Identification of plasma haptoglobin forms which loosely bind hemoglobin.

Abstract:

: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.

journal_name

Biol Chem

journal_title

Biological chemistry

authors

Spagnuolo MS,Cigliano L,Maresca B,Pugliese CR,Abrescia P

doi

10.1515/BC.2011.033

subject

Has Abstract

pub_date

2011-04-01 00:00:00

pages

371-6

issue

4

eissn

1431-6730

issn

1437-4315

journal_volume

392

pub_type

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