Biomolecular Interaction of Matrix Metalloproteinases and Their Inhibitors TIMPs
299
Knauper V, Wilhelm SM, Seperak PK, DeClerk YA, Langley KE, Osthues A, Tschesche H (l993) Direct
activation of human neutrophil pro collagenase by recombinant stromelysin. Biochem. J. 295:
581-586
Knauper V, Cowell S, Smith B, Lopez-Otin C, O'Shea M, Morris H, Zardi L, Murphy G (1997) The role
of the C-terminal domain of human collagenase-3 (MMP-13) in the activation of procollagease-3,
substrate specificity, and tissue inhibitor of metalloproteinase interaction. J. Bio!. Chern. 272:
7608-7616
Kolkenbrock H, Orgel D, Hecker-Kia A, Noack W, Ulbrich N (l991) The complex between a tissue
inhibitor of metalloproteinases (TIMP-2) and 72-kDa progelatinase is a metalloproteinase inhibitor. Eur. J. Biochem. 198: 775-781
Kolkenbrock H, Hecker-Kia A, Orgel D, Kinawi A, Ulbrich N (l996) Progelatinase B forms from
human neutrophils. Complex formation of monomer/lipocalin with TIMP-l. Bio!. Chern. 377:
529-533
Mallya SK, Mookhtiar KA, Gao Y, Brew K, Dioszegi M, Birkedal-Hansen H, Van Wart HE (l990) Characterization of 58-kilodalton human neutrophil collagenase: Comparison with human fibroblast
collagenase. Biochemistry 29: 10628-10634
Murphy G, Cockett MI, Stephens PE, Smith BJ, Docherty AJP (l987) Stromelysin is an activator of
procollagenase. Biochem. J. 248: 265-268
Murphy G, Houbrechts A, Cockett MI, Williamson RA, O'Shea M, Docherty AJ P (1991) The Nterminal domain of tissue inhibitor of metalloproteinases retains metalloproteinase inhibitory
activity. Biochemistry 30: 8102-8108
Nagase, H , Enghild J J , Suzuki K , Salvesen G (l990) Stepwise activation mechanism of the precursor
of matrix metalloproteinase 3 (stromelysin-I) by proteinases and (4-aminophenyl)mercuric acetate. Biochemistry 29: 5783-5789
Nagase H (l997) Activation mechanism of matrix metalloproteinases. Bio!. Chern. 378: 151-160
Nguyen Q, Willenbrock F, Cocket MI, O'Shea M, Docherty AJP, Murphy G (l994) Different domain
interactions are involved in the binding of tissue inhibitor of metalloproteinases to stromelysin-l
and gelatinase A. Biochemistry 33: 2089-2095
O'Shea M, Willenbrock F, Williamson RA, Crokett MI, Freedman RB, Reynolds JJ, Docherty AJ, Murphy G (l992) Site-directed mutations that alter the inhibitory activity of the tissue inhibitor of
metalloproteinases-1: importance of the N-terminal region between cysteine 3 and cysteine 13.
Biochemistry 31: 10146-10152
Pei D, Weiss SJ (l995) Furin-dependent intracellular activation of the human stromelysin-3 zymogen.
Nature 375: 244-247
Reinemer P, Grams F, Huber R, Kleine T, Schnierer S, Pieper M, Tschesche H, Bode W (l994) Structural implications for the role of the N terminus in the "superactivation" of collagenases. A crystallographic study. FEBS Letters 338: 227 -233
Sato H, Takino T, Kinoshita T, Imai K, Okada Y, Stevenson WG, Seiki M (l996a) Cell surface binding
and activation of gelatinase A induced by expression of membrane-type-l-matrix metalloproteinase (MTl-MMP). FEBS Letters 385: 238-240
Sato H, Kinoshita T, Takino T, Nakayama K, Seiki M (l996b) Activation of a recombinant membrane
type I-matrix metalloproteinase (MTl-MMP) by furin and ist interaction with tissue inhibitor of
metalloproteinases (TIMP)-2. FEBS Letters 393: 101-104
Schnierer S, Kleine T, Gote T, Hillemann A, Knauper V, Tschesche H (l993) The recombinant catalytic
domain of human neutrophil collagenase lacks type I collagenase activity. Biochem. Biophys. Res.
Commun. 191: 319-326
Springman EB, Angleton EL, Birkedal-Hansen H, Van Wart HE (l990) Multiple modes of activation of
latent human fibroblast collagenase: Evidence for the role of Cys73 active-site zinc complex in
latency and a "cysteine switch" mechanism for activation. Proc. Nat!. Acad. Sci. U.S.A. 87: 364-368
Suzuki K, Enghild JJ, Morodomi T, Salvesen G, Nagase H (l990) Mechanisms of activation of tissue
procollagenase by matrix metalloproteinase 3 (stromelysin). Biochemistry 29: 10261-10270
Tschesche H, Knauper V., Kramer S, Michaelis J, Oberhoff R, Reinke H (l992) Latent collagenase and
gelatinase from human neutrophils and their activation. In: Birkedal-Hansen H, Werb Z, Welgus H,
Van Wart H (eds) Matrix metalloproteinases and inhibitors. Gustav-Fischer Verlag, Stuttgart, New
York, Matrix Supplement 1: 245-255
Wilhelm SM, Collier JE, Marmer BL, Eisen AZ, Grant GA, Goldberg GJ (l989) SV-40 transformed
human lung fibroblasts secrete a 92-kDa type IV collagenase which is identical to that secreted by
normal human macrophages. J. Bio!. Chern. 264: 17213-17221
Willenbrock F, Crabbe T, Slocombe PM, Sutton CW, Docherty AJP, Cockett MI, O'Shea M, Brocklehurst K, Phillips IR, Murphy G (1993) The activity of the tissue inhibitors of metalloproteinases is
regulated by C-terminal domain interactions: A kinetic analysis of the inhibition of gelatinase A.
Biochemistry 32: 4330-4337
299
Knauper V, Wilhelm SM, Seperak PK, DeClerk YA, Langley KE, Osthues A, Tschesche H (l993) Direct
activation of human neutrophil pro collagenase by recombinant stromelysin. Biochem. J. 295:
581-586
Knauper V, Cowell S, Smith B, Lopez-Otin C, O'Shea M, Morris H, Zardi L, Murphy G (1997) The role
of the C-terminal domain of human collagenase-3 (MMP-13) in the activation of procollagease-3,
substrate specificity, and tissue inhibitor of metalloproteinase interaction. J. Bio!. Chern. 272:
7608-7616
Kolkenbrock H, Orgel D, Hecker-Kia A, Noack W, Ulbrich N (l991) The complex between a tissue
inhibitor of metalloproteinases (TIMP-2) and 72-kDa progelatinase is a metalloproteinase inhibitor. Eur. J. Biochem. 198: 775-781
Kolkenbrock H, Hecker-Kia A, Orgel D, Kinawi A, Ulbrich N (l996) Progelatinase B forms from
human neutrophils. Complex formation of monomer/lipocalin with TIMP-l. Bio!. Chern. 377:
529-533
Mallya SK, Mookhtiar KA, Gao Y, Brew K, Dioszegi M, Birkedal-Hansen H, Van Wart HE (l990) Characterization of 58-kilodalton human neutrophil collagenase: Comparison with human fibroblast
collagenase. Biochemistry 29: 10628-10634
Murphy G, Cockett MI, Stephens PE, Smith BJ, Docherty AJP (l987) Stromelysin is an activator of
procollagenase. Biochem. J. 248: 265-268
Murphy G, Houbrechts A, Cockett MI, Williamson RA, O'Shea M, Docherty AJ P (1991) The Nterminal domain of tissue inhibitor of metalloproteinases retains metalloproteinase inhibitory
activity. Biochemistry 30: 8102-8108
Nagase, H , Enghild J J , Suzuki K , Salvesen G (l990) Stepwise activation mechanism of the precursor
of matrix metalloproteinase 3 (stromelysin-I) by proteinases and (4-aminophenyl)mercuric acetate. Biochemistry 29: 5783-5789
Nagase H (l997) Activation mechanism of matrix metalloproteinases. Bio!. Chern. 378: 151-160
Nguyen Q, Willenbrock F, Cocket MI, O'Shea M, Docherty AJP, Murphy G (l994) Different domain
interactions are involved in the binding of tissue inhibitor of metalloproteinases to stromelysin-l
and gelatinase A. Biochemistry 33: 2089-2095
O'Shea M, Willenbrock F, Williamson RA, Crokett MI, Freedman RB, Reynolds JJ, Docherty AJ, Murphy G (l992) Site-directed mutations that alter the inhibitory activity of the tissue inhibitor of
metalloproteinases-1: importance of the N-terminal region between cysteine 3 and cysteine 13.
Biochemistry 31: 10146-10152
Pei D, Weiss SJ (l995) Furin-dependent intracellular activation of the human stromelysin-3 zymogen.
Nature 375: 244-247
Reinemer P, Grams F, Huber R, Kleine T, Schnierer S, Pieper M, Tschesche H, Bode W (l994) Structural implications for the role of the N terminus in the "superactivation" of collagenases. A crystallographic study. FEBS Letters 338: 227 -233
Sato H, Takino T, Kinoshita T, Imai K, Okada Y, Stevenson WG, Seiki M (l996a) Cell surface binding
and activation of gelatinase A induced by expression of membrane-type-l-matrix metalloproteinase (MTl-MMP). FEBS Letters 385: 238-240
Sato H, Kinoshita T, Takino T, Nakayama K, Seiki M (l996b) Activation of a recombinant membrane
type I-matrix metalloproteinase (MTl-MMP) by furin and ist interaction with tissue inhibitor of
metalloproteinases (TIMP)-2. FEBS Letters 393: 101-104
Schnierer S, Kleine T, Gote T, Hillemann A, Knauper V, Tschesche H (l993) The recombinant catalytic
domain of human neutrophil collagenase lacks type I collagenase activity. Biochem. Biophys. Res.
Commun. 191: 319-326
Springman EB, Angleton EL, Birkedal-Hansen H, Van Wart HE (l990) Multiple modes of activation of
latent human fibroblast collagenase: Evidence for the role of Cys73 active-site zinc complex in
latency and a "cysteine switch" mechanism for activation. Proc. Nat!. Acad. Sci. U.S.A. 87: 364-368
Suzuki K, Enghild JJ, Morodomi T, Salvesen G, Nagase H (l990) Mechanisms of activation of tissue
procollagenase by matrix metalloproteinase 3 (stromelysin). Biochemistry 29: 10261-10270
Tschesche H, Knauper V., Kramer S, Michaelis J, Oberhoff R, Reinke H (l992) Latent collagenase and
gelatinase from human neutrophils and their activation. In: Birkedal-Hansen H, Werb Z, Welgus H,
Van Wart H (eds) Matrix metalloproteinases and inhibitors. Gustav-Fischer Verlag, Stuttgart, New
York, Matrix Supplement 1: 245-255
Wilhelm SM, Collier JE, Marmer BL, Eisen AZ, Grant GA, Goldberg GJ (l989) SV-40 transformed
human lung fibroblasts secrete a 92-kDa type IV collagenase which is identical to that secreted by
normal human macrophages. J. Bio!. Chern. 264: 17213-17221
Willenbrock F, Crabbe T, Slocombe PM, Sutton CW, Docherty AJP, Cockett MI, O'Shea M, Brocklehurst K, Phillips IR, Murphy G (1993) The activity of the tissue inhibitors of metalloproteinases is
regulated by C-terminal domain interactions: A kinetic analysis of the inhibition of gelatinase A.
Biochemistry 32: 4330-4337