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Papadopoulou, S., Scorilas, A., Arnogianaki, N., Papapanayiotou, B., Tzimogiani, A., Agnantis, N. and Talieri, M. (2001) Expression of gelatinase-A (MMP-2) in human colon cancer and normal colon mucosa. Tumor Biology, 22, 383-389. doi:10.1159/000050641 PMid:11786732

has been cited by the following article:

• TITLE: Cooperative binding of calcium ions modulates the tertiary structure and catalytic activity of Matrix-Metalloproteinase-9

  AUTHORS: Shakila Tobwala, D. K. Srivastava

  KEYWORDS: Matrix Metalloproteinase-9; Gelatinase-B; Fluorescence Lifetime; Quenching; Acrylamide; Stern-Volmer Constant

  JOURNAL NAME: Advances in Enzyme Research, Vol.1 No.2, June 20, 2013

  ABSTRACT: To ascertain the molecular basis of Ca2+-mediated activation of matrix metalloproteinase-9 (MMP-9), we determined the accessibility of tryptophan residues to externally added acrylamide as quencher in the absence and presence of the metal ion. The steady-state and time resolved fluorescence data revealed that MMP-9 possesses two classes of tryptophan residues, “exposed” and “buried” which are quenched by the collisional rate constants (kq) of 3.2′ 109M-1.s-1 and 7.5′ 108M-1.s-1, respectively. These values are impaired by approximately two and three-fold, respectively, in the presence of 10 mM Ca2+. The Stern-Volmer constants (Ksv values) predicted from the time resolved fluorescence data (in the absence of Ca2+ ) satisfied the dynamic quenching model of the enzyme’s tryptophan residues. This was not the case in the presence of Ca2+ ; the steady-state acrylamide quenching data could only be explained by a combination of “dynamic” and “static” quenching models. A cumulative account of these data led to the suggestion that the binding of Ca2+ modulated the tertiary structure of the protein by decreasing the dynamic flexibility of the enzyme, which is manifested in further structuring of the enzyme’s active site pocket toward facilitating catalysis. Arguments are presented that the binding of Ca2+ at distal sites “dynamically” communicates with the active site residues of MMP-9 during catalysis.