Advances in assays of matrix metalloproteinases (MMPs) and their inhibitors

Journal of Enzyme Inhibition and Medicinal Chemistry

Volumn 23, Issue 2, 2008, Pages 154-167

  Cheng, Xian Chao ^a   Fang, Hao ^a   Xu, Wen Fang ^a  

^a SHANDONG UNIVERSITY   (China)

Author keywords

Assays; Inhibitors; Matrix metalloproteinases

Indexed keywords

COLLAGENASE; FLUORESCEIN ISOTHIOCYANATE; GELATIN SUCCINATE; GELATINASE A; GELATINASE B; INTERSTITIAL COLLAGENASE; MATRILYSIN; MATRIX METALLOPROTEINASE; MATRIX METALLOPROTEINASE 20; MATRIX METALLOPROTEINASE INHIBITOR; NEUTROPHIL COLLAGENASE; PRINOMASTAT; STROMELYSIN; TISSUE INHIBITOR OF METALLOPROTEINASE 2;

BIOASSAY; BIOTINYLATION; CANCER PATIENT; DISEASE ACTIVITY; DRUG EFFICACY; DRUG IDENTIFICATION; DRUG SCREENING; ENZYME ACTIVITY; ENZYME DEGRADATION; ENZYME IMMUNOASSAY; ENZYME INHIBITION; ENZYME LINKED IMMUNOSORBENT ASSAY; ENZYME STRUCTURE; ENZYMOLOGY; FLUOROMETRY; HIGH THROUGHPUT SCREENING; HUMAN; HYDROLYSIS; MALIGNANT NEOPLASTIC DISEASE; MOLECULAR PROBE; NONHUMAN; OSTEOARTHRITIS; PHAGE DISPLAY; PRIORITY JOURNAL; PROTEIN ASSEMBLY; RADIOASSAY; REVIEW; TUMOR; WESTERN BLOTTING; ZYMOGRAPHY;

ANIMALS; BIOLOGICAL ASSAY; FLUOROMETRY; HUMANS; IMMUNOASSAY; MATRIX METALLOPROTEINASES; PROTEASE INHIBITORS; SUBSTRATE SPECIFICITY;

EID: 40949134163     PISSN: 14756366     EISSN: 14756374     Source Type: Journal    
DOI: 10.1080/14756360701511292     Document Type: Review

References (114)

1. Vihinen, P., Ala-aho, R. and Kähäri, VM (2005) Matrix metalloproteinases as therapeutic targets in cancer. Curr Cancer Drug Targets, 5, pp. 203-220.
2. Loftus, IM, Naylor, AR, Bell, PR and Thompson, MM (2002) Matrix metalloproteinases and atherosclerotic plaque instability. Br J Surg, 89, pp. 680-694.
3. Leppert, D., Lindberg, RLP, Kappos, L. and Leib, SL (2001) Matrix metalloproteinases: Multifunctional effectors of inflammation in multiple sclerosis and bacterial meningitis. Brain Res Rev, 36, pp. 249-257.
4. Nagase, H., Visse, R. and Murphy, G. (2006) Structure and function of matrix metalloproteinases and TIMPs. Cardiovasc Res, 69, pp. 562-573.
5. Mannello, F., Tonti, G. and Papa, S. (2005) Matrix metalloproteinase inhibitors as anticancer therapeutics. Curr Cancer Drug Targets, 5, pp. 285-298.
6. Lombard, C., Saulnier, J. and Wallach, J. (2005) Assays of matrix metalloproteinases (MMPs) activities: A review. Biochimie, 87, pp. 265-272.
7. Paemen, L., Martens, E., Norga, K., Masure, S., Roets, E., Hoogmartens, J. and Opdenakker, G. (1996) The gelatinase inhibitory activity of tetracyclines and chemically modified tetracycline analogues as measured by a novel microtiter assay for inhibitors. Biochem Pharmacol, 52, pp. 105-111.
8. Koritsas, VM and Atkinson, HJ (1995) An assay for detecting nanogram levels of proteolytic enzymes. Anal Biochem, 227, pp. 22-26.
9. Ratnikov, B., Deryugina, E., Leng, J., Marchenko, G., Dembrow, D. and Strongin, A. (2000) Determination of matrix metalloproteinase activity using biotinylated gelatin. Anal Biochem, 286, pp. 149-155.
10. Baragi, VM, Shaw, BJ, Renkiewicz, RR, Kuipers, PJ, Welgus, HG, Mathrubutham, M., Cohen, JR and Rao, SK (2000) A versatile assay for gelatinases using succinylated gelatin. Matrix Biology, 19, pp. 267-273.
11. Ratnikov, BI, Deryugina, EI and Strongin, AY (2002) Gelatin zymography and substrate cleavage assays of matrix metalloproteinase-2 in breast carcinoma cells overexpressing membrane type-1 matrix metalloproteinase. Lab Invest, 82:11, pp. 1583-1590.
12. Kleiner, DE and Stetler-Stevenson, WG (1994) Quantitative zymography: detection of picogram quantities of gelatinases. Anal Biochem, 218:2, pp. 325-329.
13. Leber, TM and Balkwill, FR (1997) Zymography: A single-step staining method for quantitation of proteolytic activity on substrate gels. Anal Biochem, 249, pp. 24-28.
14. Yu, W. and Woessner, JF (2001) Heparin-enhanced zymographic detection of matrilysin and collagenases. Anal Biochem, 293, pp. 38-42.
15. Gerlach, RF, Demacq, C., Jung, K. and Tanus-Santos, JE (2007) Rapid separation of serum does not avoid artificially higher matrix metalloproteinase (MMP)-9 levels in serum versus plasma. Clin Biochem, 40, pp. 119-123.
16. Souza-Tarla, CD, Uzuelli, JA, Machado, AA, Gerlach, RF and Tanus-Santos, JE (2005) Methodological issues affecting the determination of plasma matrix metalloproteinase (MMP)-2 and MMP-9 activities. Clin Biochem, 38, pp. 410-414.
17. Gerlach, RF, Uzuelli, JA, Souza-Tarla, CD and Tanus-Santos, JE (2005) Effect of anticoagulants on the determination of plasma matrix metalloproteinase (MMP)-2 and MMP-9 activities. Anal Biochem, 344, pp. 147-149.
18. Iijima, T., Minami, Y., Nakamura, N., Onizuka, M., Morishita, Y., Inadome, Y. and Noguchi, M. (2004) MMP-2 activation and stepwise progression of pulmonary adenocarcinoma: Analysis of MMP-2 and MMP-9 with gelatin zymography. Pathol Intern, 54, pp. 295-301.
19. Makowski, GS and Ramsby, ML (1996) Calibrating gelatin zymograms with human gelatinase standards. Anal Biochem, 236, pp. 353-356.
20. Croall, DE, Katherin, M. and Harold, H. (2002) Casein zymography of calpains using a 4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid-imidazole buffer. Anal Biochem, 304:1, pp. 129-132.
21. Resa, PF, Mira, E. and Quesada, AR (1995) Enhanced detection of casein zymography of matrix metalloproteinases. Anal Biochem, 224, pp. 434-435.
22. Gogly, B., Groult, N., Hornebeck, W., Godeau, G. and Pellat, B. (1998) Collagen zymography as a sensitive and specific technique for the determination of subpicogram levels of interstitial collagenase. Anal Biochem, 255, pp. 211-216.
23. Troeberg, L. and Nagase, H. (2003) Measurement of matrix metalloproteinase activities in the medium of cultured synoviocytes using zymography. Meth Mol Biol, 225, pp. 77-87.
24. Frederiks, WM and Mook, OR (2004) Metabolic mapping of proteinase activity with emphasis on in situ zymography of gelatinases: Review and protocols. J Histochem Cytochem, 52:6, pp. 711-722.
25. George, SJ and Johnson, JL (2001) In situ zymography. Meth Mol Biol, 151, pp. 411-415.
26. Kurschat, P., Wickenhauser, C., Groth, W., Krieg, T. and Mauch, C. (2002) Identification of activated matrix metalloproteinase-2 (MMP-2) as the main gelatinolytic enzyme in malignant melanoma by in situ zymography. J Pathol, 197:2, pp. 179-187.
27. Nemori, R., Yamamoto, M., Kataoka, F., Hashimoto, G., Arakatsu, H., Shiomi, T. and Okada, Y. (2005) Development of in situ zymography to localize active matrix metalloproteinase-7 (matrilysin-1). J Histochem Cytochem, 53:10, pp. 1227-1234.
28. Galis, ZS, Sukhova, GK and Libby, P. (1995) Microscopic localization of active proteases by in situ zymography: Detection of matrix metalloproteinase activity in vascular tissue. FASEB J, 9:10, pp. 974-980.
29. Mungall, BA and Pollitt, CC (2001) In situ zymography: Topographical considerations. J Biochem Biophys Meth, 47, pp. 169-176.
30. Oliver, GW, Leferson, JD, Stetler-Stevenson, WG and Kleiner, DE (1997) Quantitative reverse zymography: Analysis of picogram amounts of metalloproteinase inhibitors using gelatinase A and B reverse zymograms. Anal Biochem, 244, pp. 161-166.
31. Hawkes, SP, Li, H. and Taniguchi, GT (2001) Zymography and reverse zymography for detecting MMPs, and TIMPs. Meth Mol Biol, 151, pp. 399-410.
32. Hattori, S., Fujisaki, H., Kiriyama, T., Yokoyama, T. and Irie, S. (2002) Real-time zymography and reverse zymography: A method for detecting activities of matrix metalloproteinases and their inhibitors using FITC labeled collagen and casein as substrates. Anal Biochem, 301, pp. 27-34.
33. Watanabe, K. and Hattori, S. (2002) Real-time dual zymographic analysis of matrix metalloproteinases using fluorescein-isothiocyante-labeled gelatin and texas-red-labeled casein. Anal Biochem, 307, pp. 390-392.
34. Crawford, BD and Pilgrim, DB (2005) Ontogeny and regulation of matrix metalloproteinase activity in the zebrafish embryo by in vitro and in vivo zymography. Dev Biol, 286, pp. 405-414.
35. Bremer, C., Tung, CH and Weissleder, R. (2001) In vivo molecular target assessment of matrix metalloproteinase inhibition. Nat Med, 7, pp. 743-748.
36. Bawadi, HA, Antunes, TM, Shih, F. and Losso, JN (2004) In vitro inhibition of the activation of pro-matrix metalloproteinase 1 (pro-MMP-1) and pro-matrix metalloproteinase 9 (pro-MMP-9) by rice and soybean Bowman-Birk inhibitors. J Agric Food Chem, 52, pp. 4730-4736.
37. Verheijen, JH, Nieuwenbroek, NM, Beekman, B., Hanemaaijer, R., Verspaget, HW, Ronday, HK and Bakker, AH (1997) Modified proenzymes as artificial substrates for proteolytic enzymes: Colorimetric assay of bacterial collagenase and matrix metalloproteinase activity using modified pro-urokinase. Biochem J, 323:3, pp. 603-609.
38. Hanemaaijer, R., Visser, H., Kontiiner, Y., Koolwijk, P. and Verheijen, JH (1998) A novel and simple immunocapture assay for determination of getatinase-B (MMP-9) activities in biological fluids: Saliva from patients with Sjogren's syndrome contain increased latent and active gelatinase-B levels. Matrix Biology, 17, pp. 657-665.
39. Hanemaaijer, R., Sier, CF, Visser, H., Scholte, L., van Lent, N., Toet, K., Hoekman, K. and Verheijen, JH (1999) MMP-9 activity in urine from patients with various tumors, as measured by a novel MMP activity assay using modified urokinase as a substrate. Ann N Y Acad Sci, 878, pp. 141-149.
40. Capper, SJ, Verheijen, J., Smith, L., Sully, M., Visser, H. and Hanemaaijer, R. (1999) Determination of gelatinase-A (MMP-2) activity using a novel immunocapture assay. Ann N Y Acad Sci, 878, pp. 487-490.
41. Yoshida, D., Watanabe, K., Noha, M., Takahashi, H. and Teramoto, A. (2002) Suppression of matrix metalloproteinase activity by SI-27: Detection by a new activity assay with S-2444, a specific chromogenic peptide. J Neuro Oncol, 58, pp. 1-11.
42. Hao, JL, Nagano, T., Nakamura, M., Kumagai, N., Mishima, H. and Nishida, T. (1999) Effect of galardin on collagen degradation by pseudomonas aeruginosa. Exp Eye Res, 69, pp. 595-601.
43. Kurien, BT and Scofield, RH (2006) Western blotting. Methods, 38:4, pp. 283-293.
44. Enric, E., Trini, T., Manuel, R., Senén, V., Lluis, PJ and Maria, B. (2006) Use of western blotting filtration to detect UV-cross-linked protein: RNA complexes. Anal Biochem, 353:1, pp. 138-140.
45. Obata, K., Iwata, K., Okada, Y., Kohrin, Y., Ohuchi, E., Yoshida, S., Shinmei, M. and Hayakawa, T. (1992) A one-step sandwich enzyme immunoassay for human matrix metalloproteinase 3 (stromelysin-1) using monoclonal antibodies. Clin Chim Acta, 211:1, pp. 59-72.
46. Zhang, J., Fujimoto, N., Iwata, K., Sakai, T., Okada, Y. and Hayakawa, T. (1993) A one-step sandwich enzyme immunoassay for human matrix metalloproteinase 1 (interstitial collagenase) using monoclonal antibodies. Clin Chim Acta, 219:1, pp. 1-14.
47. Fujimoto, N., Mouri, N., Iwata, K., Ohuchi, E., Okada, Y. and Hayakawa, T. (1993) A one-step sandwich enzyme immunoassay for human matrix metalloproteinase 2 (72-kDa gelatinase/type IV collagenase) using monoclonal antibodies. Clin Chim Acta, 221:1, pp. 91-103.
48. Fujimoto, N., Zhang, J., Iwata, K., Shinya, T., Okada, Y. and Hayakawa, T. (1993) A one-step sandwich enzyme immunoassay for tissue inhibitor of metalloproteinases-2 using monoclonal antibodies. Clin Chim Acta, 220:1, pp. 31-45.
49. Ohuchi, E., Azumano, I., Yoshida, S., Iwata, K. and Okada, Y. (1996) A one-step sandwich enzyme immunoassay for human matrix metalloproteinase 7 (matrilysin) using monoclonal antibodies. Clinica Chimica Acta, 244, pp. 181-198.
50. Matsuki, H., Fujimoto, N., Iwata, K., Knauper, V., Okada, Y. and Hayakawa, T. (1996) A one-step sandwich enzyme immunoassay for human matrix metalloproteinase 8 (neutrophil collagenase) using monoclonal antibodies. Clinica Chimica Acta, 244, pp. 129-143.
51. Wang, T., Aoki, T., Iwata, K., Takata, T., Uchida, T., KnaÉuper, V., Llano, E., Okada, Y. and Bartlett, JD (2000) One-step sandwich enzyme immunoassay using monoclonal antibodies for detection of human enamelysin (MMP-20). Eur J Oral Sci, 108, pp. 530-537.
52. Aoki, T., Yonezawa, K., Ohuchi, E., Fujimoto, N., Iwata, K., Shimada, T., Shiomi, T., Okada, Y. and Seiki, M. (2002) Two-step sandwich enzyme immunoassay using monoclonal antibodies for detection of soluble and membrane-associated human membrane type 1-matrix metalloproteinase. J Immunoassay Immunochem, 23:1, pp. 49-68.
53. Bergmann, U., Michaelis, J., Oberhoff, R., Knäuper, V., Beckmann, R. and Tschesche, H. (1989) Enzyme linked immunosorbent assays (ELISA) for the quantitative determination of human leukocyte collagenase and gelatinase. J Clin Chem Clin Biochem, 27:6, pp. 351-359.
54. Yoshioka, H., Oyamada, I. and Usuku, G. (1987) An assay of collagenase activity using enzyme-linked immunosorbent assay for mammalian collagenase. Anal Biochem, 166:1, pp. 172-177.
55. Clark, IM, Powell, LK, Wright, JK, Cawston, TE and Hazleman, BL (1992) Monoclonal antibodies against human fibroblast collagenase and the design of an enzyme-linked immunosorbent assay to measure total collagenase. Matrix, 12:6, pp. 475-480.
56. Clark, IM, Wright, JK, Cawston, TE and Hazleman, BL (1992) Polyclonal antibodies against human fibroblast collagenase and the design of an enzyme-linked immunosorbent assay to measure TIMP-collagenase complex. Matrix, 12:2, pp. 108-115.
57. Clark, IM, Powell, LK, Ramsey, S., Hazleman, BL and Cawston, TE (1993) The measurement of collagenase, tissue inhibitor of metalloproteinases (TIMP), and collagenase-TIMP complex in synovial fluids from patients with osteoarthritis and rheumatoid arthritis. Arthritis Rheum, 36:3, pp. 372-379.
58. Plumpton, TA, Clark, IM, Plumpton, C., Calvin, J. and Cawston, TE (1995) Development of an enzyme-linked immunosorbent assay to measure total TIMP-1 (free TIMP-1 and TIMP-1 in combination with matrix-metalloproteinases) and measurement of TIMP 1 and CRP in serum. Clin Chim Acta, 240, pp. 137-154.
59. Walakovits, LA, Moore, VL, Bhardwaj, N., Gallick, GS and Lark, MW (1992) Detection of stromelysin and collagenase in synovial fluid from patients with rheumatoid arthritis and posttraumatic knee injury. Arthritis Rheum, 35:1, pp. 35-42.
60. Doughty, JR, Goldberg, RL, Ganu, V., Melton, RA, Hu, SI and Pasquale, G Di (1993) A stromelysin assay for the assessment of metalloprotease inhibitors on human aggregated proteoglycan. Agents Actions, 39, pp. 151-153.
61. Hollander, AP, Heathfield, TF, Webber, C., Iwata, Y., Bourne, R., Rorabeck, C. and Poole, AR (1994) Increased damage to type II collagen in osteoarthritic articular cartilage detected by a new immunoassay. J Clin Invest, 93:4, pp. 1722-1732.
62. Maliszewska, M., Mader, M., Scholl, U., Azeh, I., Hardeland, R., Felgenhauer, K., Beuche, W. and Weber, F. (2001) Development of an ultrasensitive enzyme immunoassay for the determination of matrix metalloproteinase-9 (MMP-9) levels in normal human cerebrospinal fluid. J Neuroimmunol, 116, pp. 233-237.
63. Lein, M., Nowak, L., Jung, K., Koenig, F., Lichtinghagen, R., Schnorr, D. and Loening, SA (1997) Analytical aspects regarding the measurement of metalloproteinases and their inhibitors in blood. Clin Biochem, 30:6, pp. 491-496.
64. Jung, K., Gerlach, RF and Tanus-Santos, JE (2006) Preanalytical pitfalls of blood sampling to measure true circulating matrix metalloproteinase 9 and tissue inhibitors of matrix metalloproteinases. Clin Chim Acta, 373, pp. 180-181.
65. Chu, Q., Lopez, M., Hayashi, K., Ionescu, M., Billinghurst, RC, Johnson, KA, Poole, AR and Markel, MD (2002) Elevation of a collagenase generated type II collagen neoepitope and proteoglycan epitopes in synovial fluid following induction of joint instability in the dog. Osteoarthritis Cartilage, 10:8, pp. 662-669.
66. Fosang, AJ, Stanton, H., Little, CB and Atley, LM (2003) Neoepitopes as biomarkers of cartilage catabolism. Inflamm Res, 52, pp. 277-282.
67. Ryzhakova, OS and Solov'eva, NI (2005) The assay of tissue collagenase activity using fluorescein isothiocyanate labeled collagen. Biomed Khim, 51:4, pp. 432-438.
68. Steven, FS and Lowther, DA (1975) Insoluble collagen II. The use of fluorescein labelled polymeric collagen fibrils in a very sensitive assay procedure for enzymes degrading insoluble collagen. Connect Tissue Res, 4:1, pp. 7-10.
69. Homer, KA and Beighton, D. (1990) Fluorometric determination of bacterial protease activity using fluorescein isothiocyanate-labeled proteins as substrates. Anal Biochem, 191:1, pp. 133-137.
70. St-Pierre, Y., Desrosiers, M., Tremblay, P., Estéve, PO and Opdenakker, G. (1996) Flow cytometric analysis of gelatinase B (MMP-9) activity using immobilized fluorescent substrate on microspheres. Cytometry, 25:4, pp. 374-380.
71. Kholodovich, VV, Kara, DI, Gershkovich, AA, Kibirev, VK, Karabut, LV, Klimenko, IV and Korneliuk, AI (1998) New donor-acceptor pairs for fluorogenic substrates with intramolecular fluorescence energy transfer for thrombin and trypsin. Bioorg Khim, 24:3, pp. 179-185.
72. Knight, CG (1995) Fluorimetric assays of proteolytic enzymes. Meth Enzymol, 248, pp. 18-34.
73. Gershkovich, AA and Kholodovych, VV (1996) Fluorogenic substrates for proteases based on intramolecular fluorescence energy transfer (IFETS). J Biochem Biophys Meth, 33:3, pp. 135-162.
74. Fields, GB (2001) Using fluorogenic peptide substrates to assay matrix metalloproteinases. Methods Mol Biol, 151, pp. 495-518.
75. Peppard, J., Pham, Q., Clark, A., Farley, D., Sakane, Y., Graves, R., George, J. and Norey, C. (2003) Development of an assay suitable for high-throughput screening to measure matrix metalloprotease activity. Assay Drug Dev Technol, 1:3, pp. 425-433.
76. Bickett, DM, Green, MD, Berman, J., Dezube, M., Howe, AS, Brown, PJ, Roth, JT and Mcgeehan, GM (1993) A high throughput fluorogenic substrate for interstitial collagenase (MMP-1) and gelatinase (MMP-9). Anal Biochem, 212:1, pp. 58-64.
77. Knight, CG, Willenbrock, F. and Murphy, G. (1992) A novel coumarin-labelled peptide for sensitive continuous assays of the matrix metalloproteinases. FEBS Lett, 296:3, pp. 263-266.
78. Netzel-Arnett, S., Mallya, SK, Nagase, H., Birkedal-Hansen, H. and Wart, HE (1991) Continuously recording fluorescent assays optimized for five human matrix metalloproteinases. Anal Biochem, 195:1, pp. 86-92.
79. Beekman, B., Drijfhout, JW, Bloemhoff, W., Ronday, HK, Tak, PP and TeKoppele, JM (1996) Convenient fluorometric assay for matrix metalloproteinase activity and its application in biological media. FEBS Lett, 390, pp. 221-225.
80. Beekman, B., El, B., Drijfhout, JW, Ronday, HK and TeKoppele, JM (1997) Highly increased levels of active stromelysin in rheumatoid synovial fluid determined by a selective fluorogenic assay. FEBS Lett, 418, pp. 305-309.
81. Neumann, U., Kubota, H., Frei, K., Ganu, V. and Leppert, D. (2004) Characterization of Mca-Lys-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2, a fluorogenic substrate with increased specificity constants for collagenases and tumor necrosis factor converting enzyme. Anal Biochem, 328, pp. 166-173.
82. George, J., Teear, ML, Norey, CG and Burns, DD (2003) Evaluation of an imaging platform during the development of a FRET protease assay. J Biomol Screen, 8:1, pp. 72-80.
83. Itoh, M., Osaki, M., Chiba, T., Masuda, K., Akizawa, T., Yoshioka, M. and Seiki, M. (1997) Flow injection analysis for measurement of activity of matrix metalloproteinase-7 (MMP-7). J Pharm Biomed Anal, 15, pp. 1417-1426.
84. Ambrose, WP, Semin, DJ, Robbins, DL, Orden, AV, Kashem, MA, Hamilton, SA, Nelson, RM, Jett, JH and Keller, RA (1998) Detection system for reaction-rate analysis in a low-volume proteinase-inhibition assay. Anal Biochem, 263, pp. 150-157.
85. Geoghegan, KF, Emery, MJ, Martin, WH, McColl, AS and Daumy, GO (1993) Site-directed double fluorescent tagging of human renin and collagenase (MMP-1) substrate peptides using the periodate oxidation of N-terminal serine. An apparently general strategy for provision of energy-transfer substrates for proteases. Bioconjugate Chem, 4, pp. 537-544.
86. Lauer-Fields, JL, Kele, P., Sui, G., Nagase, H., Leblanc, RM and Fields, GB (2003) Analysis of matrix metalloproteinase triple-helical peptidase activity with substrates incorporating fluorogenic L- or D-amino acids. Anal Biochem, 321, pp. 105-115.
87. Lauer-Fields, JL, Broder, T., Sritharan, T., Chung, L., Nagase, H. and Fields, GB (2001) Kinetic analysis of matrix metalloproteinase activity using fluorogenic triple-helical substrates. Biochemistry, 40, pp. 5795-5803.
88. Lauer-Fields, JL and Fields, GB (2002) Triple-helical peptide analysis of collagenolytic protease activity. Biol Chem, 383:7, pp. 1095-1105.
89. Terato, K., Nagai, Y., Kawanishi, K. and Yamamoto, S. (1976) A rapid assay method of collagenase activity using 14C-labeled soluble collagen as substrate. Biochim Biophys Acta, 445:3, pp. 753-762.
90. Cawston, TE and Barrett, AJ (1979) A rapid and reproducible assay for collagenase using [1-14C]acetylated collagen. Anal Biochem, 99:2, pp. 340-345.
91. Sunada, H. and Nagai, Y. (1980) A rapid micro-assay method for gelatinolytic activity using tritium-labeled heat-denatured polymeric collagen as a substrate and its application to the detection of enzymes involved in collagen metabolism. J Biochem(Tokyo), 87:6, pp. 1765-1771.
92. Gisslow, MT and McBride, BC (1975) A rapid sensitive collagenase assay. Anal Biochem, 68:1, pp. 70-78.
93. Brownell, J., Earley, W., Kunec, E., Morgan, BA, Olyslager, B., Wahl, RC and Houck, DR (1994) Comparison of native matrix metalloproteinases and their recombinant catalytic domains using a novel radiometric assay. Arch Biochem Biophys, 314:1, pp. 120-125.
94. Manicourt, DH and Lefebvre, V. (1993) An assay for matrix metalloproteinases and other proteases acting on proteoglycans, casein, or gelatin. Anal Biochem, 215:2, pp. 171-179.
95. Johnson-Wint, B. (1980) A quantitative collagen film collagenase assay for large numbers of samples. Anal Biochem, 104:1, pp. 175-181.
96. Dean, DD and Woessner, JF (1985) A sensitive, specific assay for tissue collagenase using telopeptide-free [3H] acetylated collagen. Anal Biochem, 148:1, pp. 174-181.
97. Matthews, DJ and Wells, JA (1993) Substrate phage: Selection of protease substrates by monovalent phage display. Science, 260:5111, pp. 1113-1117.
98. Ohkubo, S., Miyadera, K., Sugimoto, Y., Matsuo, K., Wierzba, K. and Yamada, Y. (1999) Identification of substrate sequences for membrane type-1 matrix metalloproteinase using bacteriophage peptide display library. Biochem Biophys Res Commun, 266, pp. 308-313.
99. Cwirla, SE, Peters, EA, Barrett, RW and Dower, WJ (1990) Peptides on phage: A vast library of peptides for identifying ligands. Proc Nati Acad Sci USA, 87, pp. 6378-6382.
100. Ding, L., Coombs, GS, Strandberg, L., Navre, M., Corey, DR and Madison, EL (1995) Origins of the specificity of tissue-type plasminogen activator. Proc Natl Acad Sci USA, 92, pp. 7627-7631.
101. Smith, MM, Shi, L. and Navre, M. (1995) Rapid identification of highly active and selective substrates for stromelysin and matrilysin using bacteriophage peptide display libraries. J Biol Chem, 270:12, pp. 6440-6449.
102. Deng, SJ, Bickett, DM, Mitchell, JL, Lambert, MH, Blackburn, RK, Carter 3rd, HL, Neugebauer, J., Pahel, G., Weiner, MP and Moss, ML (2000) Substrate specificity of human collagenase 3 assessed using a phage-displayed peptide library. J Biol Chem, 275:40, pp. 31422-31427.
103. Samoylova, TI, Morrison, NE, Globa, LP and Cox, NR (2006) Peptide phage display: Opportunities for development of personalized anti-cancer strategies. Anticancer Agents Med Chem, 6:1, pp. 9-17.
104. Matthias, P. (2006) Phage display systems and their applications. Appl Microbiol Biotechnol, 70:1, pp. 2-11.
105. Huber, D. and Beckwith, J. (2006) Phage display extends its reach. Nat Biotechnol, 24:7, pp. 793-794.
106. Rasmussen, FH, Yeung, N., Kiefer, L., Murphy, G., Lopez-Otin, C., Vitek, MP and Moss, ML (2004) Use of a multiple-enzyme/multiple-reagent assay system to quantify activity levels in samples containing mixtures of matrix metalloproteinases. Biochemistry, 43:11, pp. 2987-2995.
107. Saghatelian, A., Jessani, N., Joseph, A., Humphrey, M. and Cravatt, BF (2004) Activity-based probes for the proteomic profiling of metalloproteases. PNAS, 101:27, pp. 10000-10005.
108. Freije, JR, Klein, T., Ooms, JA, Franke, JP and Bischoff, R. (2006) Activity-based matrix metallo-protease enrichment using automated, inhibitor affinity extractions. J Proteome Res, 5, pp. 1186-1194.
109. Catterall, JB and Cawston, TE (2003) Assays of matrix metalloproteinases (MMPs) and MMP inhibitors: Bioassays and immunoassays applicable to cell culture medium, serum, and synovial fluid. Methods Mol Biol, 225, pp. 353-364.
110. Quesada, AR, Barbacid, MM, Mira, E., Fernández-Resa, P., Márquez, G. and Aracil, M. (1997) Evaluation of fluorometric and zymographic methods as activity assays for stromelysins and gelatinases. Clin Exp Metast, 15, pp. 26-32.
111. Zucker, S., Mancuso, P., DiMassimo, B., Lysik, RM, Conner, C. and Wu, CL (1994) Comparison of techniques for measurement of gelatinases/type IV collagenases: Enzyme-linked immunoassays versus substrate degradation assays. Clin Exp Metast, 12:1, pp. 13-23.
112. Baker, SN, Brauns, EB, McCleskey, TM, Burrell, AK and Baker, GA (2006) Fluorescence quenching immunoassay performed in an ionic liquid. Chem Commun (Camb), 27, pp. 2851-2853.
113. Yi, CF, Gosiewska, A., Burtis, D. and Geesin, J. (2001) Incorporation of fluorescent enzyme substrates in agarose gel for in situ zymography. Anal Biochem, 291:1, pp. 27-33.
114. Le, QT, Ohashi, A., Hirose, S. and Katunuma, N. (2005) Reverse zymography using fluorogenic substrates for protease inhibitor detection. Electrophoresis, 26:6, pp. 1038-1045.