Recombinant hemangiopoietin promotes cell adhesion and binds heparin in its multimeric form
| العنوان: | Recombinant hemangiopoietin promotes cell adhesion and binds heparin in its multimeric form |
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| المؤلفون: | Li Fang Wang, Bin Xv, Zhongchao Han, Mei Li, Zhi Bo Han, Ping Yang, Ji‑Ping Zhang |
| المصدر: | Molecular Medicine Reports. 7:959-964 |
| بيانات النشر: | Spandidos Publications, 2013. |
| سنة النشر: | 2013 |
| مصطلحات موضوعية: | Cancer Research, Conformational change, medicine.medical_treatment, Cell, Biology, Biochemistry, law.invention, Tetramer, law, Cell Adhesion, Genetics, medicine, Humans, Progenitor cell, Cell adhesion, Molecular Biology, Heparin, Circular Dichroism, Growth factor, Cell cycle, Molecular biology, Recombinant Proteins, Protein Structure, Tertiary, Cell biology, medicine.anatomical_structure, Oncology, Recombinant DNA, Molecular Medicine, Proteoglycans, Protein Multimerization, Dimerization, Protein Binding |
| الوصف: | Hemangiopoietin (HAPO) is a novel growth factor stimulating the proliferation of hematopoietic and endothelial progenitor cells in vitro and in vivo. The native protein is a 294‑amino acid multimodular protein. The N‑terminus constitutes of two somatomedin B (SMB) homology domains that contain 14 cysteines. The central region is a putative heparin‑binding domain (pHBD) and the C‑terminus contains mucin‑like repeats. In the present study, we demonstrated that prokaryotic recombinant human HAPO (rhHAPO) self‑associates into a multimeric form with a mass weight of ~129 kDa, suggesting a homologous tetramer. rhHAPO in its multimeric form was found to be more stable and more potent in promoting HESS‑5 cell adhesion. Multimeric rhHAPO had a higher affinity to heparin compared with its dimeric form, although there was no significant conformational change. C‑terminal repeats-truncated rhHAPO (rhHAPOΔmucin) was also found to be assembled into a multimer, while deletion of pHBD (rhHAPOΔmucin‑pHBD) caused the protein to remain in a dimeric form, demonstrating that SMB domains participate in self‑aggregation of the molecule and that the pHBD region promotes the tetramerization. |
| تدمد: | 1791-3004 1791-2997 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::94026d5ea3a0ba41af1fc67657299847 https://doi.org/10.3892/mmr.2013.1274 |
| حقوق: | OPEN |
| رقم الأكسشن: | edsair.doi.dedup.....94026d5ea3a0ba41af1fc67657299847 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 17913004 17912997 |
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