Self-assembled dodecyl group-modified gelatin microparticle-based hydrogels with angiogenic properties
Source abstract
Abstract
Abstract Supplying oxygen and nutrients to implanted cells or tissues is an important factor that improves their survivability and function in regenerative medicine. Various efforts have been made to develop angiogenic materials by incorporating and releasing growth factors such as vascular endothelial growth factor (VEGF). However, these exogenous growth factors have a short half-life under physiological conditions. We therefore designed a novel angiogenic microparticle (C12-MP) comprising Alaska pollock-derived gelatin (ApGltn) modified with a dodecyl group (C12-ApGltn) to stimulate endogenous VEGF secretion. The C12-MP suspension formed an injectable hydrogel, the rheological properties and enzymatic degradation of which were evaluated. RAW264 cells, mouse macrophage-like cells, cultured with C12-MPs, secreted significantly more VEGF than the original ApGltn MPs. Based on laser Doppler perfusion imaging, the C12-MP hydrogel clearly induced increased blood perfusion in a subcutaneous mouse model compared with the original ApGltn microparticle (Org-MP) or phosphate-buffered saline controls. Histological studies revealed that the areas of nuclear factor (NF)-κB, CD31, and myeloperoxidase staining showed a greater increase at the site injected with C12-MPs than at the site injected with the original ApGltn microparticles or phosphate-buffered saline. The C12-MP hydrogel is a promising angiogenic material for constructing vascular beds for cell transplantation by promoting endogenous VEGF secretion without additional growth factors.
Source: crossref · Quality: baseline
Research context
OpenAlex topics: Angiogenesis and VEGF in Cancer · Electrospun Nanofibers in Biomedical Applications · Corneal Surgery and Treatments
SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.
References (45)
Show source-provided references
1. Tabata, Y., Miyao, M., Ozeki, M. & Ikada, Y. Controlled release of vascular endothelial growth factor by use of collagen hydrogels. J. Biomater. Sci. Polym. Ed. 11, 915–930 (2000).10.1163/156856200744101 ↗
2. Peattie, R. A. et al. Dual growth factor-induced angiogenesis in vivo using hyaluronan hydrogel implants. Biomaterials 27, 1868–1875 (2006).10.1016/j.biomaterials.2005.09.035 ↗
3. Amsden, B. Novel biodegradable polymers for local growth factor delivery. Eur. J. Pharm. Biopharm. 97, 318–328 (2015).10.1016/j.ejpb.2015.06.008 ↗
4. Laham, R. J., Rezaee, M., Post, M., Xu, X. & Sellke, F. W. Intrapericardial administration of basic fibroblast growth factor: myocardial and tissue distribution and comparison with intracoronary and intravenous administration. Catheter. Cardiovasc. Interv. 58, 375–381 (2003).10.1002/ccd.10378 ↗
5. Lazarous, D. F. et al. Comparative effects of basic fibroblast growth factor and vascular endothelial growth factor on coronary collateral development and the arterial response to injury. Circulation 94, 1074–1082 (1996).10.1161/01.CIR.94.5.1074 ↗
6. Ferrara, N., Gerber, H. P. & LeCouter, J. The biology of VEGF and its receptors. Nat. Med. 9, 669–676 (2003).10.1038/nm0603-669 ↗
7. Raetz, C. R. H. Biochemistry of endotoxins. Annu. Rev. Biochem. 59, 129–170 (1990).10.1146/annurev.bi.59.070190.001021 ↗
8. Raetz, C. R. H. & Whitfield, C. Lipopolysaccharide endotoxins. Annu. Rev. Biochem. 71, 635–700 (2002).10.1146/annurev.biochem.71.110601.135414 ↗
9. Alexander, C. & Zähringer, U. Chemical structure of lipid A - The primary immunomodulatory center of bacterial lipopolysaccharides. Trends Glycosci. Glycotechnol. 14, 69–86 (2002).10.4052/tigg.14.69 ↗
10. Lee, J. Y. et al. Reciprocal modulation of toll-like receptor-4 signaling pathways involving MyD88 and phosphatidylinositol 3-kinase/AKT by saturated and polyunsaturated fatty acids. J. Biol. Chem. 278, 37041–37051 (2003).10.1074/jbc.M305213200 ↗
11. Wong, S. W. et al. Fatty acids modulate toll-like receptor 4 activation through regulation of receptor dimerization and recruitment into lipid rafts in a reactive oxygen species-dependent manner. J. Biol. Chem. 284, 27384–27392 (2009).10.1074/jbc.M109.044065 ↗
12. Milanski, M. et al. Saturated fatty acids produce an inflammatory response predominantly through the activation of TLR4 signaling in hypothalamus: implications for the pathogenesis of obesity. J. Neurosci. 29, 359–370 (2009).10.1523/JNEUROSCI.2760-08.2009 ↗
13. Huang, S. et al. Saturated fatty acids activate TLR-mediated proinflammatory signaling pathways. J. Lipid Res. 53, 2002–2013 (2012).10.1194/jlr.D029546 ↗
14. Rocha, D. M., Caldas, A. P., Oliveira, L. L., Bressan, J. & Hermsdorff, H. H. Saturated fatty acids trigger TLR4-mediated inflammatory response. Atherosclerosis 244, 211–215 (2016).10.1016/j.atherosclerosis.2015.11.015 ↗
15. Wang, Y. et al. Saturated palmitic acid induces myocardial inflammatory injuries through direct binding to TLR4 accessory protein MD2. Nat. Commun. 8, 13997 (2017).
16. Yoshizawa, K., Mizuta, R. & Taguchi, T. Enhanced angiogenesis of growth factor-free porous biodegradable adhesive made with hexanoyl group-modified gelatin. Biomaterials 63, 14–23 (2015).10.1016/j.biomaterials.2015.06.003 ↗
17. Mizuno, Y. & Taguchi, T. Growth factor-free, angiogenic hydrogel based on hydrophobically modified Alaska pollock gelatin. J. Tissue Eng. Regen. Med. 13, 2291–2299 (2019).10.1002/term.2957 ↗
18. Nishiguchi, A., Kurihara, Y. & Taguchi, T. Underwater-adhesive microparticle dressing composed of hydrophobically-modified Alaska pollock gelatin for gastrointestinal tract wound healing. Acta Biomater. 99, 387–396 (2019).10.1016/j.actbio.2019.08.040 ↗
19. Okuyama, T. & Satake, K. On the preparation and properties of 2,4,6-trinitrophenyl-amino acids and -peptides. J. Biochem. 47, 454–466 (1960).10.1093/oxfordjournals.jbchem.a127083 ↗
20. Habeeb, A. F. S. A. Determination of free amino groups in proteins by trinitrobenzenesulfonic acid. Anal. Biochem. 14, 328–336 (1966).10.1016/0003-2697(66)90275-2 ↗
21. Adler-Nissen, J. Determination of the degree of hydrolysis of food protein hydrolysates by trinitrobenzenesulfonic acid. J. Agric. Food Chem. 27, 1256–1262 (1979).10.1021/jf60226a042 ↗
22. Mizuno, Y., Mizuta, R., Hashizume, M. & Taguchi, T. Enhanced sealing strength of a hydrophobically-modified Alaska pollock gelatin-based sealant. Biomater. Sci. 5, 982–989 (2017).10.1039/C6BM00829A ↗
23. Borch, R. F., Bernstein, M. D. & Durst, H. D. The cyanohydridoborate anion as a selective reducing agent. J. Am. Chem. Soc. 93, 2897–2904 (1971).10.1021/ja00741a013 ↗
24. Borch, R. F. & Hassid, A. I. A new method for the methylation of amines. J. Org. Chem. 37, 1673–1674 (1972).10.1021/jo00975a049 ↗
25. Sato, S., Sakamoto, T., Miyazawa, E. & Kikugawa, Y. One-pot reductive amination of aldehydes and ketones with α-picoline-borane in methanol, in water, and in neat conditions. Tetrahedron 60, 7899–7906 (2004).10.1016/j.tet.2004.06.045 ↗
26. Abdel-Magid, A. F., Carson, K. G., Harris, B. D., Maryanoff, C. A. & Shah, R. D. Reductive amination of aldehydes and ketones with sodium triacetoxyborohydride. Studies on direct and indirect reductive amination procedures. J. Org. Chem. 61, 3849–3862 (1996).10.1021/jo960057x ↗
27. Mizuno, Y. & Taguchi, T. Promotion of cell migration into a hydrophobically modified Alaska pollock gelatin-based hydrogel. Macromol. Biosci. 19, 1900083 (2019).10.1002/mabi.201900083 ↗
28. Patra, S., Basak, P. & Tibarewala, D. N. Synthesis of gelatin nano/submicron particles by binary nonsolvent aided coacervation (BNAC) method. Mater. Sci. Eng. C 59, 310–318 (2016).10.1016/j.msec.2015.10.011 ↗
29. Qin, Z., Joo, J., Gu, L. & Sailor, M. J. Size control of porous silicon nanoparticles by electrochemical perforation etching. Part. Part. Syst. Charact. 31, 252–256 (2014).10.1002/ppsc.201300244 ↗
30. Kozlov, N. K. et al. Recycling of silicon: from industrial waste to biocompatible nanoparticles for nanomedicine. Mater. Res. Express 4, 95026 (2017).10.1088/2053-1591/aa8c33 ↗
31. Zuidema, J. M., Rivet, C. J., Gilbert, R. J. & Morrison, F. A. A protocol for rheological characterization of hydrogels for tissue engineering strategies. J. Biomed. Mater. Res. - Part B Appl. Biomater. 102, 1063–1073 (2014).10.1002/jbm.b.33088 ↗
32. Browning, M. B., Cereceres, S. N., Luong, P. T. & Cosgriff-Hernandez, E. M. Determination of the in vivo degradation mechanism of PEGDA hydrogels. J. Biomed. Mater. Res. - Part A 102, 4244–4251 (2014).
33. Lysakova-Devine, T. et al. Viral inhibitory peptide of TLR4, a peptide derived from vaccinia protein A46, specifically inhibits TLR4 by directly targeting MyD88 adaptor-like and TRIF-related adaptor molecule. J. Immunol. 185, 4261–4271 (2010).10.4049/jimmunol.1002013 ↗
34. Bernert, D. B., Isenbügel, K. & Ritter, H. Synthesis of a novel glycopeptide by polymeranalogous reaction of gelatin with mono-6-para-toluenesulfonyl-β-cyclodextrin and its supramolecular properties. Macromol. Rapid Commun. 32, 397–403 (2011).10.1002/marc.201000554 ↗
35. Rodin, V. V. & Izmailova, V. N. NMR method in the study of the interfacial adsorption layer of gelatin. Colloids Surf. A Physicochem. Eng. Asp. 106, 95–102 (1996).10.1016/0927-7757(95)03358-0 ↗
36. Nakamura, H. & Ishii, M. Rheological behavior of concentrated monodispersed colloidal suspensions. Nihon Reoroji Gakkaishi 47, 1–7 (2019).10.1678/rheology.47.1 ↗
37. Gelse, K., Pöschl, E. & Aigner, T. Collagens - Structure, function, and biosynthesis. Adv. Drug Deliv. Rev. 55, 1531–1546 (2003).10.1016/j.addr.2003.08.002 ↗
38. Davidenko, N. et al. Evaluation of cell binding to collagen and gelatin: a study of the effect of 2D and 3D architecture and surface chemistry. J. Mater. Sci. Mater. Med. 27, 148 (2016).10.1007/s10856-016-5763-9 ↗
39. Nishiguchi, A. & Taguchi, T. Designing an anti-inflammatory and tissue-adhesive colloidal dressing for wound treatment. Colloids Surf. B Biointerfaces 188, 110737 (2020).10.1016/j.colsurfb.2019.110737 ↗
40. Pacheco, P., White, D. & Sulchek, T. Effects of microparticle size and Fc density on macrophage phagocytosis. PLoS ONE 8, e60989 (2013).
41. Itaya, H. et al. Expression of vascular endothelial growth factor in human monocyte/macrophages stimulated with lipopolysaccharide. Thromb. Haemost. 85, 171–176 (2001).10.1055/s-0037-1612921 ↗
42. Kiriakidis, S. et al. VEGF expression in human macrophages is NF-κB-dependent: studies using adenoviruses expressing the endogenous NF-κB inhibitor IκBα and a kinase-defective form of the IκB kinase 2. J. Cell Sci. 116, 665–674 (2003).10.1242/jcs.00286 ↗
43. Aoki, S. et al. The efficacy of basic fibroblast growth factor-loaded poly(lactic-co-glycolic acid) nanosheet for mouse wound healing. Wound Repair Regen. 25, 1008–1016 (2017).10.1111/wrr.12604 ↗
44. Ueha, S., Shand, F. H. W. & Matsushima, K. Cellular and molecular mechanisms of chronic inflammation-associated organ fibrosis. Front. Immunol. 3, 1–6 (2012).10.3389/fimmu.2012.00071 ↗
45. Dulmovits, B. M. & Herman, I. M. Microvascular remodeling and wound healing: a role for pericytes. Int. J. Biochem. Cell Biol. 44, 1800–1812 (2012).10.1016/j.biocel.2012.06.031 ↗