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Concentration of Gelatinases and Their Tissue Inhibitors in Pancreatic Inflammatory and Neoplastic Tumors and Their Influence on the Early Postoperative Course

100%
Lekstan A., Olakowski M., Jabłońska B., Łabuzek K., Olakowska E., Filip I., Lampe P.
Polish Journal of Surgery
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2013
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vol. 85
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issue 2
65-72
EN
Pancreatic cancer (PC) is the fourth leading cause of death in the world, due to neoplastic disease. Chronic pancreatitis (CP) is a progressive disease leading towards pancreatic fibrosis. The aim of the study was to assess the impact of matrix metalloproteinases 2 and 9 (MMP2 and 9) and their tissue inhibitor (TIMP 1 and 2) concentrations in case of PC and CP tissue homogenates on early treatment results of patients subject to pancreatic resections. Material and methods. The study group comprised 63 patients, including 25 (39.68%) female and 38 (60.32%) male patients. Group 1 (CP) consisted of 31 patients with CP (F: M = 10/21). Group 2 (PC) consisted of 32 patients with PC (F: M = 15:17). The pancreatic tumor samples were collected from the resected pancreas, being subject to electrophoresis and immunoenzymatic studies. After confirming their activity, MMP2, MMP9, TIMP1, TIMP2 concentrations were determined. Correlation analysis of MMPs and TIMPs concentrations was performed in relation to the following: tumor diameter, age, BMI, hospitalization, duration of symptoms and surgery, blood loss, incidence of perioperative complications. Results. Group differences were presented in terms of: age, BMI, ASA, duration of symptoms, jaundice, tumor diameter, time of operation. There were no differences considering weight loss, blood loss, extent of resection, and hospitalization. Significant MMPs and TIMPs concentration differences between groups were demonstrated. Conclusions. Comparison of PC to CP tissue samples showed significantly higher levels of metalloproteinases and TIMPs in the former. Positive correlations of MMP1, TIMP1 and 2 with tumor diameter (CP) were observed, and MMP2 with the duration of surgery and blood loss (PC). There was no MMPs and TIMPs concentration levels influence on the incidence of postoperative complications.
2
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Collagenases and gelatinases in bone healing. The focus on mandibular fractures

72%
Kurzepa J., Baran M., Watroba S., Barud M., Babula D.
Current Issues in Pharmacy and Medical Sciences
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2014
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vol. 27
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issue 2
121-126
EN
Due to high amount of collagen fibres in the structure of bone, the enzymes capable of collagen digestion play a key role in bone remodelling. Matrix metalloproteinases (MMPs), prevailing extracellular endopeptideses, can digest extracellularly located proteins, e.g. collagen, proteoglycans, elastin or fibronectin. Among MMPs, collagenases (MMP-1, MMP-8 and MMP-13) and gelatinases (MMP-2 and MMP-9) can cleave collagen particles to forms that are able to undergo further steps of catabolism intracellularly. In addition, activity of the gelatinases (as an activation of proinflammatory cytokines) facilitates spreading inflammation that is necessary during the first stage of bone healing. Further studies related to the role of various MMPs in mandibular fractures should precisely explain their function in the bone healing and evaluate the influence of MMPs inhibitors on that process. This review provides the basic information about two groups among MMPs family, collagenases and gelatinases, and their role in repairing processes after mandibular fractures.
3
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Charakterystyka elektroforetyczna aktywności metaloproteinazowej surowicy pacjentów z przewlekłą białaczką limfocytową – badania wstępne

58%
Pietrzak J., Wodziński D., Franiak-Pietryga I., Mirowski M.
Folia Medica Lodziensia
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2015
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vol. 42
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issue 1
49-62
EN
Metalloproteinases play an important role in the development and metastasis of many cancers. Their activity is also an important component of tumorgenesis associated processes such as angiogenesis, decreased apoptosis, or unlimited proliferation of pathological cells. In this study we tried to estimate a differences of metalloproteinase activity digesting the gelatin in the sera of patients with chronic lymphocytic leukemia and healthy people, by the zymographic technique. To confirm that the gelatinolytic activity originated from the metalloproteinases their specific inhibitors: phenanthroline and ethylene– diaminetetraacetic acid were used. In patient’s sera a zymographic analysis revealed the presence of additional activity. The first of them are located in a region corresponding to a molecular weight of approximately 240 kDa, probably corresponds to the dimer of proMMP–9. Another two active fractions present in the sera of patients suffering from leukemia corresponded to a molecular weight of about 110 and 130 kDa probably represents a complex of proMMP–9 with lipocain. In a control sera, only one activity could be observed exhibiting a molecular weight of about 110 kDa, which is stronger than corresponding fraction in patient’s sera. The biggest difference between the two investigated sera was gelatynolytic activity located in the region of a molecular weight of about 94 kDa, which probably corresponded to proMMP–9. In some leukemic sera this activity was several times higher compared to the control samples, in which there was a constant and relatively low level of it. Despite significant activity of proMMP–9 in sera of patients with CLL no biologically active equivalent band of molecular weight 84 kDa were detected. The fractions which corresponded to different forms of MMP–2 (72, 64 kDa) were present in the sera of tumor and control, although proMMP–2 was more strongly expressed in the control samples.
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