Activity of MUC1 cancer antigen-binding plasma anti-α-galactoside antibody correlates inversely with size of autologous lipoprotein(a)
| Autor: | P.S. Appukuttan, Jessy John, Vasantha Kalaivani, Mandagini Geetha |
|---|---|
| Rok vydání: | 2019 |
| Předmět: |
0301 basic medicine
General Biochemistry Genetics and Molecular Biology Antibodies Serine Affinity maturation 03 medical and health sciences chemistry.chemical_compound Plasma 0302 clinical medicine Antigens Neoplasm Neoplasms Humans MUC1 Original Research biology Chemistry Mucin-1 Cancer susceptibility Galactosides Lipoprotein(a) Molecular biology Galactoside Cancer antigen 030104 developmental biology Immunoglobulin M 030220 oncology & carcinogenesis Immunoglobulin G biology.protein Antibody |
| Zdroj: | Exp Biol Med (Maywood) |
| ISSN: | 1535-3699 |
| Popis: | Variation in ligand-binding affinity of natural plasma anti-α-galactoside antibody (anti-Gal) is a plausible reason for differing anti-cancer defense among individuals since serine- and threonine-rich peptide sequences (STPS) in the cancer-specific MUC-1 antigen are surrogate ligands for this antibody. As affinity of a natural antibody could be modulated by systemic antigens by processes including affinity maturation, we examined the contribution of the size of lipoprotein(a) [Lp(a)], an efficient autologous anti-Gal-binding macromolecule that possesses variable numbers of STPS due to genetically determined size polymorphism, towards the specific activity (activity per unit mass) of anti-Gal. Binding of purified Lp(a) to FITC-labeled anti-Gal, measured in terms of increase in fluorescence of the latter, was inhibited by LDL in proportion to Lp(a) size presumably because LDL molecules also bind noncovalently and in proportion to Lp(a) size at the O-glycosylated and STPS-rich region of Lp(a). For the same reason, circulating forms of smaller Lp(a) which carried fewer or no noncovalently attached LDL molecules were more efficient ligands for the antibody than the same number of larger ones ( P |
| Databáze: | OpenAIRE |
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