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Laminin heparin-binding peptides bind to several growth factors and enhance diabetic wound healing
by
Hubbell, Jeffrey A.
, Ishihara, Jun
, Ishihara, Ako
, Sasaki, Koichi
, White, Michael J. V.
, Briquez, Priscilla S.
, Fukunaga, Kazuto
in
13/107
/ 13/31
/ 13/51
/ 631/61/490
/ 631/80/79/750
/ 692/699/2743/137/138
/ Animals
/ Anticoagulants
/ Binding
/ Binding Sites
/ Biomaterials
/ Cell surface
/ Cells, Cultured
/ Diabetes
/ Diabetes mellitus
/ Diabetes Mellitus, Type 2 - genetics
/ Diabetes Mellitus, Type 2 - metabolism
/ Diabetes Mellitus, Type 2 - physiopathology
/ Endothelial cells
/ Extracellular matrix
/ Fibrin
/ Fibroblasts
/ Growth factors
/ Heparin
/ Heparin - metabolism
/ Humanities and Social Sciences
/ Humans
/ Intercellular Signaling Peptides and Proteins - metabolism
/ Isoforms
/ Laminin
/ Laminin - metabolism
/ Male
/ Mice, Inbred C57BL
/ Morphogenesis
/ multidisciplinary
/ Peptides
/ Peptides - metabolism
/ Platelet-derived growth factor
/ Platelet-derived growth factor BB
/ Protein Binding
/ Receptors
/ Regeneration
/ Science
/ Science (multidisciplinary)
/ Skin - injuries
/ Syndecan
/ Tissue engineering
/ Vascular endothelial growth factor
/ Wound Healing
2018
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Laminin heparin-binding peptides bind to several growth factors and enhance diabetic wound healing
by
Hubbell, Jeffrey A.
, Ishihara, Jun
, Ishihara, Ako
, Sasaki, Koichi
, White, Michael J. V.
, Briquez, Priscilla S.
, Fukunaga, Kazuto
in
13/107
/ 13/31
/ 13/51
/ 631/61/490
/ 631/80/79/750
/ 692/699/2743/137/138
/ Animals
/ Anticoagulants
/ Binding
/ Binding Sites
/ Biomaterials
/ Cell surface
/ Cells, Cultured
/ Diabetes
/ Diabetes mellitus
/ Diabetes Mellitus, Type 2 - genetics
/ Diabetes Mellitus, Type 2 - metabolism
/ Diabetes Mellitus, Type 2 - physiopathology
/ Endothelial cells
/ Extracellular matrix
/ Fibrin
/ Fibroblasts
/ Growth factors
/ Heparin
/ Heparin - metabolism
/ Humanities and Social Sciences
/ Humans
/ Intercellular Signaling Peptides and Proteins - metabolism
/ Isoforms
/ Laminin
/ Laminin - metabolism
/ Male
/ Mice, Inbred C57BL
/ Morphogenesis
/ multidisciplinary
/ Peptides
/ Peptides - metabolism
/ Platelet-derived growth factor
/ Platelet-derived growth factor BB
/ Protein Binding
/ Receptors
/ Regeneration
/ Science
/ Science (multidisciplinary)
/ Skin - injuries
/ Syndecan
/ Tissue engineering
/ Vascular endothelial growth factor
/ Wound Healing
2018
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Laminin heparin-binding peptides bind to several growth factors and enhance diabetic wound healing
by
Hubbell, Jeffrey A.
, Ishihara, Jun
, Ishihara, Ako
, Sasaki, Koichi
, White, Michael J. V.
, Briquez, Priscilla S.
, Fukunaga, Kazuto
in
13/107
/ 13/31
/ 13/51
/ 631/61/490
/ 631/80/79/750
/ 692/699/2743/137/138
/ Animals
/ Anticoagulants
/ Binding
/ Binding Sites
/ Biomaterials
/ Cell surface
/ Cells, Cultured
/ Diabetes
/ Diabetes mellitus
/ Diabetes Mellitus, Type 2 - genetics
/ Diabetes Mellitus, Type 2 - metabolism
/ Diabetes Mellitus, Type 2 - physiopathology
/ Endothelial cells
/ Extracellular matrix
/ Fibrin
/ Fibroblasts
/ Growth factors
/ Heparin
/ Heparin - metabolism
/ Humanities and Social Sciences
/ Humans
/ Intercellular Signaling Peptides and Proteins - metabolism
/ Isoforms
/ Laminin
/ Laminin - metabolism
/ Male
/ Mice, Inbred C57BL
/ Morphogenesis
/ multidisciplinary
/ Peptides
/ Peptides - metabolism
/ Platelet-derived growth factor
/ Platelet-derived growth factor BB
/ Protein Binding
/ Receptors
/ Regeneration
/ Science
/ Science (multidisciplinary)
/ Skin - injuries
/ Syndecan
/ Tissue engineering
/ Vascular endothelial growth factor
/ Wound Healing
2018
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Laminin heparin-binding peptides bind to several growth factors and enhance diabetic wound healing
Journal Article
Laminin heparin-binding peptides bind to several growth factors and enhance diabetic wound healing
2018
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Overview
Laminin, as a key component of the basement membrane extracellular matrix (ECM), regulates tissue morphogenesis. Here, we show that multiple laminin isoforms promiscuously bind to growth factors (GFs) with high affinity, through their heparin-binding domains (HBDs) located in the α chain laminin-type G (LG) domains. These domains also bind to syndecan cell-surface receptors, promoting attachment of fibroblasts and endothelial cells. We explore the application of these multifunctional laminin HBDs in wound healing in the type-2 diabetic mouse. We demonstrate that covalent incorporation of laminin HBDs into fibrin matrices improves retention of GFs and significantly enhances the efficacy of vascular endothelial cell growth factor (VEGF-A165) and platelet-derived growth factor (PDGF-BB) in promoting wound healing in vivo, under conditions where the GFs alone in fibrin are inefficacious. This laminin HBD peptide may be clinically useful by improving biomaterial matrices as both GF reservoirs and cell scaffolds, leading to effective tissue regeneration.
Laminins are important regulators of epidermal wound healing. Here, the authors show that laminins bind to multiple growth factors via their heparin-binding domains, and that incorporation of these domains into fibrin matrices increases growth factor retention, promoting wound healing in type 2 diabetic mouse models.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ 13/31
/ 13/51
/ Animals
/ Binding
/ Diabetes
/ Diabetes Mellitus, Type 2 - genetics
/ Diabetes Mellitus, Type 2 - metabolism
/ Diabetes Mellitus, Type 2 - physiopathology
/ Fibrin
/ Heparin
/ Humanities and Social Sciences
/ Humans
/ Intercellular Signaling Peptides and Proteins - metabolism
/ Isoforms
/ Laminin
/ Male
/ Peptides
/ Platelet-derived growth factor
/ Platelet-derived growth factor BB
/ Science
/ Syndecan
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