Dual physical dynamic bond-based injectable and biodegradable hydrogel for tissue regeneration

2016 ◽  
Vol 4 (6) ◽  
pp. 1175-1185 ◽  
Author(s):  
Xiaochu Ding ◽  
Jin Gao ◽  
Hassan Awada ◽  
Yadong Wang
Keyword(s):  
Growth Factors ◽  
Sustained Release ◽  
Tissue Regeneration ◽  
Shear Thinning ◽  
Heparin Binding ◽  
Biodegradable Hydrogel ◽  
Heparin Binding Growth Factors

Heparin-binding growth factors are incorporated in a new shear thinning hydrogel for sustained release with prolonged bioactivity for tissue regeneration.

Heparin stimulates the proliferation of intestinal epithelial cells in primary culture

1994 ◽  
Vol 107 (2) ◽  
pp. 401-411
Author(s):  
N. Flint ◽  
F.L. Cove ◽  
G.S. Evans
Keyword(s):  
Growth Factors ◽  
Heparan Sulphate ◽  
Primary Cultures ◽  
Cell Types ◽  
Heparin Binding ◽  
Epithelial Proliferation ◽  
Inhibition Of Proliferation ◽  
Trophic Effect ◽  
Heparin Binding Growth Factors

Heparin is a sulphated glycosaminoglycan derived from mast cells and has a number of functions including the inhibition of proliferation in several cell types and interactions with a range of heparin-binding growth factors. We report that heparin is a trophic factor in primary cultures of rat small intestinal epithelium. Heparin elicits a dose-dependent increase in epithelial proliferation and inhibits the growth of associated mesenchyme. The trophic effect of this molecule is not reproduced by other glycosaminoglycans including heparan sulphate but is dependent upon extensive molecular sulphation. Highly sulphated polysaccharides that are structurally unrelated to heparin (e.g. dextran sulphate and pentosan polysulphate) also stimulate epithelial proliferation in primary cultures. Heparin may act by the potentiation of mesenchyme-derived heparin-binding growth factors and these data suggest an in vivo role for mast cell-derived heparin in mucosal wound regeneration.

IMMUNOASSAY FOR MEASURING THE HEPARIN-BINDING GROWTH FACTORS HARP AND MK IN BIOLOGICAL FLUIDS

2002 ◽  
Vol 23 (1) ◽  
pp. 33-48 ◽  
Author(s):  
Patrick Soulié ◽  
Mélanie Héroult ◽  
Isabelle Bernard ◽  
Marie-Emmanuelle Kerros ◽  
Pierre Emmanuel Milhiet ◽  
...  
Keyword(s):  
Growth Factors ◽  
Biological Fluids ◽  
Heparin Binding ◽  
Heparin Binding Growth Factors

A New Method for purifying Heparin-binding Growth Factors

1989 ◽  
Vol 556 (1 Heparin and R) ◽  
pp. 166-172 ◽  
Author(s):  
Y. SHING ◽  
M. KLAGSBRUN ◽  
J. FOLKMAN
Keyword(s):  
Growth Factors ◽  
New Method ◽  
Heparin Binding ◽  
Heparin Binding Growth Factors

scholarly journals Activated mesothelial cells produce heparin-binding growth factors: implications for tumour metastases

2000 ◽  
Vol 82 (6) ◽  
pp. 1233-1238 ◽  
Author(s):  
D G Jayne ◽  
S L Perry ◽  
E Morrison ◽  
S M Farmery ◽  
P J Guillou
Keyword(s):  
Growth Factors ◽  
Mesothelial Cells ◽  
Heparin Binding ◽  
Heparin Binding Growth Factors

Amphiregulin Is Produced by Myeloma Cells and Is Involved in Tumor-Environment Interactions in Multiple Myeloma.

Blood ◽  
2004 ◽  
Vol 104 (11) ◽  
pp. 4306-4306
Author(s):  
Karène Mahtouk ◽  
Dirk Hose ◽  
Thierry Reme ◽  
John De Vos ◽  
Michel Jourdan ◽  
...  
Keyword(s):  
Multiple Myeloma ◽  
Bone Marrow ◽  
Growth Factors ◽  
Plasma Cells ◽  
Myeloma Cell ◽  
Erbb Receptors ◽  
Heparin Binding ◽  
Myeloma Cells ◽  
Heparin Binding Growth Factors ◽  
Egf Family

Abstract Multiple myeloma (MM) is characterized by the accumulation of clonal malignant plasma cells in the bone marrow. One of the hallmarks of plasma cells is the expression of the heparan-sulfate proteoglycan syndecan-1. In epithelial cells, syndecan-1 plays a major role as a coreceptor for heparin-binding growth factors and chemokines. This stresses that heparin-binding growth factors may play a major role in the biology of MM cells. Recently we have demonstrated that heparin-binding EGF-like growth factor (HB-EGF), one of the ten members of the Epidermal Growth Factor (EGF) family, is produced by the tumor microenvironment and is able to trigger myeloma cell growth. As amphiregulin (AREG) is another member of the EGF family that also binds heparan-sulphate chains, we investigated its role in MM. We looked for AREG expression on a panel of 7 normal plasmablastic cells (PPCs), 7 normal bone marrow plasma cells (BMPCs), purified MM cells from 65 patients and 20 myeloma cell lines (HMCLs), with Affymetrix U133A+B microarrays. We showed that primary MM cells overexpress AREG compared to normal BMPCs and PPCs. We then investigated the expression of the ErbB receptors with real-time RT-PCR. Myeloma cells variably expressed the 4 ErbB receptors. Normal BMPCs also expressed ErbB1 and ErbB2 unlike PPCs that did not express any ErbB receptors. We demonstrated that the high AREG expression by primary myeloma cells may have a dual effect. On the one hand, AREG stimulated IL-6 production and growth of bone-marrow stromal cells that highly express the AREG ErbB1 receptor. On the other hand, AREG could promote HMCL proliferation, suggesting that a functional autocrine loop involving AREG and ErbB receptors is involved in MM cell growth. Finally, we looked for the effect of ErbB inhibitors on MM cells of 14 patients cultured for 6 days together with their bone marrow environment. A pan-ErbB inhibitor (PD-169540, Pfizer) and an ErbB1-inhibitor (IRESSA, Astrazeneca) induced strong MM cell apoptosis in respectively 71% of patients (10 of 14) and 29% of patients (4 of 14). Of major interest, when PD169540 or IRESSA were combined with dexamethasone, they induced a dramatic myeloma cell death (respectively 92% and 69% inhibition of MM cell survival), while non-myeloma cells were unaffected. Thus ErbB activation is critical to trigger MM-cell survival in short-term culture. In conclusion, our findings provide evidence for a major role of AREG and HB-EGF in the biology of multiple myeloma and identify ErbB receptors as putative therapeutic targets. These data emphasize the interest of clinical evaluation of specific-ErbB-inhibitors in patients with MM, either used alone or in combination with dexamethasone.

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