Identification of plasma haptoglobin forms which loosely bind hemoglobin

Maria Stefania Spagnuolo1, Luisa Cigliano, Bernardetta Maresca

  • 1Istituto per il Sistema Produzione Animale in Ambiente Mediterraneo, Consiglio Nazionale delle Ricerche, Naples, Italy.

Biological Chemistry
|February 8, 2011
PubMed

Haptoglobin (Hpt) is known to capture circulating free hemoglobin (Hb) and bind apolipoprotein (Apo) A-I or E. Here, we report that Hb can be tightly bound by most of Hpt molecules (TB-Hpt, 80%), whereas loosely bound by a minor part of them (LB-Hpt, 20%). LB-Hpt amount was significantly increased (over 60%) in patients with acute coronary syndrome. LB-Hpt bound ApoA-I and ApoE less efficiently than TB-Hpt (8- and 4-fold less, respectively) and did not affect their activity of stimulating the enzyme lecithin-cholesterol acyltransferase. LB-Hpt and TB-Hpt displayed comparable levels of nitrotyrosine residues, but differences in glycan chains. Changes in LB-Hpt level might be associated with changes in Hpt functions.

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