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Volumn 220, Issue , 2015, Pages 79-88

Heparin desulfation modulates VEGF release and angiogenesis in diabetic wounds

Author keywords

Angiogenesis; Glycosaminoglycans; Growth factors; Heparin; Hydrogels; VEGF

Indexed keywords

COMPLEXATION; DRUG PRODUCTS; ENDOTHELIAL CELLS; POLYETHYLENE GLYCOLS; POLYSACCHARIDES;

EID: 84945276142     PISSN: 01683659     EISSN: 18734995     Source Type: Journal    
DOI: 10.1016/j.jconrel.2015.10.028     Document Type: Article
Times cited : (107)

References (48)
  • 1
    • 84933070290 scopus 로고    scopus 로고
    • Extracellular matrix-inspired growth factor delivery systems for skin wound healing
    • P.S. Briquez, J.A. Hubbell, and M.M. Martino Extracellular matrix-inspired growth factor delivery systems for skin wound healing Adv. Wound Care 8 2015 479 489 10.1089/wound.2014.0603
    • (2015) Adv. Wound Care , vol.8 , pp. 479-489
    • Briquez, P.S.1    Hubbell, J.A.2    Martino, M.M.3
  • 2
    • 85007210857 scopus 로고    scopus 로고
    • Clinical application of growth factors and cytokines in wound healing
    • S. Barrientos, H. Brem, O. Stojadinovic, and M. Tomic-Canic Clinical application of growth factors and cytokines in wound healing Wound Repair Regen. 22 2014 569 578 10.1111/wrr.12205
    • (2014) Wound Repair Regen. , vol.22 , pp. 569-578
    • Barrientos, S.1    Brem, H.2    Stojadinovic, O.3    Tomic-Canic, M.4
  • 4
    • 84864126835 scopus 로고    scopus 로고
    • CCR2 recruits an inflammatory macrophage subpopulation critical for angiogenesis in tissue repair
    • S. Willenborg, T. Lucas, G. van Loo, J.A. Knipper, T. Krieg, I. Haase, and et al. CCR2 recruits an inflammatory macrophage subpopulation critical for angiogenesis in tissue repair Blood 120 2012 613 625 10.1182/blood-2012-01-403386
    • (2012) Blood , vol.120 , pp. 613-625
    • Willenborg, S.1    Lucas, T.2    Van Loo, G.3    Knipper, J.A.4    Krieg, T.5    Haase, I.6
  • 5
    • 2442717879 scopus 로고    scopus 로고
    • Topical vascular endothelial growth factor accelerates diabetic wound healing through increased angiogenesis and by mobilizing and recruiting bone marrow-derived cells
    • R.D. Galiano, O.M. Tepper, C.R. Pelo, K.A. Bhatt, M. Callaghan, N. Bastidas, and et al. Topical vascular endothelial growth factor accelerates diabetic wound healing through increased angiogenesis and by mobilizing and recruiting bone marrow-derived cells A.J.P. 164 2004 1935 1947 10.1016/S0002-9440(10)63754-6
    • (2004) A.J.P. , vol.164 , pp. 1935-1947
    • Galiano, R.D.1    Tepper, O.M.2    Pelo, C.R.3    Bhatt, K.A.4    Callaghan, M.5    Bastidas, N.6
  • 6
    • 0028815417 scopus 로고
    • Site-specific therapeutic angiogenesis after systemic administration of vascular endothelial growth factor
    • C. Bauters, T. Asahara, L.P. Zheng, and S. Takeshita Site-specific therapeutic angiogenesis after systemic administration of vascular endothelial growth factor J. Vasc. Surg. 21 1995 314 325
    • (1995) J. Vasc. Surg. , vol.21 , pp. 314-325
    • Bauters, C.1    Asahara, T.2    Zheng, L.P.3    Takeshita, S.4
  • 7
    • 0028116874 scopus 로고
    • Intramuscular administration of vascular endothelial growth factor induces dose-dependent collateral artery augmentation in a rabbit model of chronic limb ischemia
    • S. Takeshita, L.Q. Pu, L.A. Stein, A.D. Sniderman, S. Bunting, N. Ferrara, and et al. Intramuscular administration of vascular endothelial growth factor induces dose-dependent collateral artery augmentation in a rabbit model of chronic limb ischemia Circulation 90 1994 II-228 II-234
    • (1994) Circulation , vol.90 , pp. II228-II234
    • Takeshita, S.1    Pu, L.Q.2    Stein, L.A.3    Sniderman, A.D.4    Bunting, S.5    Ferrara, N.6
  • 8
    • 33144457649 scopus 로고    scopus 로고
    • Plasmin modulates vascular endothelial growth factor-a-mediated angiogenesis during wound repair
    • D. Roth, M. Piekarek, M. Paulsson, H. Christ, W. Bloch, T. Krieg, and et al. Plasmin modulates vascular endothelial growth factor-a-mediated angiogenesis during wound repair Am. J. Pathol. 168 2006 670 684 10.2353/ajpath.2006.050372
    • (2006) Am. J. Pathol. , vol.168 , pp. 670-684
    • Roth, D.1    Piekarek, M.2    Paulsson, M.3    Christ, H.4    Bloch, W.5    Krieg, T.6
  • 9
    • 84878114080 scopus 로고    scopus 로고
    • The promotion of endothelial cell attachment and spreading using FNIII10 fused to VEGF-A165
    • S. Traub, J. Morgner, M.M. Martino, S. Höning, M.A. Swartz, S.A. Wickström, and et al. The promotion of endothelial cell attachment and spreading using FNIII10 fused to VEGF-A165 Biomaterials 34 2013 5958 5968 10.1016/j.biomaterials.2013.04.050
    • (2013) Biomaterials , vol.34 , pp. 5958-5968
    • Traub, S.1    Morgner, J.2    Martino, M.M.3    Höning, S.4    Swartz, M.A.5    Wickström, S.A.6
  • 10
    • 0347725622 scopus 로고    scopus 로고
    • Ability of chronic wound fluids to degrade peptide growth factors is associated with increased levels of elastase activity and diminished levels of proteinase inhibitors
    • D.R. Yager, S.M. Chen, S.I. Ward, O.O. Olutoye, R.F. Diegelmann, and I. Kelman Cohen Ability of chronic wound fluids to degrade peptide growth factors is associated with increased levels of elastase activity and diminished levels of proteinase inhibitors Wound Repair Regen. 5 1997 23 32
    • (1997) Wound Repair Regen. , vol.5 , pp. 23-32
    • Yager, D.R.1    Chen, S.M.2    Ward, S.I.3    Olutoye, O.O.4    Diegelmann, R.F.5    Kelman Cohen, I.6
  • 11
    • 0033910462 scopus 로고    scopus 로고
    • Expression and proteolysis of vascular endothelial growth factor is increased in chronic wounds
    • G. Lauer, S. Sollberg, M. Cole, I. Flamme, J. Stürzebecher, K. Mann, and et al. Expression and proteolysis of vascular endothelial growth factor is increased in chronic wounds J. Investig. Dermatol. 115 2000 12 18 10.1046/j.1523-1747.2000.00036.x
    • (2000) J. Investig. Dermatol. , vol.115 , pp. 12-18
    • Lauer, G.1    Sollberg, S.2    Cole, M.3    Flamme, I.4    Stürzebecher, J.5    Mann, K.6
  • 12
    • 33745643590 scopus 로고    scopus 로고
    • Treatment with intramuscular vascular endothelial growth factor gene compared with placebo for patients with diabetes mellitus and critical limb ischemia: A double-blind randomized trial
    • Y.H. Kusumanto, V. van Weel, N.H. Mulder, A.J. Smit, J.J.A.M. van den Dungen, J.M.M. Hooymans, and et al. Treatment with intramuscular vascular endothelial growth factor gene compared with placebo for patients with diabetes mellitus and critical limb ischemia: a double-blind randomized trial Hum. Gene Ther. 17 2006 683 691 10.1089/Hum.2006.17.683
    • (2006) Hum. Gene Ther. , vol.17 , pp. 683-691
    • Kusumanto, Y.H.1    Van Weel, V.2    Mulder, N.H.3    Smit, A.J.4    Van Den Dungen, J.J.A.M.5    Hooymans, J.M.M.6
  • 15
    • 0345257207 scopus 로고    scopus 로고
    • Physical polymer matrices based on affinity interactions between peptides and polysaccharides
    • B.L. Seal, and A. Panitch Physical polymer matrices based on affinity interactions between peptides and polysaccharides Biomacromolecules 4 2003 1572 1582 10.1021/bm0342032
    • (2003) Biomacromolecules , vol.4 , pp. 1572-1582
    • Seal, B.L.1    Panitch, A.2
  • 16
    • 33644809242 scopus 로고    scopus 로고
    • Heparin functionalized PEG gels that modulate protein adsorption for hMSC adhesion and differentiation
    • D.S.W. Benoit, and K.S. Anseth Heparin functionalized PEG gels that modulate protein adsorption for hMSC adhesion and differentiation Acta Biomater. 1 2005 461 470 10.1016/j.actbio.2005.03.002
    • (2005) Acta Biomater. , vol.1 , pp. 461-470
    • Benoit, D.S.W.1    Anseth, K.S.2
  • 17
    • 33746038183 scopus 로고    scopus 로고
    • PEG-cross-linked heparin is an affinity hydrogel for sustained release of vascular endothelial growth factor
    • G. Tae, M. Scatena, P.S. Stayton, and A.S. Hoffman PEG-cross-linked heparin is an affinity hydrogel for sustained release of vascular endothelial growth factor J. Biomater. Sci. Polym. Ed. 17 2006 187 197 10.1163/156856206774879090
    • (2006) J. Biomater. Sci. Polym. Ed. , vol.17 , pp. 187-197
    • Tae, G.1    Scatena, M.2    Stayton, P.S.3    Hoffman, A.S.4
  • 18
    • 36048941406 scopus 로고    scopus 로고
    • Photo-crosslinkable and biodegradable pluronic/heparin hydrogels for local and sustained delivery of angiogenic growth factor
    • J.J. Yoon, H.J. Chung, and T.G. Park Photo-crosslinkable and biodegradable pluronic/heparin hydrogels for local and sustained delivery of angiogenic growth factor J. Biomed. Mater. Res. 83 2007 597 605 10.1002/jbm.a.31271
    • (2007) J. Biomed. Mater. Res. , vol.83 , pp. 597-605
    • Yoon, J.J.1    Chung, H.J.2    Park, T.G.3
  • 20
    • 34548637042 scopus 로고    scopus 로고
    • Production of heparin-functionalized hydrogels for the development of responsive and controlled growth factor delivery systems
    • T. Nie, A. Baldwin, N. Yamaguchi, and K.L. Kiick Production of heparin-functionalized hydrogels for the development of responsive and controlled growth factor delivery systems J. Control. Release 122 2007 287 296 10.1016/j.jconrel.2007.04.019
    • (2007) J. Control. Release , vol.122 , pp. 287-296
    • Nie, T.1    Baldwin, A.2    Yamaguchi, N.3    Kiick, K.L.4
  • 21
    • 53149099301 scopus 로고    scopus 로고
    • Structural and functional characterisation of poly(vinyl alcohol) and heparin hydrogels
    • A. Nilasaroya, L.A. Poole-Warren, J.M. Whitelock, and P. Jo Martens Structural and functional characterisation of poly(vinyl alcohol) and heparin hydrogels Biomaterials 29 2008 4658 4664 10.1016/j.biomaterials.2008.08.011
    • (2008) Biomaterials , vol.29 , pp. 4658-4664
    • Nilasaroya, A.1    Poole-Warren, L.A.2    Whitelock, J.M.3    Jo Martens, P.4
  • 22
    • 77549088407 scopus 로고    scopus 로고
    • Heparin-based hydrogel as a matrix for encapsulation and cultivation of primary hepatocytes
    • M. Kim, J.Y. Lee, C.N. Jones, A. Revzin, and G. Tae Heparin-based hydrogel as a matrix for encapsulation and cultivation of primary hepatocytes Biomaterials 31 2010 3596 3603 10.1016/j.biomaterials.2010.01.068
    • (2010) Biomaterials , vol.31 , pp. 3596-3603
    • Kim, M.1    Lee, J.Y.2    Jones, C.N.3    Revzin, A.4    Tae, G.5
  • 23
    • 84896394738 scopus 로고    scopus 로고
    • Heparin-functionalized polymeric biomaterials in tissue engineering and drug delivery applications
    • Y. Liang, and K.L. Kiick Heparin-functionalized polymeric biomaterials in tissue engineering and drug delivery applications Acta Biomater. 10 2014 1588 1600 10.1016/j.actbio.2013.07.031
    • (2014) Acta Biomater. , vol.10 , pp. 1588-1600
    • Liang, Y.1    Kiick, K.L.2
  • 24
    • 67849094098 scopus 로고    scopus 로고
    • A star-PEG-heparin hydrogel platform to aid cell replacement therapies for neurodegenerative diseases
    • U. Freudenberg, A. Hermann, P.B. Welzel, K. Stirl, S.C. Schwarz, M. Grimmer, and et al. A star-PEG-heparin hydrogel platform to aid cell replacement therapies for neurodegenerative diseases Biomaterials 30 2009 5049 5060 10.1016/j.biomaterials.2009.06.002
    • (2009) Biomaterials , vol.30 , pp. 5049-5060
    • Freudenberg, U.1    Hermann, A.2    Welzel, P.B.3    Stirl, K.4    Schwarz, S.C.5    Grimmer, M.6
  • 26
    • 77956009638 scopus 로고    scopus 로고
    • FGF-2 and VEGF functionalization of starPEG-heparin hydrogels to modulate biomolecular and physical cues of angiogenesis
    • A. Zieris, S. Prokoph, K.R. Levental, P.B. Welzel, M. Grimmer, U. Freudenberg, and et al. FGF-2 and VEGF functionalization of starPEG-heparin hydrogels to modulate biomolecular and physical cues of angiogenesis Biomaterials 31 2010 7985 7994 10.1016/j.biomaterials.2010.07.021
    • (2010) Biomaterials , vol.31 , pp. 7985-7994
    • Zieris, A.1    Prokoph, S.2    Levental, K.R.3    Welzel, P.B.4    Grimmer, M.5    Freudenberg, U.6
  • 27
    • 80855130875 scopus 로고    scopus 로고
    • Dual independent delivery of pro-angiogenic growth factors from starPEG-heparin hydrogels
    • A. Zieris, K. Chwalek, S. Prokoph, K.R. Levental, P.B. Welzel, U. Freudenberg, and et al. Dual independent delivery of pro-angiogenic growth factors from starPEG-heparin hydrogels J. Control. Release 156 2011 28 36 10.1016/j.jconrel.2011.06.042
    • (2011) J. Control. Release , vol.156 , pp. 28-36
    • Zieris, A.1    Chwalek, K.2    Prokoph, S.3    Levental, K.R.4    Welzel, P.B.5    Freudenberg, U.6
  • 28
  • 29
    • 33644977975 scopus 로고    scopus 로고
    • VEGF165-binding sites within heparan sulfate encompass two highly sulfated domains and can be liberated by K5 lyase
    • C.J. Robinson, B. Mulloy, J.T. Gallagher, and S.E. Stringer VEGF165-binding sites within heparan sulfate encompass two highly sulfated domains and can be liberated by K5 lyase J. Biol. Chem. 281 2006 1731 1740 10.1074/jbc.M510760200
    • (2006) J. Biol. Chem. , vol.281 , pp. 1731-1740
    • Robinson, C.J.1    Mulloy, B.2    Gallagher, J.T.3    Stringer, S.E.4
  • 30
    • 84916601128 scopus 로고    scopus 로고
    • Biohybrid networks of selectively desulfated glycosaminoglycans for tunable growth factor delivery
    • A. Zieris, R. Dockhorn, A. Röhrich, R. Zimmermann, M. Müller, P.B. Welzel, and et al. Biohybrid networks of selectively desulfated glycosaminoglycans for tunable growth factor delivery Biomacromolecules 15 2014 4439 4446 10.1021/bm5012294
    • (2014) Biomacromolecules , vol.15 , pp. 4439-4446
    • Zieris, A.1    Dockhorn, R.2    Röhrich, A.3    Zimmermann, R.4    Müller, M.5    Welzel, P.B.6
  • 31
    • 0023690338 scopus 로고
    • Interaction of heparin and antithrombin III, the role of O-sulfate groups
    • M. Petitou, and J. Lormeau Interaction of heparin and antithrombin III, the role of O-sulfate groups Eur. J. Biochem. 176 1988 637 640
    • (1988) Eur. J. Biochem. , vol.176 , pp. 637-640
    • Petitou, M.1    Lormeau, J.2
  • 32
    • 0033113620 scopus 로고    scopus 로고
    • Sugars slide into heparin activity
    • P. Sinaÿ Sugars slide into heparin activity Nature 398 1999 377 378 10.1038/18783
    • (1999) Nature , vol.398 , pp. 377-378
    • Sinaÿ, P.1
  • 33
    • 0022565392 scopus 로고
    • N.M.R. Spectroscopic observations related to the function of sulfate groups in heparin. Calcium binding vs. Biological activity
    • L. Ayotte, and A.S. Perlin N.m.r. spectroscopic observations related to the function of sulfate groups in heparin. Calcium binding vs. biological activity Carbohydr. Res. 145 1986 267 277 10.1016/S0008-6215(00)90434-8
    • (1986) Carbohydr. Res. , vol.145 , pp. 267-277
    • Ayotte, L.1    Perlin, A.S.2
  • 34
    • 0032052499 scopus 로고    scopus 로고
    • Novel regio-and stereoselective O-6-desulfation of the glucosamine moiety of heparin with N-methylpyrrolidinone-water or N, N-dimethylformamide-water mixtures
    • H. Baumann, H. Scheen, B. Huppertz, and R. Keller Novel regio-and stereoselective O-6-desulfation of the glucosamine moiety of heparin with N-methylpyrrolidinone-water or N, N-dimethylformamide-water mixtures Carbohydr. Res. 308 1998 381 388
    • (1998) Carbohydr. Res. , vol.308 , pp. 381-388
    • Baumann, H.1    Scheen, H.2    Huppertz, B.3    Keller, R.4
  • 35
    • 0016874584 scopus 로고
    • Selective N-desulfation of heparin with dimethyl sulfoxide containing water or methanol
    • Y. Inoue, and K. Nagasawa Selective N-desulfation of heparin with dimethyl sulfoxide containing water or methanol Carbohydr. Res. 46 1976 87 95 10.1016/S0008-6215(00)83533-8
    • (1976) Carbohydr. Res. , vol.46 , pp. 87-95
    • Inoue, Y.1    Nagasawa, K.2
  • 36
    • 23144451377 scopus 로고    scopus 로고
    • Preparation of monomodal polyelectrolyte complex nanoparticles of PDADMAC/poly(maleic acid- alt-α-methylstyrene) by consecutive centrifugation
    • M. Müller, B. Kessler, and S. Richter Preparation of monomodal polyelectrolyte complex nanoparticles of PDADMAC/poly(maleic acid- alt-α-methylstyrene) by consecutive centrifugation Langmuir 21 2005 7044 7051 10.1021/la050716d
    • (2005) Langmuir , vol.21 , pp. 7044-7051
    • Müller, M.1    Kessler, B.2    Richter, S.3
  • 37
    • 76249093853 scopus 로고    scopus 로고
    • Enzymatically degradable heparin-polyethylene glycol gels with controlled mechanical properties
    • M.V. Tsurkan, K.R. Levental, U. Freudenberg, and C. Werner Enzymatically degradable heparin-polyethylene glycol gels with controlled mechanical properties Chem. Commun. 46 2010 1141 1143 10.1039/B921616B
    • (2010) Chem. Commun. , vol.46 , pp. 1141-1143
    • Tsurkan, M.V.1    Levental, K.R.2    Freudenberg, U.3    Werner, C.4
  • 39
    • 0026098597 scopus 로고
    • Improved method of human umbilical arterial endothelial cell culture
    • J.R. Weis, B. Sun, and G.M. Rodgers Improved method of human umbilical arterial endothelial cell culture Thromb. Res. 61 1991 171 173
    • (1991) Thromb. Res. , vol.61 , pp. 171-173
    • Weis, J.R.1    Sun, B.2    Rodgers, G.M.3
  • 40
    • 80052951552 scopus 로고    scopus 로고
    • Engineering the growth factor microenvironment with fibronectin domains to promote wound and bone tissue healing
    • M.M. Martino, F. Tortelli, M. Mochizuki, S. Traub, D. Ben-David, G.A. Kuhn, and et al. Engineering the growth factor microenvironment with fibronectin domains to promote wound and bone tissue healing Sci. Transl. Med. 3 2011 100ra89 10.1126/scitranslmed.3002614
    • (2011) Sci. Transl. Med. , vol.3 , pp. 100ra89
    • Martino, M.M.1    Tortelli, F.2    Mochizuki, M.3    Traub, S.4    Ben-David, D.5    Kuhn, G.A.6
  • 41
    • 0036871472 scopus 로고    scopus 로고
    • Desulfation of sulfated carbohydrates
    • R. Takano Desulfation of sulfated carbohydrates Trends Glycosci. Glycotechnol. 14 2002 343 354
    • (2002) Trends Glycosci. Glycotechnol. , vol.14 , pp. 343-354
    • Takano, R.1
  • 42
    • 0030795733 scopus 로고    scopus 로고
    • Vascular endothelial growth factor: Crystal structure and functional mapping of the kinase domain receptor binding site
    • Y.A. Muller, B. Li, H.W. Christinger, J.A. Wells, B.C. Cunningham, and A.M. de Vos Vascular endothelial growth factor: crystal structure and functional mapping of the kinase domain receptor binding site Proc. Natl. Acad. Sci. U. S. A. 94 1997 7192 7197
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 7192-7197
    • Muller, Y.A.1    Li, B.2    Christinger, H.W.3    Wells, J.A.4    Cunningham, B.C.5    De Vos, A.M.6
  • 43
    • 0032776557 scopus 로고    scopus 로고
    • Structural features in heparin that interact with VEGF165 and modulate its biological activity
    • K. Ono, H. Hattori, S. Takeshita, A. Kurita, and M. Ishihara Structural features in heparin that interact with VEGF165 and modulate its biological activity Glycobiology 9 1999 705 711
    • (1999) Glycobiology , vol.9 , pp. 705-711
    • Ono, K.1    Hattori, H.2    Takeshita, S.3    Kurita, A.4    Ishihara, M.5
  • 44
    • 0035850221 scopus 로고    scopus 로고
    • On the importance and mechanisms of burst release in matrix-controlled drug delivery systems
    • X. Huang, and C.S. Brazel On the importance and mechanisms of burst release in matrix-controlled drug delivery systems J. Control. Release 73 2001 121 136
    • (2001) J. Control. Release , vol.73 , pp. 121-136
    • Huang, X.1    Brazel, C.S.2
  • 45
    • 0027082811 scopus 로고
    • The extracellular regulation of growth factor action
    • R. Flaumenhaft, and D.B. Rifkin The extracellular regulation of growth factor action Mol. Biol. Cell 3 1992 1057 1065
    • (1992) Mol. Biol. Cell , vol.3 , pp. 1057-1065
    • Flaumenhaft, R.1    Rifkin, D.B.2
  • 46
    • 52049121792 scopus 로고    scopus 로고
    • Chapter 3. Endothelial cell adhesion and migration
    • Elsevier
    • C.A. Reinhart King Chapter 3. Endothelial cell adhesion and migration Methods in Enzymology 2008 Elsevier 45 64 10.1016/S0076-6879(08)02003-X
    • (2008) Methods in Enzymology , pp. 45-64
    • Reinhart King, C.A.1
  • 47
    • 0003127656 scopus 로고    scopus 로고
    • A novel, quantitative model for study of endothelial cell migration and sprout formation within three-dimensional collagen matrices
    • R.B. Vernon, and E.H. Sage A novel, quantitative model for study of endothelial cell migration and sprout formation within three-dimensional collagen matrices Microvasc. Res. 57 1999 118 133 10.1006/mvre.1998.2122
    • (1999) Microvasc. Res. , vol.57 , pp. 118-133
    • Vernon, R.B.1    Sage, E.H.2


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