메뉴 건너뛰기




Volumn 18, Issue 4, 1999, Pages 403-411

The proteolytic activity and cleavage specificity of fibronectin- gelatinase and fibronectin-lamininase

Author keywords

2 macroglobulin; Fibronectin; FN gelatinase; FN lamininase; Retroviral aspartic proteinases

Indexed keywords

ALPHA 2 MACROGLOBULIN; ASPARTIC PROTEINASE; FIBRONECTIN; GELATINASE;

EID: 0032774325     PISSN: 02778033     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1020684508212     Document Type: Article
Times cited : (12)

References (40)
  • 1
    • 0028808210 scopus 로고
    • Fibronectin and integrins in invasion and metastasis
    • Akiyama, S. K., Olden, K., and Yamada, K. M. (1995). Fibronectin and integrins in invasion and metastasis. Cancer Metast. Rev. 14, 173-189.
    • (1995) Cancer Metast. Rev. , vol.14 , pp. 173-189
    • Akiyama, S.K.1    Olden, K.2    Yamada, K.M.3
  • 2
    • 0018377938 scopus 로고
    • Isolation of a collagen-binding fragment from fibronectin and cold-insoluble globulin
    • Balian, G., Click, E. M., Crouch, E., Davidson, J. M., and Bornstein, P. (1979). Isolation of a collagen-binding fragment from fibronectin and cold-insoluble globulin. J. Biol. Chem. 254, 1429-1432.
    • (1979) J. Biol. Chem. , vol.254 , pp. 1429-1432
    • Balian, G.1    Click, E.M.2    Crouch, E.3    Davidson, J.M.4    Bornstein, P.5
  • 4
    • 0026546935 scopus 로고
    • Fibronectin fragments stimulate tumor necrosis factor secretion by human monocytes
    • Beezold, D. H., and Personius, C. (1992), Fibronectin fragments stimulate tumor necrosis factor secretion by human monocytes. J. Leukoc. Biol. 51, 59-64.
    • (1992) J. Leukoc. Biol. , vol.51 , pp. 59-64
    • Beezold, D.H.1    Personius, C.2
  • 5
    • 0030573971 scopus 로고    scopus 로고
    • Fibronectin fragments induce the expression of stromelysin-1 mRNA and protein in bovine chondrocytes in monolayer culture
    • Bewsey, K. E., Wen, C., Purple, C., and Homandberg, G. A. (1996). Fibronectin fragments induce the expression of stromelysin-1 mRNA and protein in bovine chondrocytes in monolayer culture. Biochem. Biophys. Acta 1317, 55-64.
    • (1996) Biochem. Biophys. Acta , vol.1317 , pp. 55-64
    • Bewsey, K.E.1    Wen, C.2    Purple, C.3    Homandberg, G.A.4
  • 6
    • 0021321955 scopus 로고
    • A rapid, sensitive method for detection of alkaline phosphatase conjugated anti-antibody on Western blots
    • Blake, M. S., Johnston, K. H., Russell-Jones, G. J., and Gotschlich, E. C. (1984). A rapid, sensitive method for detection of alkaline phosphatase conjugated anti-antibody on Western blots. Anal. Biochem. 136, 175-179.
    • (1984) Anal. Biochem. , vol.136 , pp. 175-179
    • Blake, M.S.1    Johnston, K.H.2    Russell-Jones, G.J.3    Gotschlich, E.C.4
  • 8
    • 0020679024 scopus 로고
    • Transformation-enhancing activity in plasma of tumor patients, relationship with fibronectin fragments
    • De Petro, G., Barlati, S., Vartio, T., and Vaheri, A. (1983). Transformation-enhancing activity in plasma of tumor patients, relationship with fibronectin fragments. Int. J. Cancer 31, 157-162.
    • (1983) Int. J. Cancer , vol.31 , pp. 157-162
    • De Petro, G.1    Barlati, S.2    Vartio, T.3    Vaheri, A.4
  • 10
    • 0021415850 scopus 로고
    • The synthesis, purification, and evaluation of a chromophoric substrate for pepsin and other aspartyl proteases: Design of a substrate based on subside preferences
    • Dunn, B. M., Kammermann, B., and McCurry, K. R. (1984). The synthesis, purification, and evaluation of a chromophoric substrate for pepsin and other aspartyl proteases: Design of a substrate based on subside preferences. Anal. Biochem. 138, 68-73.
    • (1984) Anal. Biochem. , vol.138 , pp. 68-73
    • Dunn, B.M.1    Kammermann, B.2    McCurry, K.R.3
  • 14
    • 0018854046 scopus 로고
    • Electrophoretic analysis of plasminogen activators in polyacrylamide gels containing sodium dodecyl sulfate and copolymerized substrates
    • Heussen, C., and Dowdle, E. B. (1980) Electrophoretic analysis of plasminogen activators in polyacrylamide gels containing sodium dodecyl sulfate and copolymerized substrates. Anal. Biochem. 102, 196-202.
    • (1980) Anal. Biochem. , vol.102 , pp. 196-202
    • Heussen, C.1    Dowdle, E.B.2
  • 15
    • 0023030010 scopus 로고
    • Heparin-binding fragments of fibronectin are potent inhibitors of endothelial cell growth: Structure-function correlation
    • Homandberg, G. A., Kramer-Bjerke, J., Grant, D., Christianson, G., and Eisenstein, R. (1986). Heparin-binding fragments of fibronectin are potent inhibitors of endothelial cell growth: Structure-function correlation, Biochim. Biophys. Acta 874, 61-71.
    • (1986) Biochim. Biophys. Acta , vol.874 , pp. 61-71
    • Homandberg, G.A.1    Kramer-Bjerke, J.2    Grant, D.3    Christianson, G.4    Eisenstein, R.5
  • 16
    • 0011734952 scopus 로고
    • Fibronectin fragment mediated damage to joint cartilage
    • Homandberg, G. A., Meyer R., and Williams, J. M. (1991). Fibronectin fragment mediated damage to joint cartilage, Anat. Rec. 229, 39-40.
    • (1991) Anat. Rec. , vol.229 , pp. 39-40
    • Homandberg, G.A.1    Meyer, R.2    Williams, J.M.3
  • 17
    • 0027674014 scopus 로고
    • Fibronectin and cancer: Rationales for the use of antiadhesives in cancer treatment
    • Humphries, M. J. (1993). Fibronectin and cancer: Rationales for the use of antiadhesives in cancer treatment. Cancer Biol. 4, 293-299.
    • (1993) Cancer Biol. , vol.4 , pp. 293-299
    • Humphries, M.J.1
  • 18
    • 0004043397 scopus 로고
    • Springer-Verlag, New York
    • Hynes, R. O. (1990). Fibronectins, Springer-Verlag, New York.
    • (1990) Fibronectins
    • Hynes, R.O.1
  • 19
    • 85109220005 scopus 로고
    • Application of bifunctional reagents for topological investigation
    • Kamp, R. M. (1988) Application of bifunctional reagents for topological investigation. Mod. Meth. Protein Chem. 3, 275-298.
    • (1988) Mod. Meth. Protein Chem. , vol.3 , pp. 275-298
    • Kamp, R.M.1
  • 22
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 23
    • 0025834586 scopus 로고
    • Latent fibronectin-degrading serine proteinase activity in N-terminal heparin-binding domain of human plasma fibronectin
    • Lambert Vidmar, S., Lottspeich, F., Emod, I., Planchenault, T., and Keil-Dlouha, V. (1991a). Latent fibronectin-degrading serine proteinase activity in N-terminal heparin-binding domain of human plasma fibronectin. Eur. J. Biochem. 201, 71-77.
    • (1991) Eur. J. Biochem. , vol.201 , pp. 71-77
    • Lambert Vidmar, S.1    Lottspeich, F.2    Emod, I.3    Planchenault, T.4    Keil-Dlouha, V.5
  • 24
    • 0025866527 scopus 로고
    • Collagen-binding domain of human plasma fibronectin contains a latent type-IV collagenase
    • Lambert Vidmar, S., Lottspeich, F., Emod, I, Imhoff, J., and Keil-Dlouha, V. (1991b) Collagen-binding domain of human plasma fibronectin contains a latent type-IV collagenase. Eur. J. Biochem. 201, 79-84.
    • (1991) Eur. J. Biochem. , vol.201 , pp. 79-84
    • Lambert Vidmar, S.1    Lottspeich, F.2    Emod, I.3    Imhoff, J.4    Keil-Dlouha, V.5
  • 25
    • 0014930908 scopus 로고
    • Effects of secondary enzyme-substrate interactions on the cleavage of synthetic peptides by pepsin
    • Medzihradszky, K., Voynick I. M.., Medzihradszky-Schweiger, H., and Fruton, J. S. (1970). Effects of secondary enzyme-substrate interactions on the cleavage of synthetic peptides by pepsin. Biochemistry 9, 1154-1162.
    • (1970) Biochemistry , vol.9 , pp. 1154-1162
    • Medzihradszky, K.1    Voynick, I.M.2    Medzihradszky-Schweiger, H.3    Fruton, J.S.4
  • 26
    • 0023657298 scopus 로고
    • Modification of the binding site(s) of lectins by an affinity column carrying an activated galactose-terminated lagand
    • Moroney, S. E., D'Alarcao, J. D., Goldmacher, V. S., Lambert, J. M., and Blatter, W. A. (1987). Modification of the binding site(s) of lectins by an affinity column carrying an activated galactose-terminated lagand. Biochemistry 26, 8390-8398.
    • (1987) Biochemistry , vol.26 , pp. 8390-8398
    • Moroney, S.E.1    D'Alarcao, J.D.2    Goldmacher, V.S.3    Lambert, J.M.4    Blatter, W.A.5
  • 27
    • 0004133195 scopus 로고
    • Academic Press, San Diego, California
    • Mosher, D. F. (1989). Fibronectin, Academic Press, San Diego, California.
    • (1989) Fibronectin
    • Mosher, D.F.1
  • 28
    • 0029891838 scopus 로고    scopus 로고
    • The CED-3/ICE-like protease Mch2 is activated during apoptosis and cleaves the death substrate lamin A
    • Orth, K., Chinnaiyan, A. M., Garg, M., Froelich, Ch. J., and Dixit, V. M. (1996). The CED-3/ICE-like protease Mch2 is activated during apoptosis and cleaves the death substrate lamin A. J. Biol. Chem. 271, 16443-16446.
    • (1996) J. Biol. Chem. , vol.271 , pp. 16443-16446
    • Orth, K.1    Chinnaiyan, A.M.2    Garg, M.3    Froelich, Ch.J.4    Dixit, V.M.5
  • 29
    • 0026316549 scopus 로고
    • Analysis of retroviral protease cleavage sites reveals two types of cleavage sites and the structural requirements of the PI amino acid
    • Pettit, S. C., Simsic, J., Loeb, D. D., Everitt, L., Hutchinson III, C. A.; and Swanstrom, R. (1991). Analysis of retroviral protease cleavage sites reveals two types of cleavage sites and the structural requirements of the PI amino acid. J. Biol. Chem. 266, 14539-14547.
    • (1991) J. Biol. Chem. , vol.266 , pp. 14539-14547
    • Pettit, S.C.1    Simsic, J.2    Loeb, D.D.3    Everitt, L.4    Hutchinson C.A. III5    Swanstrom, R.6
  • 31
    • 0026345896 scopus 로고
    • A cumulative specificity model for proteases from human immunodeficiency virus type 1 and 2, inferred from statistical analysis of an extended substrate data base
    • Poorman, R. A., Tomasselli, A. G., Heinrickson, R. L., and Kézdy, F. J. (1991). A cumulative specificity model for proteases from human immunodeficiency virus type 1 and 2, inferred from statistical analysis of an extended substrate data base J. Biol. Chem. 266, 14554-14561.
    • (1991) J. Biol. Chem. , vol.266 , pp. 14554-14561
    • Poorman, R.A.1    Tomasselli, A.G.2    Heinrickson, R.L.3    Kézdy, F.J.4
  • 32
    • 0025053763 scopus 로고
    • Mechanisms of protein silver staining in polyacry-lamide gels: A 10-year synthesis
    • Rabilloud, T. (1990) Mechanisms of protein silver staining in polyacry-lamide gels: A 10-year synthesis. Electrophoresis 11, 785-794.
    • (1990) Electrophoresis , vol.11 , pp. 785-794
    • Rabilloud, T.1
  • 33
    • 0001800923 scopus 로고
    • Direct microsequenceing of blotted and covalently attached proteins in a cross-flow reaction chamber
    • Jörnvall, H., Höog, J. O., and Gustavson, A. M., eds., Birkenhäuser, Basel
    • Reinke, H., Fischer, S., Reimann, F., and Tschesche, H. (1991). Direct microsequenceing of blotted and covalently attached proteins in a cross-flow reaction chamber, in Methods in Protein Sequence Analysis Jörnvall, H., Höog, J. O., and Gustavson, A. M., eds.), Birkenhäuser, Basel, pp. 55-66.
    • (1991) Methods in Protein Sequence Analysis , pp. 55-66
    • Reinke, H.1    Fischer, S.2    Reimann, F.3    Tschesche, H.4
  • 34
    • 0019518874 scopus 로고
    • Location of heparin-binding sites of fibronectin. Detection of a hitherto unrecognized transamidase sensitive site
    • Richter, H., Seidl, M., and Hörmann, H. (1981). Location of heparin-binding sites of fibronectin. Detection of a hitherto unrecognized transamidase sensitive site. Biol. Chem. Hoppe-Seyler 362, 399-408.
    • (1981) Biol. Chem. Hoppe-Seyler , vol.362 , pp. 399-408
    • Richter, H.1    Seidl, M.2    Hörmann, H.3
  • 35
    • 0014211618 scopus 로고
    • On the size of the active site in proteases. I. Papain
    • Schechter, I., and Berger, A. (1967). On the size of the active site in proteases. I. Papain. Biochem. Biophys. Res. Commun. 27, 157-162.
    • (1967) Biochem. Biophys. Res. Commun. , vol.27 , pp. 157-162
    • Schechter, I.1    Berger, A.2
  • 37
    • 0027021585 scopus 로고
    • Fibronectin fragments, but not intact fibronectin, signalling through the fibronectin receptor, induced metalloproteinase gene expression in fibroblasts
    • Tremble, P. M., Damsky, C. H., and Werb, Z. (1992). Fibronectin fragments, but not intact fibronectin, signalling through the fibronectin receptor, induced metalloproteinase gene expression in fibroblasts. Matrix 1, 212-214.
    • (1992) Matrix , vol.1 , pp. 212-214
    • Tremble, P.M.1    Damsky, C.H.2    Werb, Z.3
  • 38
    • 0343071970 scopus 로고
    • Insulin: HPLC mapping of protease digestion products
    • Vestling, M. M. (1991). Insulin: HPLC mapping of protease digestion products. J. Chem. Educ. 68, 958-960.
    • (1991) J. Chem. Educ. , vol.68 , pp. 958-960
    • Vestling, M.M.1
  • 39
    • 0018582608 scopus 로고
    • Purification of fibronectin from human plasma by affinity chromatography under non-denaturing conditions
    • Vuento, M., and Vaheri, A. (1979). Purification of fibronectin from human plasma by affinity chromatography under non-denaturing conditions. Biochem. J. 183, 334-337.
    • (1979) Biochem. J. , vol.183 , pp. 334-337
    • Vuento, M.1    Vaheri, A.2
  • 40
    • 0028206370 scopus 로고
    • Cartilage chondrolysis by fibronectin fragments is associated with release of several proteinases: Stromelysin plays a major role in chondrolysis
    • Xie, D.-L., Hui, F., Meyers, R., and Homandberg, G. A. (1994). Cartilage chondrolysis by fibronectin fragments is associated with release of several proteinases: Stromelysin plays a major role in chondrolysis. Arch. Biochim. Biophys. 311, 205-212.
    • (1994) Arch. Biochim. Biophys. , vol.311 , pp. 205-212
    • Xie, D.-L.1    Hui, F.2    Meyers, R.3    Homandberg, G.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.