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Glycosaminoglycans promote HARP/PTN dimerization.
I Bernard-Pierrot1, M Héroult, G Lemaître
1la Réparation et la Régénération Tissulaires (CRRET), CNRS UPRES-A 7053, Université Paris XII, Avenue du Général de Gaulle, Créteil Cedex, 94010, France.
Biochemical and Biophysical Research Communications
|December 22, 1999
Summary
Heparin affin regulatory peptide (HARP) forms dimers, a process crucial for its biological activity. This dimerization requires heparin or other sulfated glycosaminoglycans, influencing cellular growth and differentiation.
Area of Science:
- Biochemistry
- Cell Biology
- Molecular Biology
Background:
- Heparin affin regulatory peptide (HARP), also known as pleiotrophin (PTN), is a secreted polypeptide involved in cellular growth and differentiation.
- HARP's interaction with heparin suggests a role in biological processes similar to heparin-binding fibroblast growth factor, which utilizes dimerization for mitogenic activity.
Purpose of the Study:
- To investigate the oligomerization potential of HARP.
- To identify factors influencing HARP dimerization and assess its biological relevance.
Main Methods:
- Dissuccinimidyl suberate cross-linking experiments.
- Affinity chromatography.
- Cellular expression and conditioned medium analysis.
Main Results:
- Human HARP forms noncovalent dimers.
- Dimerization is dependent on the presence of heparin or sulfated glycosaminoglycans.
- HARP is secreted as a dimer and associates with the cell surface and extracellular matrix.
Conclusions:
- HARP dimerization is a heparin/glycosaminoglycan-dependent process.
- This dimerization is relevant to HARP's biological functions in cellular processes.
- HARP functions as a dimer in its secreted and cell-associated forms.