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Identification of plasma haptoglobin forms which loosely bind hemoglobin
-
Maria Stefania Spagnuolo
,
Luisa Cigliano
Published/Copyright:
July 25, 2011
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.
Received: 2010-7-26
Accepted: 2010-11-24
Published Online: 2011-07-25
Published in Print: 2011-04-01
©2011 by Walter de Gruyter Berlin New York
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Keywords for this article
affinity chromatography;
apolipoprotein A-I;
apolipoprotein E;
lectin-binding
Articles in the same Issue
- Guest Editorial
- Highlight: Mechanisms of RNA-mediated regulation
- HIGHLIGHT: 62ND MOSBACH COLLOQUIUM OF THE GBM ‘MECHANISMS OF RNA-MEDIATED REGULATION’
- Clustered regularly interspaced short palindromic repeats (CRISPRs): the hallmark of an ingenious antiviral defense mechanism in prokaryotes
- Regulatory RNAs in cyanobacteria: developmental decisions, stress responses and a plethora of chromosomally encoded cis-antisense RNAs
- RNA-dependent RNA polymerases in RNA silencing
- Traces of post-transcriptional RNA modifications in deep sequencing data
- Allele-selective inhibition of ataxin-3 (ATX3) expression by antisense oligomers and duplex RNAs
- PROTEIN STRUCTURE AND FUNCTION
- The effects of a plant proteinase inhibitor from Enterolobium contortisiliquum on human tumor cell lines
- Role of unique basic residues in cytotoxic, antibacterial and antiparasitic activities of human eosinophil cationic protein
- Antiangiogenic kringles derived from human plasminogen and apolipoprotein(a) inhibit fibrinolysis through a mechanism that requires a functional lysine-binding site
- Changing nucleotide specificity of the DEAD-box helicase Hera abrogates communication between the Q-motif and the P-loop
- Identification of plasma haptoglobin forms which loosely bind hemoglobin
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- Organelle stress-induced activating transcription factor-3 downregulates low-density lipoprotein receptor expression in Sk-Hep1 human liver cells
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