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The Amino Acid Sequence of a Monoclonal γ3‐Heavy Chain from a Patient with Articular γ‐Heavy Chain Deposition Disease
Author(s) -
Danevad,
Sletten,
Gaarder,
Mellbye,
Husby
Publication year - 2000
Publication title -
scandinavian journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.934
H-Index - 88
eISSN - 1365-3083
pISSN - 0300-9475
DOI - 10.1046/j.1365-3083.2000.00730.x
Subject(s) - sequence (biology) , monoclonal antibody , peptide sequence , chemistry , antibody , heavy chain , monoclonal , immunoglobulin light chain , microbiology and biotechnology , biology , biochemistry , immunology , gene
Abnormal deposition of proteins, including monoclonal immunoglobulin γ‐heavy chains, may cause tissue damage and organ dysfunction. We here report the amino acid sequence of the free γ‐heavy chains present in serum and urine of the first reported case (patient G. L.) of synovial heavy chain deposition disease. The protein was heavily deleted and consisted of the hinge, in addition to the CH2 and CH3 domains, in a dimeric form, thus lacking its variable domain as well as the CH1 domain. The sequence was consistent with the γ3 subclass (γ3GL). Gm typing revealed the γ3 allotypes G3m(b0) and G3m(b1) in accordance with the residues Pro123, Phe128, Thr171 and Phe268 in γ3GL. Furthermore, the γ3GL molecule was glycosylated at Asn in position 129. Finally, the γ3GL protein was shown to contain a typical binding site for the first complement component, C1q, namely the residues Glu150, Lys152 and Lys154, with the potential of binding and activating complement, causing tissue damage following deposition.