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Ghislain Opdenakker - One of the best experts on this subject based on the ideXlab platform.
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the collagen binding domain of Gelatinase a modulates degradation of collagen iv by Gelatinase b
Journal of Molecular Biology, 2009Co-Authors: Magda Gioia, Christopher M Overall, Susanna Monaco, Philippe E Van Den Steen, Diego Sbardella, Giuseppe Grasso, Stefano Marini, Ghislain Opdenakker, Massimo ColettaAbstract:Summary Type IV collagen remodeling plays a critical role in inflammatory responses, angiogenesis and metastasis. Its remodeling is executed by a family of matrix metalloproteinases (MMPs), of which the constitutive Gelatinase A (MMP2) and the inducible Gelatinase B (MMP9) are key examples. Thus, in many pathological conditions, both Gelatinases act together. Kinetic data are reported for the enzymatic processing at 37 °C of type IV collagen from human placenta by MMP9 and its modulation by the fibronectin-like collagen binding domain (CBD) of MMP2. The α1 and α2 chain components of type IV collagen were cleaved by Gelatinases and identified by mass spectrometry as well as Edman sequencing. Surface plasmon resonance interaction assays showed that CBD bound type IV collagen at two topologically distinct sites. On the basis of linked-function analysis, we demonstrated that CBD of MMP2 tuned the cleavage of collagen IV by MMP9, presumably by inducing a ligand-linked structural change on the type IV collagen. At low concentrations, the CBD bound the first site and thereby allosterically modulated the binding of MMP9 to collagen IV, thus enhancing the collagenolytic activity of MMP9. At high concentrations, CBD binding to the second site interfered with MMP9 binding to collagen IV, acting as a competitive inhibitor. Interestingly, modulation of collagen IV degradation by inactive forms of MMP2 also occurred in a cell-based system, revealing that this interrelationship affected neutrophil migration across a collagen IV membrane. The regulation of the proteolytic processing by a catalytically inactive domain (i.e., CBD) suggests that the two Gelatinases might cooperate in degrading substrates even when either one is inactive. This observation reinforces the idea of exosite targets for MMP inhibitors, which should include all macromolecular substrate recognition sites.
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the collagen binding domain of Gelatinase a modulates degradation of collagen iv by Gelatinase b
Journal of Molecular Biology, 2009Co-Authors: Magda Gioia, Christopher M Overall, Susanna Monaco, Philippe E Van Den Steen, Diego Sbardella, Giuseppe Grasso, Stefano Marini, Ghislain Opdenakker, Massimo ColettaAbstract:Summary Type IV collagen remodeling plays a critical role in inflammatory responses, angiogenesis and metastasis. Its remodeling is executed by a family of matrix metalloproteinases (MMPs), of which the constitutive Gelatinase A (MMP2) and the inducible Gelatinase B (MMP9) are key examples. Thus, in many pathological conditions, both Gelatinases act together. Kinetic data are reported for the enzymatic processing at 37 °C of type IV collagen from human placenta by MMP9 and its modulation by the fibronectin-like collagen binding domain (CBD) of MMP2. The α1 and α2 chain components of type IV collagen were cleaved by Gelatinases and identified by mass spectrometry as well as Edman sequencing. Surface plasmon resonance interaction assays showed that CBD bound type IV collagen at two topologically distinct sites. On the basis of linked-function analysis, we demonstrated that CBD of MMP2 tuned the cleavage of collagen IV by MMP9, presumably by inducing a ligand-linked structural change on the type IV collagen. At low concentrations, the CBD bound the first site and thereby allosterically modulated the binding of MMP9 to collagen IV, thus enhancing the collagenolytic activity of MMP9. At high concentrations, CBD binding to the second site interfered with MMP9 binding to collagen IV, acting as a competitive inhibitor. Interestingly, modulation of collagen IV degradation by inactive forms of MMP2 also occurred in a cell-based system, revealing that this interrelationship affected neutrophil migration across a collagen IV membrane. The regulation of the proteolytic processing by a catalytically inactive domain (i.e., CBD) suggests that the two Gelatinases might cooperate in degrading substrates even when either one is inactive. This observation reinforces the idea of exosite targets for MMP inhibitors, which should include all macromolecular substrate recognition sites.
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Gelatinase b matrix metalloproteinase 9 contributes to cellular infiltration in a murine model of zymosan peritonitis
Immunobiology, 2006Co-Authors: Elzbieta Kolaczkowska, Ghislain Opdenakker, Magdalena Chadzinska, Anna Scislowskaczarnecka, Barbara Plytycz, Bernd ArnoldAbstract:Abstract Murine zymosan-induced peritonitis represents a well-defined model of acute inflammation. However, the molecular mechanisms by which leukocytes degrade basement membranes during extravasation into the peritoneum are not clear. Gelatinase B (MMP-9) is thought to participate in cellular migration, yet its role in leukocyte transmigration through endothelia during inflammation remains controversial. The aim of the present study was to evaluate the role of MMP-9 in the cell influx during zymosan-induced experimental peritonitis. In zymosan-treated Balb/c mice MMP-9 and its natural inhibitor (tissue inhibitor of metalloproteinase 1 – TIMP-1) were present in the peritoneal fluid and plasma at the time of peritoneal neutrophil (polymorphonuclear leukocyte – PMN) infiltration and persisted there until the time of monocytes/macrophages influx. To probe the function of Gelatinases, Gelatinase B-deficient mice (MMP-9−/−) were used as well as Balb/c mice treated with cyclic CTTHWGFTLC (INH), a specific peptide inhibitor of Gelatinases. The studies revealed that in either group of mice deprived of MMP-9 activity, PMN infiltration was impaired at the time of their maximal extravasation (6 h) while tumor necrosis factor α (TNF-α), cytokine-induced neutrophil chemoattractant (KC) and interleukin 10 (IL-10) levels were not changed. At later stages (24 h post-zymosan) a significant increase in PMNs was observed in MMP-9−/− mice, but not in the inhibitor-treated mice, in comparison to their respective controls. Moreover, intraperitoneal (i.p.) injection of recombinant mouse pro-MMP-9 induced leukocyte accumulation in peritoneum. Collectively, the findings indicate that Gelatinase B participates in leukocyte transmigration; however, its function can be compensated by other mechanisms.
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Chemokines and Gelatinases in the aqueous humor of patients with active uveitis.
American Journal of Ophthalmology, 2004Co-Authors: Ahmed M. Abu El-asrar, Sofie Struyf, Francis J Descamps, Saleh A. Al-obeidan, Paul Proost, Jozef Van Damme, Ghislain Opdenakker, Karel GeboesAbstract:Abstract Purpose To investigate the involvement of the chemokines CXCL10/IP-10, CXCL11/I-TAC, CXCL8/1L-8, CXCL6/GCP-2, CCL3/MIP-1α, and CCL18/PARC, and Gelatinases A and B in uveitis. Design Prospective, experimental, case-control study. Methods Aqueous humor samples from 30 patients with active uveitis, and 14 control patients and paired serum samples were assayed for chemokines with specific enzyme-linked immunosorbent assays (ELISAs) and for Gelatinase levels by quantitative zymography. Results In control AH, none of the chemokines was detected. Gelatinase A was detected in all samples, and Gelatinase B was detected in only one sample. In patients with uveitis, IP-10 was detected in all AH samples, whereas I-TAC, IL-8, GCP-2, MIP-1α, and PARC were detected in three, 16, six, two, and 12 samples, respectively. IP-10 levels were significantly higher in AH samples than those of serum ( P = .006). Gelatinase A was detected in 29 AH samples and Gelatinase B was detected in 26 samples. Gelatinase A levels were significantly higher in AH samples from patients than those of controls ( P r = .627; P r = .508; P = .002), Gelatinase B ( r = .685; P r = .595; P Conclusions These data suggest a pathogenic role of the T lymphocyte chemoattractant IP-10 and Gelatinases in the recruitment and activity of T cells into the eye in patients with uveitis and in the pathogenesis of uveitis.
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Gelatinase B in vernal keratoconjunctivitis.
Archives of Ophthalmology, 2001Co-Authors: Ahmed M. Abu El-asrar, Ilse Van Aelst, Samir M. Al-mansouri, Luc Missotten, Ghislain Opdenakker, Karel GeboesAbstract:Objectives To investigate the expression of Gelatinase B in the conjunctiva of patients with vernal keratoconjunctivitis (VKC) and the cellular source of this enzyme. Methods Conjunctival biopsy specimens from 12 patients with active VKC and 12 control subjects were studied using immunohistochemical techniques and a monoclonal antibody against Gelatinase B. The phenotype of Gelatinase B + inflammatory cells was examined using double immunohistochemical analysis and monoclonal antibodies against eosinophil peroxidase or macrophage CD68. Quantitative zymography was used to compare the activity of Gelatinase B in conjunctival biopsy specimens from 10 patients with active VKC and 7 control subjects. Results Gelatinase B was detected in a few polymorphonuclear cells in 8 control specimens. All VKC specimens showed Gelatinase B immunoreactivity in the epithelial and stromal inflammatory infiltrate. Compared with control specimens, VKC specimens showed significantly more Gelatinase B–positive cells (mean ± SD, 40.8 ± 29.9 vs 10.3 ± 2.4; P P Conclusions These findings suggest overexpression of Gelatinase B by eosinophils in VKC specimens and participation of Gelatinase B in the pathologic changes in VKC. Clinical Relevance Control of the release and/or activation of Gelatinase B in eosinophils may provide a new therapeutic strategy for treating VKC.
Norbert Pallua - One of the best experts on this subject based on the ideXlab platform.
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effect of oxidized regenerated cellulose collagen matrix on proteases in wound exudate of patients with diabetic foot ulcers
Journal of Wound Ostomy and Continence Nursing, 2011Co-Authors: Dietmar Ulrich, Michael Wöltje, Ralf Smeets, Frank Unglaub, Norbert PalluaAbstract:PURPOSE: The aim of this study was to investigate the influence of oxidized regenerated cellulose/collagen matrix on the concentration and activity of Gelatinases, elastase, and plasmin in wound exudate. SUBJECTS AND SETTING: The study included 32 patients with diabetic foot ulcers. Ten patients with a mean age of 66 ± 9 years (mean ± SD) were treated with hydrocolloid dressings; 22 patients with a mean age of 57 ± 12 years were treated with oxidized regenerated/collagen matrix and hydrocolloid dressings. METHODS: Wound exudate was collected on days 0, 5, 14, and every 14 days thereafter for 12 weeks. Total protein was determined according to Bradford's technique. The levels of elastase and plasmin were measured spectrofluorometrically. Besides, Gelatinase activity and matrix metalloproteinase-2 concentration were analyzed. The surface area of all ulcers was measured by planimetry. RESULTS: Patients treated with oxidized regenerated cellulose/collagen matrix showed a significant decrease in elastase, plasmin, and Gelatinase activities in wound exudates. The matrix metalloproteinase-2 concentration was significantly reduced on days 14, 28, 42, and 56 in comparison to day 0. Furthermore, wound size was significantly reduced at days 14 and 28 in oxidized regenerated cellulose/collagen matrix-treated patients (P <.05). CONCLUSION: Our results showed a significant and immediate reduction in the levels of all tested proteases in the wound exudate of diabetic foot ulcer patients treated with oxidized regenerated cellulose/collagen matrix. These patients also experienced a significantly greater reduction in wound size. Copyright
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Effect of oxidized regenerated cellulose/collagen matrix on proteases in wound exudate of patients with diabetic foot ulcers.
Journal of Wound Ostomy and Continence Nursing, 2011Co-Authors: Dietmar Ulrich, Michael Wöltje, Ralf Smeets, Frank Unglaub, Norbert PalluaAbstract:PURPOSE: The aim of this study was to investigate the influence of oxidized regenerated cellulose/collagen matrix on the concentration and activity of Gelatinases, elastase, and plasmin in wound exudate. SUBJECTS AND SETTING: The study included 32 patients with diabetic foot ulcers. Ten patients with a mean age of 66 ± 9 years (mean ± SD) were treated with hydrocolloid dressings; 22 patients with a mean age of 57 ± 12 years were treated with oxidized regenerated/collagen matrix and hydrocolloid dressings. METHODS: Wound exudate was collected on days 0, 5, 14, and every 14 days thereafter for 12 weeks. Total protein was determined according to Bradford's technique. The levels of elastase and plasmin were measured spectrofluorometrically. Besides, Gelatinase activity and matrix metalloproteinase-2 concentration were analyzed. The surface area of all ulcers was measured by planimetry. RESULTS: Patients treated with oxidized regenerated cellulose/collagen matrix showed a significant decrease in elastase, plasmin, and Gelatinase activities in wound exudates. The matrix metalloproteinase-2 concentration was significantly reduced on days 14, 28, 42, and 56 in comparison to day 0. Furthermore, wound size was significantly reduced at days 14 and 28 in oxidized regenerated cellulose/collagen matrix-treated patients (P
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Effect of oxidised regenerated cellulose/collagen matrix on proteases in wound exudate of patients with chronic venous ulceration
International Wound Journal, 2008Co-Authors: Ralf Smeets, Michael Wöltje, Frank Unglaub, Dietmar J O Ulrich, Norbert PalluaAbstract:: Oxidised regenerated cellulose/collagen matrix (ORC/collagen matrix) modifies wound microenvironments by binding and inactivating excess levels of proteases such as elastase, plasmin and Gelatinases in wound exudates. To compare levels of the Gelatinases matrix metalloproteinase 2 (MMP-2), elastase and plasmin in wound exudates collected from chronic venous insufficiency patients with venous leg ulcers treated with either an ORC/collagen matrix or a standard control therapy. During a 12-week treatment period, wound exudate samples were obtained from a control group of 10 patients treated with a hydrocolloid dressing and a treatment group of 17 patients treated with a combination of ORC/collagen matrix and hydrocolloid dressing. On admission and days 5, 14 and every subsequent 14th day, ulcers were photographed to determine healing rate and changes in ulcer appearance, and MMP-2 concentration and the Gelatinase, elastase and plasmin activities were analysed from wound exudates. The patients treated with ORC/collagen matrix showed a significant decrease in elastase, plasmin and gelastinase activity as compared with the control group, with no significant difference in the MMP-2 concentrations between the two groups. The results show a significant and immediate reduction in protease activity in wound exudates from venous leg ulcers treated with ORC/collagen.
Massimo Coletta - One of the best experts on this subject based on the ideXlab platform.
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the collagen binding domain of Gelatinase a modulates degradation of collagen iv by Gelatinase b
Journal of Molecular Biology, 2009Co-Authors: Magda Gioia, Christopher M Overall, Susanna Monaco, Philippe E Van Den Steen, Diego Sbardella, Giuseppe Grasso, Stefano Marini, Ghislain Opdenakker, Massimo ColettaAbstract:Summary Type IV collagen remodeling plays a critical role in inflammatory responses, angiogenesis and metastasis. Its remodeling is executed by a family of matrix metalloproteinases (MMPs), of which the constitutive Gelatinase A (MMP2) and the inducible Gelatinase B (MMP9) are key examples. Thus, in many pathological conditions, both Gelatinases act together. Kinetic data are reported for the enzymatic processing at 37 °C of type IV collagen from human placenta by MMP9 and its modulation by the fibronectin-like collagen binding domain (CBD) of MMP2. The α1 and α2 chain components of type IV collagen were cleaved by Gelatinases and identified by mass spectrometry as well as Edman sequencing. Surface plasmon resonance interaction assays showed that CBD bound type IV collagen at two topologically distinct sites. On the basis of linked-function analysis, we demonstrated that CBD of MMP2 tuned the cleavage of collagen IV by MMP9, presumably by inducing a ligand-linked structural change on the type IV collagen. At low concentrations, the CBD bound the first site and thereby allosterically modulated the binding of MMP9 to collagen IV, thus enhancing the collagenolytic activity of MMP9. At high concentrations, CBD binding to the second site interfered with MMP9 binding to collagen IV, acting as a competitive inhibitor. Interestingly, modulation of collagen IV degradation by inactive forms of MMP2 also occurred in a cell-based system, revealing that this interrelationship affected neutrophil migration across a collagen IV membrane. The regulation of the proteolytic processing by a catalytically inactive domain (i.e., CBD) suggests that the two Gelatinases might cooperate in degrading substrates even when either one is inactive. This observation reinforces the idea of exosite targets for MMP inhibitors, which should include all macromolecular substrate recognition sites.
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the collagen binding domain of Gelatinase a modulates degradation of collagen iv by Gelatinase b
Journal of Molecular Biology, 2009Co-Authors: Magda Gioia, Christopher M Overall, Susanna Monaco, Philippe E Van Den Steen, Diego Sbardella, Giuseppe Grasso, Stefano Marini, Ghislain Opdenakker, Massimo ColettaAbstract:Summary Type IV collagen remodeling plays a critical role in inflammatory responses, angiogenesis and metastasis. Its remodeling is executed by a family of matrix metalloproteinases (MMPs), of which the constitutive Gelatinase A (MMP2) and the inducible Gelatinase B (MMP9) are key examples. Thus, in many pathological conditions, both Gelatinases act together. Kinetic data are reported for the enzymatic processing at 37 °C of type IV collagen from human placenta by MMP9 and its modulation by the fibronectin-like collagen binding domain (CBD) of MMP2. The α1 and α2 chain components of type IV collagen were cleaved by Gelatinases and identified by mass spectrometry as well as Edman sequencing. Surface plasmon resonance interaction assays showed that CBD bound type IV collagen at two topologically distinct sites. On the basis of linked-function analysis, we demonstrated that CBD of MMP2 tuned the cleavage of collagen IV by MMP9, presumably by inducing a ligand-linked structural change on the type IV collagen. At low concentrations, the CBD bound the first site and thereby allosterically modulated the binding of MMP9 to collagen IV, thus enhancing the collagenolytic activity of MMP9. At high concentrations, CBD binding to the second site interfered with MMP9 binding to collagen IV, acting as a competitive inhibitor. Interestingly, modulation of collagen IV degradation by inactive forms of MMP2 also occurred in a cell-based system, revealing that this interrelationship affected neutrophil migration across a collagen IV membrane. The regulation of the proteolytic processing by a catalytically inactive domain (i.e., CBD) suggests that the two Gelatinases might cooperate in degrading substrates even when either one is inactive. This observation reinforces the idea of exosite targets for MMP inhibitors, which should include all macromolecular substrate recognition sites.
James P Quigley - One of the best experts on this subject based on the ideXlab platform.
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the isolation characterization and molecular cloning of a 75 kda Gelatinase b like enzyme a member of the matrix metalloproteinase mmp family an avian enzyme that is mmp 9 like in its cell expression pattern but diverges from mammalian Gelatinase b i
Journal of Biological Chemistry, 2000Co-Authors: Elizabeth Hahndantona, Ronald T Aimes, James P QuigleyAbstract:Abstract We have isolated a novel 75-kDa Gelatinase from a chicken macrophage cell line, HD11. Biochemical and immunological characterization of the purified enzyme demonstrated that it is distinct from the chicken 72-kDa Gelatinase A (MMP-2). The enzyme is capable of specific gelatin binding and rapid gelatin cleavage. Incubation with an organomercurial compound (p-aminophenylmercuric acetate) induces proteolytic processing and activation of this enzyme, and the resultant gelatinolytic activity is sensitive to both zinc chelators and tissue inhibitors of metalloproteinases. A full-length cDNA for the enzyme has been cloned, and sequence analysis demonstrated that the enzyme possesses the characteristic multidomain structure of an MMP Gelatinase including a cysteine switch prodomain, three fibronectin type II repeats, a catalytic zinc binding region, and a hemopexin-like domain. The 75-kDa Gelatinase is produced by phorbol ester-treated chicken bone marrow cells, monocytes, and polymorphonuclear leukocytes, cell types that charac- teristically produce the 92-kDa mammalian Gelatinase B (MMP-9). The absence of a 90–110-kDa Gelatinase in these cell types indicates that the 75-kDa Gelatinase is likely the avian counterpart of Gelatinase B. However, the protein is only 59% identical to human Gelatinase B, whereas all previously cloned chicken MMP homologues are 75–90% identical to their human counterparts. In addition, the new 75-kDa chicken Gelatinase lacks the type V collagen domain that is found in all mammalian Gelatinase Bs. Furthermore, the secreted enzyme appears structurally distinct from known Gelatinase Bs and the activated enzyme can cleave fibronectin, which is not a substrate for mammalian Gelatinase B. Thus the results of this study indicate that a second MMP Gelatinase exists in chickens, and although it is MMP-9/Gelatinase B-like in its overall domain structure and expression pattern, it appears to be biochemically divergent from mammalian Gelatinase B.
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matrix metalloproteinase 2 is an interstitial collagenase inhibitor free enzyme catalyzes the cleavage of collagen fibrils and soluble native type i collagen generating the specific and length fragments
Journal of Biological Chemistry, 1995Co-Authors: Ronald T Aimes, James P QuigleyAbstract:Abstract The 72-kDa Gelatinase/type IV collagenase (MMP-2) is a member of the matrix metalloproteinase (MMP) family of enzymes. This enzyme is known to cleave type IV collagen as well as degrade denatured collagens. However, native interstitial collagens are reportedly resistant to MMP-2 and are thought to be susceptible only to the interstitial collagenases MMP-1 and MMP-8. In this study we report that both human and chicken MMP-2, free of tissue inhibitors of metalloproteinases (TIMPs) are capable of cleaving soluble, triple helical type I collagen generating the ¾- and ¼-length collagen fragments characteristic of vertebrate interstitial collagenases. MMP-2 cleaves at the same Gly-Ile/Leu bond in the collagen α chains as interstitial collagenases with k and K values similar to that of MMP-1. MMP-2 also is capable of degrading reconstituted type I collagen fibrils. The closely related 92-kDa Gelatinase/type IV collagenase (MMP-9) is unable to cleave soluble or fibrillar collagen under identical conditions indicating that the specific collagenolytic activity of MMP-2 is not a general property of Gelatinases. That MMP-2, a potent Gelatinase, also can cleave fibrillar collagen provides an alternative to the proposal that two enzymes, an interstitial collagenase and a Gelatinase, are required for the complete dissolution of stromal collagen during cellular invasion.
Ralf Smeets - One of the best experts on this subject based on the ideXlab platform.
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effect of oxidized regenerated cellulose collagen matrix on proteases in wound exudate of patients with diabetic foot ulcers
Journal of Wound Ostomy and Continence Nursing, 2011Co-Authors: Dietmar Ulrich, Michael Wöltje, Ralf Smeets, Frank Unglaub, Norbert PalluaAbstract:PURPOSE: The aim of this study was to investigate the influence of oxidized regenerated cellulose/collagen matrix on the concentration and activity of Gelatinases, elastase, and plasmin in wound exudate. SUBJECTS AND SETTING: The study included 32 patients with diabetic foot ulcers. Ten patients with a mean age of 66 ± 9 years (mean ± SD) were treated with hydrocolloid dressings; 22 patients with a mean age of 57 ± 12 years were treated with oxidized regenerated/collagen matrix and hydrocolloid dressings. METHODS: Wound exudate was collected on days 0, 5, 14, and every 14 days thereafter for 12 weeks. Total protein was determined according to Bradford's technique. The levels of elastase and plasmin were measured spectrofluorometrically. Besides, Gelatinase activity and matrix metalloproteinase-2 concentration were analyzed. The surface area of all ulcers was measured by planimetry. RESULTS: Patients treated with oxidized regenerated cellulose/collagen matrix showed a significant decrease in elastase, plasmin, and Gelatinase activities in wound exudates. The matrix metalloproteinase-2 concentration was significantly reduced on days 14, 28, 42, and 56 in comparison to day 0. Furthermore, wound size was significantly reduced at days 14 and 28 in oxidized regenerated cellulose/collagen matrix-treated patients (P <.05). CONCLUSION: Our results showed a significant and immediate reduction in the levels of all tested proteases in the wound exudate of diabetic foot ulcer patients treated with oxidized regenerated cellulose/collagen matrix. These patients also experienced a significantly greater reduction in wound size. Copyright
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Effect of oxidized regenerated cellulose/collagen matrix on proteases in wound exudate of patients with diabetic foot ulcers.
Journal of Wound Ostomy and Continence Nursing, 2011Co-Authors: Dietmar Ulrich, Michael Wöltje, Ralf Smeets, Frank Unglaub, Norbert PalluaAbstract:PURPOSE: The aim of this study was to investigate the influence of oxidized regenerated cellulose/collagen matrix on the concentration and activity of Gelatinases, elastase, and plasmin in wound exudate. SUBJECTS AND SETTING: The study included 32 patients with diabetic foot ulcers. Ten patients with a mean age of 66 ± 9 years (mean ± SD) were treated with hydrocolloid dressings; 22 patients with a mean age of 57 ± 12 years were treated with oxidized regenerated/collagen matrix and hydrocolloid dressings. METHODS: Wound exudate was collected on days 0, 5, 14, and every 14 days thereafter for 12 weeks. Total protein was determined according to Bradford's technique. The levels of elastase and plasmin were measured spectrofluorometrically. Besides, Gelatinase activity and matrix metalloproteinase-2 concentration were analyzed. The surface area of all ulcers was measured by planimetry. RESULTS: Patients treated with oxidized regenerated cellulose/collagen matrix showed a significant decrease in elastase, plasmin, and Gelatinase activities in wound exudates. The matrix metalloproteinase-2 concentration was significantly reduced on days 14, 28, 42, and 56 in comparison to day 0. Furthermore, wound size was significantly reduced at days 14 and 28 in oxidized regenerated cellulose/collagen matrix-treated patients (P
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Effect of oxidised regenerated cellulose/collagen matrix on proteases in wound exudate of patients with chronic venous ulceration
International Wound Journal, 2008Co-Authors: Ralf Smeets, Michael Wöltje, Frank Unglaub, Dietmar J O Ulrich, Norbert PalluaAbstract:: Oxidised regenerated cellulose/collagen matrix (ORC/collagen matrix) modifies wound microenvironments by binding and inactivating excess levels of proteases such as elastase, plasmin and Gelatinases in wound exudates. To compare levels of the Gelatinases matrix metalloproteinase 2 (MMP-2), elastase and plasmin in wound exudates collected from chronic venous insufficiency patients with venous leg ulcers treated with either an ORC/collagen matrix or a standard control therapy. During a 12-week treatment period, wound exudate samples were obtained from a control group of 10 patients treated with a hydrocolloid dressing and a treatment group of 17 patients treated with a combination of ORC/collagen matrix and hydrocolloid dressing. On admission and days 5, 14 and every subsequent 14th day, ulcers were photographed to determine healing rate and changes in ulcer appearance, and MMP-2 concentration and the Gelatinase, elastase and plasmin activities were analysed from wound exudates. The patients treated with ORC/collagen matrix showed a significant decrease in elastase, plasmin and gelastinase activity as compared with the control group, with no significant difference in the MMP-2 concentrations between the two groups. The results show a significant and immediate reduction in protease activity in wound exudates from venous leg ulcers treated with ORC/collagen.