Searched for: subject%3A%22Enzyme%255C%2BPrecursors%22
(1 - 10 of 10)
document
Beklen, A. (author), Tüter, G. (author), Sorsa, T. (author), Hanemaaijer, R. (author), Virtanen, I. (author), Tervahartiala, T. (author), Konttinen, Y.T. (author)
Activated matrix metalloproteinase-3 (MMP-3) can contribute to periodontal ligament destruction in adult periodontitis. Since MMP-3 has been reported to activate proMMP-8 and -9, it was speculated that gingival tissue fibroblast-derived MMP-3 might, in periodontitis, be responsible for activation of gingival crevicular fluid (GCF) neutrophil...
article 2006
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TNO Kwaliteit van Leven (author), Verheijen, J.H. (author), Huisman, L.G.M. (author), van Lent, N. (author), Neumann, U. (author), Paganetti, P. (author), Erik Hack, C. (author), Bouwman, F. (author), Lindeman, J. (author), Bollen, E.L.E.M. (author), Hanemaaijer, R. (author)
Background: Formation of deposits of the insoluble amyloid β-peptide is believed to be causally related with neurodegeneration in Alzheimer disease (AD). The β-peptide originates from a larger amyloid precursor protein (APP) by the action of proteolytic enzymes. The first proteolytic event leading to amyloid formation is the cleavage of APP by...
article 2006
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Gaubius Instituut TNO (author), Tchetverikov, I. (author), Ronday, H.K. (author), van El, B. (author), Kiers, G.H. (author), Verzijl, N. (author), TeKoppele, J.M. (author), Huizinga, T.W.J. (author), de Groot, J. (author), Hanemaaijer, R. (author)
Objective: To analyse matrix metalloproteinases (MMPs) and tissue inhibitor-1 of MMPs (TIMP-1) levels in the systemic circulation and synovial fluid (SF) of patients with RA and to compare these levels with inflammatory and collagen degradation markers. Methods: ProMMP-1, -2, -3, -8, -9, TIMP-1, levels of MMP/ α2-macroglobulin complexes, and...
article 2004
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Heikkilä, P. (author), Teronen, O. (author), Hirn, M.Y. (author), Sorsa, T. (author), Tervahartiala, T. (author), Salo, T. (author), Konttinen, Y.T. (author), Halttunen, T. (author), Moilanen, M. (author), Hanemaaijer, R. (author), Laitinen, M. (author)
Background. Bisphosphonates reduce the bone metastasis formation and angiogenesis but the exact molecular mechanisms involved are unclear. Progelatinase A (proMMP-2; 78 KDa) is activated up during the tumor spread and metastasis by a cell surface-associated matrix metalloproteinase (membrane-type matrix metalloproteinase [MT1-MMP] or MMP-14)....
article 2003
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de Groot, J. (author), Verzijl, N. (author), Budde, M. (author), Bijlsma, J.W.J. (author), Lafeber, F.P.J.G. (author), TeKoppele, J.M. (author), Gaubius Instituut (author)
The integrity of the collagen network is essential for articular cartilage to fulfill its function in load support and distribution. Damage to the collagen network is one of the first characteristics of osteoarthritis. Since extensive collagen damage is considered irreversible, it is crucial that chondrocytes maintain a functional collagen...
article 2001
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Centraal Instituut voor Voedingsonderzoek TNO TNO Voeding (author), Conesa, A. (author), Weelink, G. (author), van den Hondel, C.A.M.J.J. (author), Punt, P.J. (author)
The Caldariomyces fumago chloroperoxidase (CPO) is synthesised as a 372-aa precursor which undergoes two proteolytic processing events: removal of a 21-aa N-terminal signal peptide and of a 52-aa C-terminal propeptide. The Aspergillus niger expression system developed for CPO was used to get insight into the function of this C-terminal...
article 2001
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Gaubius Instituut TNO (author), Verheijen, J.H. (author), Nieuwenbroek, N.M.E. (author), Beekman, B. (author), Hanemaaijer, R. (author), Verspaget, H.W. (author), Ronday, K.H. (author), Bakker, A.H.F. (author)
We describe a new principle for assessment of the activity of proteolytic enzymes of all classes and show the application of this principle for the quantitative assay of bacterial collagenase and human matrix metalloproteinases (MMPs). Central to this new principle is the presence of a proenzyme that can be activated into an active enzyme by a...
article 1997
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de Munk, G.A.W. (author), Molinari, A. (author), Rijken, D.C. (author), Gaubius Laboratory Netherlands Instituut voor verouderings- en vaatziekten onderzoek TNO (author)
Chemicals/CAS: amino acid, 65072-01-7; prourokinase, 82657-92-9; thrombin, 9002-04-4; thrombomodulin, 112049-68-0; Enzyme Precursors; Receptors, Cell Surface; Receptors, Thrombin; saruplase, 99149-95-8; Thrombin, EC 3.4.21.5; Urinary Plasminogen Activator, EC 3.4.21.73
article 1993
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Rijken, D.C. (author), Groeneveld, E. (author), Gaubius Instituut TNO (author)
Recent studies suggest that plasminogen activators not only hydrolyse a specific arginine-valine bond in plasminogen, but may also cleave other proteins such as fibronectin. We studied the substrate specificity, particularly the preference for arginyl over lysyl peptide bonds, of tissue-type plasminogen activator (t-PA) as well as of two-chain...
article 1991
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Binnema, D.J. (author), Dooijewaard, G. (author), van Iersel, J.J.L. (author), Turion, P.N.C. (author), Kluft, C. (author), Gaubius Instituut TNO (author)
Apart from tissue-type plasminogen activator (t-PA) and urokinase-type plasminogen activator (u-PA), a third PA appears to occur in human plasma. Its activity is initiated when appropriate triggers of the contact system are added, and the activation depends on the presence of factor XII and prekallikrein in plasma. The activity of this, so...
article 1990
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