthma
KW - Vasoactive intestinal peptide autoantobody
KW - Vasoactive intestinal peptide receptor
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U2 - 10.1016/0165-5728(89)90032-5
DO - 10.1016/0165-5728(89)90032-5
M3 - Article
C2 - 2542371
AN - SCOPUS:0024392858
SN - 0165-5728
VL - 23
SP - 133
EP - 142
JO - Journal of Neuroimmunology
JF - Journal of Neuroimmunology
IS - 2
ER -