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2012 | 59 | 4 | 679-684
Article title

Differential distribution of cathepsin b in human umbilical cord tissues

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The extracellular matrix components are differentially distributed among various structures of the umbilical cord. Wharton's jelly is especially rich in collagens and growth factors. Cathepsin B is a major cysteine protease involved in collagen degradation, as well as in the activation of precursor forms of other collagenolytic enzymes and growth factors. We assessed the activity and expression of cathepsin B in the umbilical cord arteries, veins and Wharton's jelly. Extracts of separated umbilical cord components were subjected to an activity assay with the use of specific fluorogenic substrate. The expression of cathepsin B protein was qualitatively evaluated by Western immunoblotting and quantitatively determined with an immunoenzymatic method. The total cathepsin B activity and content calculated per gram of DNA were higher in Wharton's jelly than in the umbilical cord vessels, and the latter parameter was the lowest in the umbilical cord arteries. Moreover, the expression and the activity of latent cathepsin B (following activation by pepsin digestion) calculated per gram of DNA were the highest in Wharton's jelly and the lowest in the umbilical cord arteries. High expression and activity of latent, pepsin-activatable cathepsin B related to DNA content in Wharton's jelly seem to reflect the stimulation of its cells by high amounts of collagen I and growth factors.
Physical description
  • Department of Medical Biochemistry, Medical Academy of Białystok, Białystok, Poland
  • Department of Medical Biochemistry, Medical Academy of Białystok, Białystok, Poland
  • Department of Medical Biochemistry, Medical Academy of Białystok, Białystok, Poland
  • Achkar C, Gong QM, Frankfater A, Bajkowski AS (1990) Differences in targeting and secretion of cathepsins B and L by BALB/3T3 fibroblasts and Moloney murine sarcoma virus-transformed BALB/3T3 fibroblasts. J Biol Chem 265: 13650-13654.
  • Andl CD, McCowan KM, Allison GL, Rustgi AK (2010) Cathepsin B is the driving force of esophageal cell invasion in a fibroblast-dependent manner. Neoplasia 12: 485-498.
  • Baici A, Lang A, Zwicky R, Müntener K (2005) Cathepsin B in osteoarthritis: uncontrolled proteolysis in the wrong place. Semin Arthritis Rheum 34: 24-28.
  • Bańkowski E (1999) Collagen of the umbilical cord and its alteration in EPH-gestosis (preeclampsia). Proc Indian Acad Sci (Chem Sci) 111: 207-213.
  • Bańkowski E, Romanowicz L, Jaworski S (1994) Alterations in collagen of umbilical cord arteries in patients with EPH-gestosis. Acta Biochim Pol 41: 170-173.
  • Barrett AJ, Kirschke H (1981) Cathepsin B, cathepsin H and cathepsin L. Methods Enzymol 80: 535-561.
  • Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248-254.
  • Cavallo-Medved D, Sloane BF (2003) Cell-surface cathepsin B: understanding its functional significance. Curr Top Dev Biol 54: 313-341.
  • Chan SJ, San Segundo B, McCormick MB, Steiner DF (1986) Nucleotide and predicted amino acid sequences of cloned human and mouse preprocathepsin B cDNAs. Proc Natl Acad Sci USA 83: 7721-7725.
  • Downs TR, Wilfinger WW (1983) Fluorometric quantification of DNA in cells and tissue. Anal Biochem 131: 538-547.
  • Eiján AM, Sandes EO, Riveros MD, Thompson S, Pasik L, Mallagrino H, Celeste F, Casabé AR (2003) High expression of cathepsin B in transitional bladder carcinoma correlates with tumor invasion. Cancer 98: 262-268.
  • Galewska Z, Bańkowski E, Romanowicz L, Gogiel T, Wolańska M, Jaworski S (2005) Preeclampsia-associated reduction of cathepsin D activity in the umbilical cord. Clin Chim Acta 351: 177-184.
  • Gogiel T, Bańkowski E, Jaworski S (2003) Proteoglycans of Wharton's jelly. Int J Biochem Cell Biol 35: 1461-1469.
  • Guo M, Mathieu PA, Linebaugh B, Sloane BF, Reiners JJ Jr (2002) Phorbol ester activation of a proteolytic cascade capable of activating latent transforming growth factor-β. A process initiated by the exocytosis of cathepsin B. J Biol Chem 277: 14829-14837.
  • Hamer I, Delaive E, Dieu M, Abdel-Sater F, Mercy L, Jadot M, Arnould T (2009) Up-regulation of cathepsin B expression and enhanced secretion in mitochondrial DNA-depleted osteosarcoma cells. Biol Cell 101: 31-41.
  • Hanewinkel H, Glössl J, Kresse H (1987) Biosynthesis of cathepsin B in cultured normal and I-cell fibroblasts. J Biol Chem 262: 12351-12355.
  • Hill T, Lewicki P (2007) STATISTICS: Methods and applications. StatSoft, Tulsa.
  • Jacob MP, Badier-Commander C, Fontaine V, Benazzoug Y, Feldman L, Michel JB (2001) Extracellular matrix remodeling in the vascular wall. Pathol Biol 49: 326-332.
  • Keppler D, Sloane BF (1996) Cathepsin B: Multiple enzyme forms from a single gene and their relation to cancer. Enzyme Protein 49: 94-105.
  • Kliman HJ (1998) Umbilical cord. In Encyclopedia of reproduction. Knobil E, Neill J, eds, vol 4, pp 585-596. Academic Press, New York.
  • Kobayashi K, Kubota T, Aso T (1998) Study on myofibroblast differentiation in the stroma cells of Wharton's jelly: expression and localization of alpha-smooth muscle actin. Early Hum Dev 51: 223-233.
  • Koblinski JE, Dosescu J, Sameni M, Moin K, Clark K, Sloane BF (2002) Interaction of human breast fibroblasts with collagen I increases secretion of procathepsin B. J Biol Chem 277: 32220-32227.
  • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685.
  • Lemaire R, Huet G, Zerimech F, Grard G, Fontaine C, Duquesnoy B, Flipo RM (1997) Selective induction of the secretion of cathepsins B and L by cytokines in synovial fibroblast-like cells. Br J Rheumatol 36: 735-743.
  • Mach L, Stüwe K, Hagen A, Ballaun C, Glössl J (1992) Proteolytic processing and glycosylation of cathepsin B. The role of the primary structure of the latent precursor and of the carbohydrate moiety for cell-type-specific molecular forms of the enzyme. Biochem J 282: 577-582.
  • Małkowski A, Sobolewski K, Jaworski S, Bańkowski E (2008) TGF-beta binding in human Wharton's jelly. Mol Cell Biochem 311: 137-143.
  • Mitchell KE, Weiss ML, Mitchell BM, Martin P, Davis D, Morales L, Helwig B, Beerenstrauch M, Abou-Easa K, Hildreth T, Troyer D, Medicetty S (2003) Matrix cells from Wharton's jelly form neurons and glia. Stem Cells 21: 50-60.
  • Moin K, Day NA, Sameni M, Hasnain S, Hirama T, Sloane BF (1992) Human tumour cathepsin B. Comparison with normal liver cathepsin B. Biochem J 285: 427-434.
  • Moles A, Tarrats N, Fernández-Checa JC, Marí M (2009) Cathepsins B and D drive hepatic stellate cell proliferation and promote their fibrogenic potential. Hepatology 49: 1297-1307.
  • Mort JS, Buttle DJ (1997) Cathepsin B. Int J Biochem Cell Biol 29: 715-720.
  • Mort JS, Recklies A, Poole R (1984) Extracellular presence of the lysosomal proteinase cathepsin B in rheumatoid synovium and its activity at neutral pH. Arthritis Rheum 27: 509-515.
  • Nanaev AK, Kohnen G, Milovanov AP, Domogatsky SP, Kaufmann P (1997) Stromal differentiation and architecture of the human umbilical cord. Placenta 18: 53-64.
  • Poręba W, Gawlik K, Gutowicz J (2002) Katepsyna B a proces inwazji nowotworowej. Postepy Biochem 48: 111-120 (Polish).
  • Qian F, Bajkowski AS, Steiner DF, Chan SJ, Frankfater A (1989) Expression of five cathepsins in murine melanomas of varying metastatic potential and normal tissues. Cancer Res 49: 4870-4875.
  • Reisenauer A, Eickelberg O, Wille A, Heimburg A, Reinhold A, Sloane BF, Welte T, Bühling F (2007) Increased carcinogenic potential of myeloid tumor cells induced by aberrant TGF-β1-signaling and upregulation of cathepsin B. Biol Chem 388: 639-650.
  • Romanov YA, Svintsitskaya VA, Smirnov VN (2003) Searching for alternative sources of postnatal human mesenchymal stem cells: candidate MSC-like cells from umbilical cord. Stem Cells 21: 105-110.
  • Romanowicz L, Sobolewski K (2000) Extracellular matrix components of the wall of umbilical cord vein and their alterations in pre-eclampsia. J Perinat Med 28: 140-146.
  • Ryan RE, Sloane BF, Sameni M, Wood PL (1995) Microglial cathepsin B: an immunological examination of cellular and secreted species. J Neurochem 65: 1035-1045.
  • Schmitt M, Jänicke F, Graeff H (1997) Tumor-associated proteases. Fibrinolysis 6 (Suppl 4): 3-26.
  • Skrzydlewska E, Sulkowska M, Koda M, Sulkowski S (2005) Proteolytic-antiproteolytic balance and its regulation in carcinogenesis. World J Gastroenterol 11: 1251-1266.
  • Sobolewski K, Bańkowski E, Chyczewski L, Jaworski S (1997) Collagen and glycosaminoglycans of Wharton's jelly. Biol Neonate 71: 11-21.
  • Sobolewski K, Małkowski A, Bańkowski E, Jaworski S (2005) Wharton's jelly as a reservoir of peptide growth factors. Placenta 26: 747-752.
  • Takechi K, Kuwabara Y, Mizuno M (1993) Ultrastructural and immunohistochemical studies of Wharton's jelly umbilical cord cells. Placenta 14: 235-245.
  • Wang HS, Hung SC, Peng ST, Huang CC, Wei HM, Guo YJ, Fu YS, Lai MC, Chen CC (2004) Mesenchymal stem cells in the Wharton's jelly of the human umbilical cord. Stem Cells 22: 1330-1337.
  • Weiss ML, Mitchell KE, Hix JE, Medicetty S, El-Zarkouny SZ, Grieger D, Troyer DL (2003) Transplantation of porcine umbilical cord matrix cells into the brain. Exp Neurol 182: 288-299.
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