PMID: 43803Dec 1, 1979

The pathochemistry of kernicterus

Early Human Development
R P WennbergL F Rasmussen

Abstract

The stoichiometry of bilirubin--albumin interaction has been analyzed and quantitated in several recent studies, confirming that albumin binding of bilirubin obeys the law of mass action [4, 5, 14, 16, 26, 36, 43, 46, 61, 65, 73, 92, 111]. These studies provide a basis for interpreting bilirubin transport, cell uptake and toxicity from physicochemical and pharmacologic perspectives [35, 42, 58, 59]. In this report, we propose a model of the pathogenesis of kernicterus which views serum albumin and tissue as competing with each other for binding the miscible bilirubin pool. Evidence is presented to show that bilirubin normally binds reversibly to cellular membranes and certain soluble enzymes just as it does to albumin; the unbound bilirubin concentration is the driving force for both albumin and tissue binding. We propose that albumin binding is determined by the concentration of free bilirubin anion (which is essentially unaffected by physiologic pH changes), and that tissue binding is mainly determined by the concentration of free bilirubin acid (which is greatly influenced by pH). When bilirubin--tissue complexes are formed, essential cell functions may be inhibited, producing cellular acidosis, irreversible intracellular ag...Continue Reading

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Related Concepts

ALB
Bilirubin, (4E,15E)-Isomer
Plasma Protein Binding Capacity
Oxidative Phosphorylation
Plasma Albumin
Kernicterus
Hydrogen-Ion Concentration
Plasma Membrane
Newborn Physiological Jaundice
Exchange Transfusion, Whole Blood

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