298
4
Acknowledgements
H. TSCHESCHE and M. FARR
We thank Dr. W. Jager and Dr. B. Haase (BIACORE AB) for supplying the BIAcore
instrument. The financial support by the SFBs 549 and 223 is greatly acknowledged.
References
Baragi VM, Fliszar CJ, Conroy MC, Ye QZ, Shipley JM, Welgus HG (1994) Contribution of the Cterminal domain of metalloproteinases to binding by tissue inhibitor of metalloproteinases. J. BioI.
Chern. 269: 12692-12697
Birkedal-Hansen H, Moore WGI, Bodden MK, Windsor LJ, Birkedal-Hansen, B, DeCarlo A, Engler JA
(1993) Matrix metalloproteinases: A review. Crit. Rev. Oral Bio!. Med. 4: 197-250
Blaser J, Knauper V, Osthues A, Reinke H, Tschesche H (1991) Mercurial activation of human polymorphonuclear leucocyte pro collagenase. Eur. J. Biochem. 202: 1223-1230
Bode W, Gomis-Riith FX, Stockier W (1993) Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc-binding environments (HEXXHXXGXXH and Met-turn) and topologies and should be grouped into a common family, the 'metzincins'. FEBS Letters 331(1,2): 134-140
Bode W, Reinemer P, Huber R, Kleine T, Schnierer S, Tschesche H (1994)The X-ray crystal structure
of the catalytic domain of human neutrophil collagenase inhibited by a substrate analogue reveals
the essentials for catalysis and specificity. EMBO J. 13: 1263-1269
Calvete JJ, Varela PF, Sanz L, Romero A, Mann K, Topfer-Petersen E (1996) A procedure for the largescale isolation of major bovine seminal plasma proteins. Prot. Exp. Purif. 8: 48-56
DeClerck YA, Yean TD, Lee Y, Tomich JM, Langley KE (1993) Characterization of the functional
domain of tissue inhibitor of metalloproteinases-2 (TIMP-2). Biochem. J. 289: 65-69
Fangerstam LG, O'Shannessy (1993) Handbook of affinity chromatography 63: 229-252, Marcel Dekker Inc.
Fernandez-Catalan C, Bode W, Huber R, Turk D, Calvete JJ, Lichte A, Tschesche H, Maskos K (1988)
Crystal structure of the complex formed by the membrane type I-matrix metalloproteinase with
the tissue inhibitor of metalloproteinases-2, the soluble progelatinase A receptor. The EMBO J. 17:
5238-5248
Goldberg GI, Barry LM, Marmer BL, Grant GA, Eisen AZ, Wilhelm S, He C (1989) Human 72-kDa
type IV collagenase forms a complex with a tissue inhibitor of metalloproteinases designated
T1MP-2. Proc. Nat!. Acad. Sci. USA 86: 8207-8211
Gomez DE, Alonso DF, Yoshiji H, Thorgeirsson UP (1997) Tissue inhibitors of metalloproteinases:
structure, regulation and biological functions. Eur. J. Cell Bio!. 74: 111-122
Gomis-Riith FX, Maskos K, Betz M, Bergner A, Huber R, Suzuki K, Yoshida N, Nagase H, Brew K,
Bourenkov GP, Bartunik H, Bode W (1997) Mechanism of inhibition of the human matrix metalloproteinase stromelysin-l by T1MP-l. Nature 389: 77-81
Grant GA, Eisen AZ, Marmer BL, Roswit WT, Goldberg GI (1987) The activation of human skin fibroblast procollagenase. Sequence identification of the major conversion products. J. Bio!. Chern. 262:
5886-5889
Hayakawa T (1994) Tissue inhibitors of metalloproteinases and their cell growth-promoting activity.
Cell Struct. Funct.19: 109-114
He C, Wilhelm SM, Pentland AP, Marmer BL, Grant GA, Eisen AZ, Goldberg GI (1989) Tissue cooperation in a proteolytic cascade activating human interstitial collagenase. Proc. Nat!. Acad. Sci. USA
86: 2632- 2636
Huang W, Suzuki K, Nagase H, Arumugam S, Van Doren SR, Brew K (1996) Folding and characterization of the amino-terminal domain of human tissue inhibitor of metalloproteinases-l (T1MP-l)
expressed at high yield in E. coli. FEBS Letters 384: 155-161
Jager W, Haase B, Lutz V, Herberg FW, Zimmermann B (1997) Biomolekulare Interaktionsanalyse
(BIA) mit SPR-Biosensortechnologie. Biospektrum 4/1997: 82-87
Jonsson U, Malmqvist M (1992) Real time biospecific interaction analysis. The integration of surface
plasmon resonance detection, general biospecific interface chemistry and microfluidics into one
analytical system. Advances in Biosensors 2: 291-336
Knauper V, Kramer S, Reinecke H, Tschesche H (1990) Characterization and activation of procollagenase from polymorphonuclear leucocytes. N-terminal sequence determination of the proenzyme
and various proteolytically active forms. Eur. J. Biochem. 189: 295-300
4
Acknowledgements
H. TSCHESCHE and M. FARR
We thank Dr. W. Jager and Dr. B. Haase (BIACORE AB) for supplying the BIAcore
instrument. The financial support by the SFBs 549 and 223 is greatly acknowledged.
References
Baragi VM, Fliszar CJ, Conroy MC, Ye QZ, Shipley JM, Welgus HG (1994) Contribution of the Cterminal domain of metalloproteinases to binding by tissue inhibitor of metalloproteinases. J. BioI.
Chern. 269: 12692-12697
Birkedal-Hansen H, Moore WGI, Bodden MK, Windsor LJ, Birkedal-Hansen, B, DeCarlo A, Engler JA
(1993) Matrix metalloproteinases: A review. Crit. Rev. Oral Bio!. Med. 4: 197-250
Blaser J, Knauper V, Osthues A, Reinke H, Tschesche H (1991) Mercurial activation of human polymorphonuclear leucocyte pro collagenase. Eur. J. Biochem. 202: 1223-1230
Bode W, Gomis-Riith FX, Stockier W (1993) Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc-binding environments (HEXXHXXGXXH and Met-turn) and topologies and should be grouped into a common family, the 'metzincins'. FEBS Letters 331(1,2): 134-140
Bode W, Reinemer P, Huber R, Kleine T, Schnierer S, Tschesche H (1994)The X-ray crystal structure
of the catalytic domain of human neutrophil collagenase inhibited by a substrate analogue reveals
the essentials for catalysis and specificity. EMBO J. 13: 1263-1269
Calvete JJ, Varela PF, Sanz L, Romero A, Mann K, Topfer-Petersen E (1996) A procedure for the largescale isolation of major bovine seminal plasma proteins. Prot. Exp. Purif. 8: 48-56
DeClerck YA, Yean TD, Lee Y, Tomich JM, Langley KE (1993) Characterization of the functional
domain of tissue inhibitor of metalloproteinases-2 (TIMP-2). Biochem. J. 289: 65-69
Fangerstam LG, O'Shannessy (1993) Handbook of affinity chromatography 63: 229-252, Marcel Dekker Inc.
Fernandez-Catalan C, Bode W, Huber R, Turk D, Calvete JJ, Lichte A, Tschesche H, Maskos K (1988)
Crystal structure of the complex formed by the membrane type I-matrix metalloproteinase with
the tissue inhibitor of metalloproteinases-2, the soluble progelatinase A receptor. The EMBO J. 17:
5238-5248
Goldberg GI, Barry LM, Marmer BL, Grant GA, Eisen AZ, Wilhelm S, He C (1989) Human 72-kDa
type IV collagenase forms a complex with a tissue inhibitor of metalloproteinases designated
T1MP-2. Proc. Nat!. Acad. Sci. USA 86: 8207-8211
Gomez DE, Alonso DF, Yoshiji H, Thorgeirsson UP (1997) Tissue inhibitors of metalloproteinases:
structure, regulation and biological functions. Eur. J. Cell Bio!. 74: 111-122
Gomis-Riith FX, Maskos K, Betz M, Bergner A, Huber R, Suzuki K, Yoshida N, Nagase H, Brew K,
Bourenkov GP, Bartunik H, Bode W (1997) Mechanism of inhibition of the human matrix metalloproteinase stromelysin-l by T1MP-l. Nature 389: 77-81
Grant GA, Eisen AZ, Marmer BL, Roswit WT, Goldberg GI (1987) The activation of human skin fibroblast procollagenase. Sequence identification of the major conversion products. J. Bio!. Chern. 262:
5886-5889
Hayakawa T (1994) Tissue inhibitors of metalloproteinases and their cell growth-promoting activity.
Cell Struct. Funct.19: 109-114
He C, Wilhelm SM, Pentland AP, Marmer BL, Grant GA, Eisen AZ, Goldberg GI (1989) Tissue cooperation in a proteolytic cascade activating human interstitial collagenase. Proc. Nat!. Acad. Sci. USA
86: 2632- 2636
Huang W, Suzuki K, Nagase H, Arumugam S, Van Doren SR, Brew K (1996) Folding and characterization of the amino-terminal domain of human tissue inhibitor of metalloproteinases-l (T1MP-l)
expressed at high yield in E. coli. FEBS Letters 384: 155-161
Jager W, Haase B, Lutz V, Herberg FW, Zimmermann B (1997) Biomolekulare Interaktionsanalyse
(BIA) mit SPR-Biosensortechnologie. Biospektrum 4/1997: 82-87
Jonsson U, Malmqvist M (1992) Real time biospecific interaction analysis. The integration of surface
plasmon resonance detection, general biospecific interface chemistry and microfluidics into one
analytical system. Advances in Biosensors 2: 291-336
Knauper V, Kramer S, Reinecke H, Tschesche H (1990) Characterization and activation of procollagenase from polymorphonuclear leucocytes. N-terminal sequence determination of the proenzyme
and various proteolytically active forms. Eur. J. Biochem. 189: 295-300