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Non‐enzymatic modification of proteins by steroids: Pathological implications for autoimmunity and glucocorticoid toxicity
Author(s) -
Bucala Richard,
Cerami Anthony
Publication year - 1985
Publication title -
bioessays
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.175
H-Index - 184
eISSN - 1521-1878
pISSN - 0265-9247
DOI - 10.1002/bies.950030204
Subject(s) - steroid , chemistry , enzyme , lysine , biochemistry , glucocorticoid , covalent bond , in vivo , toxicity , hormone , biology , endocrinology , amino acid , organic chemistry , microbiology and biotechnology
Abstract Certain steroids can react with proteins to form stable, covalent addition products. 16α‐hydroxyestrone and the glucocorticoids, for example, contain ketol moieties which permit them to react non‐enzymatically with proteins by forming Schiffbase rearrangement products with lysine residues. The oral contraceptive agent, 17α‐ethinylestradiol, can add to proteins after being enzymatically activated by microsomal oxidation. Elevated plasma levels of these steroids result in an increased amount of protein modification in vivo. Recent investigations have linked the occurrence of steroid‐modified proteins with pathological sequelae associated with high steroid levels.