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Number of results
2015 | 42 | 1 | 49-62

Article title

Charakterystyka elektroforetyczna aktywności metaloproteinazowej surowicy pacjentów z przewlekłą białaczką limfocytową – badania wstępne

Content

Title variants

EN
Electrophoretic characteristics of metalloproteinase’s activity of serum of patients with chronic lymphocytic leukemia – preliminary data

Languages of publication

EN

Abstracts

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.

Discipline

Year

Volume

42

Issue

1

Pages

49-62

Physical description

Contributors

author
  • 1Zakład Biochemii Farmaceutycznej i Diagnostyki Molekularnej z Pracownią Diagnostyki Molekularnej i Farmakogenomiki, Międzywydziałowa Katedra Diagnostyki Laboratoryjnej i Molekularnej, Wydział Farmaceutyczny, Uniwersytet Medyczny w Łodzi
  • 1Zakład Biochemii Farmaceutycznej i Diagnostyki Molekularnej z Pracownią Diagnostyki Molekularnej i Farmakogenomiki, Międzywydziałowa Katedra Diagnostyki Laboratoryjnej i Molekularnej, Wydział Farmaceutyczny, Uniwersytet Medyczny w Łodzi
  • 2Zakład Genetyki Klinicznej, Katedra Genetyki Klinicznej i Laboratoryjnej, Uniwersytet Medyczny w Łodzi
  • 1Zakład Biochemii Farmaceutycznej i Diagnostyki Molekularnej z Pracownią Diagnostyki Molekularnej i Farmakogenomiki, Międzywydziałowa Katedra Diagnostyki Laboratoryjnej i Molekularnej, Wydział Farmaceutyczny, Uniwersytet Medyczny w Łodzi

References

  • Dmoszyńska A, Robak T. Podstawy hematologii. Czelej, Lublin, 2008.
  • Szczeklik A. Choroby wewnętrzne. MP, Kraków, 2005.
  • Löffek S, Schilling O, Franzke CW. Biological role of matrix metalloproteinases: a critical balance. Eur Respir J. 2011; 38: 191–208.
  • Farina AR, Mackay AR. Gelatinase B/MMP–9 in Tumour Pathogenesis and Progression. Cancers. 2014; 6: 240–296.
  • Fink K, Boratyński J. Rola metaloproteinaz w modyfikacji macierzy zewnątrz–komórkowej w nowotworowym wzroście inwazyjnym, w przerzutowaniu i w angiogenezie. Postpy Hig Med. Dośw. 2012; 66: 609–628.
  • Kessenbrock K, Plaks V, Werb Z. Matrix metalloproteinases regulators of the tumor mocroenviroment. Cell. 2010; 141: 52–67.
  • Klein T, Bischoff R. Physiology and pathophysiology of matrix metalloproteases. Amino Acids. 2011; 41: 271–290.
  • Hidalgo M, Eckhardt SG. Development of Matrix Metalloproteinase Inhibitors in Cancer Therapy. J Natl Cancer Inst. 2001; 93: 178–193.
  • Yu XF, Han ZC. Matrix metalloproteinases in bone marrow: roles of gelatinases in physiological hematopoiesis and hematopoietic malignancies. Histol Histopathol. 2006; 21: 519–531.
  • Trocmé C, Gaudin P, Berthier S, Barro C, Zaoui P, Morel F. Human B Lymphocytes Synthesize the 92–kDa Gelatinase, Matrix Metalloproteinase–9. J Biol Chem. 1998; 273: 20677–20684.
  • Melamed D, Messika O, Glass–Marmor L, Miller A. Modulation of matrix metalloproteinase–9 (MMP–9) secretion in B lymphopoiesis. Int Immunol. 2006; 18:1355–1362.
  • D’Ascenzo S, Giusti I, Millimaggi D, Marci R, Tatone C, Cardigno Colonna R i wsp. Intrafollicular expression of matrix metalloproteinases and their inhibitors in normally ovulating women compared with patients undergoing in vitro fertilization treatment. Eur J Endocrinol. 2004; 151: 87–91.
  • Urbaniak J, Dybaś E, Krajewska M, Weyde W, Klinger M, Woźniak M. Ocena przydatności zymografii żelatynowej do oznaczania metaloproteinazy 9 (MMP–9) w osoczu krwi. Diag Lab. 2007; 43: 657–667.
  • Kamiguti AS, Lee ES, Till KJ, Harris RJ, Glenn MA, Lin K i wsp. The role of matrix metalloproteinase 9 in the pathogenesis of chronic lymphocytic leukemia. Br J Haematol. 2004; 125: 128–140.
  • Peak NJ, Foster HE, Khawaja K, Cawston TE, Rowan AD. Assessment of the clinical significance of gelatinase activity in patients with juvenile idiopathic arthritis using quantitative protein substrate zymography. Ann Rheum Dis. 2006; 65: 501–507.
  • Beckly Kelly EA, Busse WW, Jarjour NN. Increased matrix metalloproteinase–9 in the airway after allergen challenge. Am J Respir Crit Care Med. 2000; 162: 1157–1161.
  • Molica S, Vitelli G, Levato D, Giannarelli D, Vacca A, Cuneo A i wsp. Increased serum levels of matrix metalloproteinase–9 predict clinical outcome of patients with early B–cell chronic lymphocytic leukaemia. Eur J Haematol. 2003; 70: 373–378.
  • Chen S, Meng F, Chen Z, Tomlinson BN, Wesley JM, Sun GY i wsp. Two dimensional zymography differentiates gelatinase isoforms in stimulated microglial cells and in brain tissues of acute brain injuries. PLoS One. 2015; 10(4): e0123852, doi: 10.1371/journal.pone.0123852 (dostęp od 10.04.2015).

Document Type

paper

Publication order reference

Identifiers

YADDA identifier

bwmeta1.element.psjd-03ad88da-7573-401b-b652-05626190478f
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