Stimulation of wound healing, using brain extract with fibroblast growth factor (FGF) activity

Buntrock, P; Buntrock, M; Marx, I; Kranz, D; Jentzsch, K.D.; Heder, G.

doi:10.1016/s0232-1513(84)80057-2

Cited by 41 publications

(17 citation statements)

References 11 publications

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“…5 They play important roles in angiogenesis, mitogenesis, embryonic pattern formation and development, cellular differentiation, and wound healing. 1,[6][7][8][9][10] Only FGF-1 and FGF-2 are expressed at high levels in adults. FGF-1 expression is predominantly confined to the central nervous system, but FGF-2 is ubiquitously expressed throughout all adult tissues.…”

Section: Introductionmentioning

confidence: 99%

Differential regulation of the fibroblast growth factor (FGF) family by α2-macroglobulin: evidence for selective modulation of FGF-2–induced angiogenesis

Asplin

Mathew

et al. 2001

Blood

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The fibroblast growth factor (FGF) family has an important role in processes such as angiogenesis, wound healing, and development in which precise control of proteinase activity is important. The human plasma proteinase inhibitor ␣ 2 -macroglobulin (␣ 2 M) regulates cellular growth by binding and modulating the activity of many cytokines and growth factors. These studies investigate the ability of native and activated ␣ 2 M (␣ 2 M*) to bind to members of the FGF family. Both ␣ 2 M and ␣ 2 M* bind specifically and saturably to FGF-1, -2, -4, and -6, although the binding to ␣ 2 M* is of significantly higher affinity. Neither ␣ 2 M nor ␣ 2 M* bind to FGF-5, -7, -9, or -10. FGF-2 was chosen for more extensive study in view of its important role in angiogenesis. It was demonstrated that FGF-2 binds to the previously identified TGF-␤ binding site. The ␣ 2 M* inhibits FGF-2-dependent fetal bovine heart endothelial cell proliferation in a dose-dependent manner. Unexpectedly, IntroductionFibroblast growth factors (FGF) constitute a family of heparinbinding proteins that exert pleiotropic effects on cells from all embryonic lineages. 1,2 Sequencing of FGF-1 and FGF-2 has led to the identification of at least 19 proteins that are members of this mammalian family. 3,4 The FGFs are expressed during both embryogenesis and in mature organisms. 5 They play important roles in angiogenesis, mitogenesis, embryonic pattern formation and development, cellular differentiation, and wound healing. 1,[6][7][8][9][10] Only FGF-1 and FGF-2 are expressed at high levels in adults. FGF-1 expression is predominantly confined to the central nervous system, but FGF-2 is ubiquitously expressed throughout all adult tissues. 5 FGF-2 is a potent mitogen for mesoderm-derived cells, such as endothelial cells. 1,11 FGF-2 induces cell proliferation in endothelial cells derived from large vessels or capillaries with a median effective concentration of 1.5 to 2.6 pM. 12 In model systems of angiogenesis, such as the rabbit cornea, the chick chorioallantoic membrane, and the hamster cheek pouch, FGF-2 exerts a potent angiogenic effect. 6,13-15 FGF-1 and -2 are both involved in vasculogenesis, because epiblast cells can be induced to differentiate into endothelial cells by incubation with either of these FGFs. 8 FGF-2 up-regulates the urinary plasminogen activator receptor and stimulates the release of urinary plasminogen activator and collagenase in endothelial cells. [16][17][18] Additionally, FGFs act as chemoattractants for endothelial cells. 19 The ability of the FGFs to exert their effects depends on their interaction with both cellsurface receptor tyrosine kinases and extracellular and cell-surfacebound heparan sulfate proteoglycans. 20,21 However, the nature of the interactions of the FGFs with proteins and molecules that are predominantly fluid-phase has not been extensively investigated.The plasma protein ␣ 2 -macroglobulin (␣ 2 M) is a 718-kd homotetrameric glycoprotein that inactivates proteinases from all 4 mechanistic classes. 22 Proteinase i...

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Section: Introductionmentioning

confidence: 99%

Differential regulation of the fibroblast growth factor (FGF) family by α2-macroglobulin: evidence for selective modulation of FGF-2–induced angiogenesis

Asplin

Mathew

et al. 2001

Blood

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“…hFGF-2 is a potent mitogen for endothelial cells [3] and for other cells of mesodermal and neuroectodermal origin [1,2]. The wound-healing activity of hFGF-2 [4,5] renders it a potential therapeutic agent of industrial importance [6,7].…”

Section: Introductionmentioning

confidence: 99%

Susceptibility towards intramolecular disulphide-bond formation affects conformational stability and folding of human basic fibroblast growth factor

Estapé¹,

Heuvel²,

Rinas³

1998

Biochemical Journal

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The conformational stability and the folding properties of the all-beta-type protein human basic fibroblast growth factor (hFGF-2) were studied by means of fluorescence spectroscopy. The results show that the instability of the biological activity of hFGF-2 is also reflected in a low conformational stability of the molecule. The reversibility of the unfolding and refolding process was established under reducing conditions. Determination of the free-energy of unfolding in the presence of reducing agents revealed that the conformational stability of hFGF-2 (DeltaGH2Oapp congruent with21 kJ. mol-1, 25 degreesC) is low compared with other globular proteins under physiological conditions (20-60 kJ.mol-1). However, the conformational stability of hFGF-2 is particularly low under non-reducing conditions. This instability is attributed to intramolecular disulphide-bond formation, rendering the molecule more susceptible to denaturant-induced unfolding. In addition, denaturant-induced unfolding of hFGF-2 renders the protein more susceptible to irreversible oxidative denaturation. Experimental evidence is provided that the irreversibility of the unfolding and refolding process in the absence of reducing agents is linked to the formation of an intramolecular disulphide bond involving cysteines 96 and 101.

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“…The acceleration of wound-healing potential of CPPP may be due to its flavonoids properties and mainly due to their antimicrobial activity, wound contraction, and increased reepithelialisation rate [28]. Flavonoids decreased lipid peroxidation, prevented cell death, enhanced DNA synthesis, and improved angiogenesis [29]. …”

Section: Discussionmentioning

confidence: 99%

Potential Activity of 3-(2-Chlorophenyl)-1-phenyl-propenonein Accelerating Wound Healing in Rats

Dhiyaaldeen

Alshawsh

Salama

et al. 2014

BioMed Research International

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Wound healing involves inflammation followed by granular tissue development and scar formation. In this study, synthetic chalcone 3-(2-Chlorophenyl)-1-phenyl-propenone (CPPP) was investigated for a potential role in enhancing wound healing and closure. Twenty-four male rats were divided randomly into 4 groups: carboxymethyl cellulose (CMC) (0.2 mL), Intrasite gel, and CPPP (25 or 50 mg/mL). Gross morphology, wounds treatment with the CPPP, and Intrasite gel accelerate the rate of wound healing compared to CMC group. Ten days after surgery, the animals were sacrificed. Histological assessment revealed that the wounds treated with CPPP showed that wound closure site contained little amount of scar and the granulation tissue contained more collagen and less inflammatory cells than wound treated with CMC. This finding was confirmed with Masson's trichrome staining. The antioxidant defence enzymes catalase (CAT) and superoxide dismutase (SOD) were significantly increased in the wound homogenates treated with CPPP (P < 0.05) compared to CMC treated group. However, in the CPPP treatment group, lipid peroxidation (MDA) was significantly decreased (P < 0.05), suggesting that the CPPP also has an important role in protection against lipid peroxidation-induced skin injury after ten days of treatment with CPPP, which is similar to the values of cytokines TGF-β and TNF-α in tissue homogenate. Finally the administration of CPPP at a dosage of 25 and 50 mg/kg was suitable for the stimulation of wound healing.

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Stimulation of wound healing, using brain extract with fibroblast growth factor (FGF) activity

Cited by 41 publications

References 11 publications

Differential regulation of the fibroblast growth factor (FGF) family by α2-macroglobulin: evidence for selective modulation of FGF-2–induced angiogenesis

Differential regulation of the fibroblast growth factor (FGF) family by α2-macroglobulin: evidence for selective modulation of FGF-2–induced angiogenesis

Susceptibility towards intramolecular disulphide-bond formation affects conformational stability and folding of human basic fibroblast growth factor

Potential Activity of 3-(2-Chlorophenyl)-1-phenyl-propenonein Accelerating Wound Healing in Rats

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