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Related Experiment Video

Updated: Jul 13, 2026

Using a GFP-tagged TMEM184A Construct for Confirmation of Heparin Receptor Identity

Using a GFP-tagged TMEM184A Construct for Confirmation of Heparin Receptor Identity

Published on: February 17, 2017

Binding between the integrin alphaXbeta2 (CD11c/CD18) and heparin.

Thomas Vorup-Jensen¹, Lianli Chi, Louise C Gjelstrup

¹Immune Disease Institute (formerly CBR Institute for Biomedical Research), Department of Pathology, Harvard Medical School, Boston, Massachusetts 02115, USA.

The Journal of Biological Chemistry

|August 19, 2007

Summary

This study identifies specific heparin structures that bind to the integrin alphaXbeta2 receptor, crucial for cell adhesion and signaling. Longer, highly sulfated heparin chains are key for potent inhibition of iC3b binding.

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Area of Science:

Biochemistry
Cell Biology
Immunology

Background:

Cell surface receptors and sulfated glucosamineglycans mediate cell adhesion and signaling.
Heparin, a sulfated polysaccharide, binds to the integrin receptor alphaXbeta2 (p150,95, CD11c/CD18).

Purpose of the Study:

To identify structural motifs in heparin responsible for high-affinity binding to the integrin alphaXbeta2 I domain.
To investigate the role of heparin chain length and sulfation in inhibiting alphaXbeta2 binding to complement fragment iC3b.

Main Methods:

Analysis of heparin oligomers of varying chain lengths and sulfation.
Inhibition assays using the alphaX I domain and iC3b.
Direct binding studies of the alphaX I domain to immobilized heparin.
Assessment of Mg2+ requirement and conformational changes in the alphaXbeta2 receptor.

Main Results:

Heparin oligomers of 10 saccharide residues or longer strongly inhibited alphaX I domain binding to iC3b.
Smaller heparin oligomers and fondaparinux did not block binding.
Fully sulfated 12-saccharide heparin oligomers showed high affinity (1.3 microM) for the alphaX I domain and acted as potent iC3b antagonists.
Heparin binding to the alphaX I domain is conformationally regulated, Mg2+-dependent, and induces allosteric changes in the alphaXbeta2 receptor ectodomain.

Conclusions:

Specific structural features of heparin, particularly longer, fully sulfated chains, are critical for high-affinity binding to the integrin alphaXbeta2 I domain.
Heparin acts as a potent antagonist of iC3b binding by inducing conformational changes in the alphaXbeta2 receptor, highlighting the allosteric regulation of integrin function by glycosaminoglycans.