메뉴 건너뛰기




Volumn 47, Issue 2, 2009, Pages 153-177

Quantitative determination and localization of cathepsin D and its inhibitors

Author keywords

Activity; Cathepsin D; Cathepsin D inhibitors; Cell distribution; Concentration; Tissue distribution

Indexed keywords

ALBUMIN; ALPHA GLOBIN; BETA ENDORPHIN; BETA GLOBIN; CASEIN; CATHEPSIN B; CATHEPSIN D; CATHEPSIN D INHIBITOR; CATHEPSIN L; HEMOGLOBIN; MYOGLOBIN; PEPSTATIN; PROCATHEPSIN D; PROTEIN INHIBITOR; SOMATOMEDIN B RECEPTOR; SYNTHETIC PEPTIDE; UNCLASSIFIED DRUG;

EID: 73549114458     PISSN: 02398508     EISSN: None     Source Type: Journal    
DOI: 10.2478/v10042-009-0073-4     Document Type: Review
Times cited : (22)

References (236)
  • 1
    • 0025635945 scopus 로고
    • Characterization of hemoglobin-hydrolyzing and proteinases in human and rat neutrophils
    • 1
    • [ 1] Ochmaru E, Sakai H, Saku T, Kunimatsu K, Kato Y, Kato I, Yamamoto K. Characterization of hemoglobin-hydrolyzing and proteinases in human and rat neutrophils. J Biochem. 1990;108:1009-1015.
    • (1990) J Biochem , vol.108 , pp. 1009-1015
    • Ochmaru, E.1    Sakai, H.2    Saku, T.3    Kunimatsu, K.4    Kato, Y.5    Kato, I.6    Yamamoto, K.7
  • 4
    • 0015835407 scopus 로고
    • Metody pomiaru aktywnooeci enzymów proteolitycznych.
    • 4
    • [ 4] Worowski K, Mariak T. Metody pomiaru aktywnooeci enzymów proteolitycznych. Diagn Lab. 1973;9:219-232.
    • (1973) Diagn Lab , vol.9 , pp. 219-232
    • Worowski, K.1    Mariak, T.2
  • 5
    • 73549095509 scopus 로고
    • 5] Barrett AJ. Cathepsin D and other carboxyl proteinases, Proteinases in mammalian cell and tissue ed
    • [ 5] Barrett AJ. Cathepsin D and other carboxyl proteinases, in: Proteinases in mammalian cell and tissue ed. AJ Barrett. Nort-Holland Publ Comp, Amsterdam. 1977:209-248.
    • (1977) Nort-Holland Publ Comp, Amsterdam , pp. 209-248
  • 6
    • 0018145511 scopus 로고
    • Improvements of the Anson assay for measuring proteolytic activities in acidic pH range
    • 6
    • [ 6] Lanoe J, Dumnigan J. Improvements of the Anson assay for measuring proteolytic activities in acidic pH range. Anal Biochem. 1978;89:461-471.
    • (1978) Anal Biochem , vol.89 , pp. 461-471
    • Lanoe, J.1    Dumnigan, J.2
  • 7
    • 85009302741 scopus 로고    scopus 로고
    • [ 7] Worowski K, Ostrowska H. Cathepsin D. Post Biol Kom. 1980;7:119-147.
    • [ 7] Worowski K, Ostrowska H. Cathepsin D. Post Biol Kom. 1980;7:119-147.
  • 9
    • 0031885645 scopus 로고    scopus 로고
    • A novel methodology for the investigation of intracellular proteolytic processing in intact cells
    • 9
    • [ 9] Reis RCM, Sorgine MHF, Coelho-Sampaio T. A novel methodology for the investigation of intracellular proteolytic processing in intact cells. Eur J Cell Biol. 1998;75:192-197.
    • (1998) Eur J Cell Biol , vol.75 , pp. 192-197
    • Reis, R.C.M.1    Sorgine, M.H.F.2    Coelho-Sampaio, T.3
  • 10
    • 73549092698 scopus 로고    scopus 로고
    • Determination of activity and concentration of cathepsin and their inhibitors
    • Roszkowska-Jakimiec W, Worowska A, Gacko M, Worowski K. Determination of activity and concentration of cathepsin and their inhibitors. Diagn Lab. 2000;36:103-119.
    • (2000) Diagn Lab , vol.36 , pp. 103-119
    • Roszkowska-Jakimiec, W.1    Worowska, A.2    Gacko, M.3    Worowski, K.4
  • 11
    • 17444381438 scopus 로고    scopus 로고
    • Oznaczanie aktywnooeci katepsyny D w osoczu krwi przy użyciu hemoglobiny zdenaturowanej kwasem solnym.
    • Greczaniuk A, Roszkowska-Jakimiec W, Gacko M, Worowska A. Oznaczanie aktywnooeci katepsyny D w osoczu krwi przy użyciu hemoglobiny zdenaturowanej kwasem solnym. Diagn Lab. 2001;36:97-101.
    • (2001) Diagn Lab , vol.36 , pp. 97-101
    • Greczaniuk, A.1    Roszkowska-Jakimiec, W.2    Gacko, M.3    Worowska, A.4
  • 12
    • 73549088493 scopus 로고    scopus 로고
    • Method of cathepsin D activity and concentration determination
    • Roszkowska-Jakimiec W, Gacko M, Worowska A. Method of cathepsin D activity and concentration determination. Diagn Lab. 2007;43:275-282.
    • (2007) Diagn Lab , vol.43 , pp. 275-282
    • Roszkowska-Jakimiec, W.1    Gacko, M.2    Worowska, A.3
  • 13
    • 0028238397 scopus 로고
    • Structural requirements of procathepsin D activation and maturation
    • Richo GR, Conner GE. Structural requirements of procathepsin D activation and maturation. J Biol Chem. 1994;296:14806-14812.
    • (1994) J Biol Chem , vol.296 , pp. 14806-14812
    • Richo, G.R.1    Conner, G.E.2
  • 14
    • 0035074341 scopus 로고    scopus 로고
    • The molecular machinery for lysosom biogenesis
    • Mullins C, Bonifacino JS. The molecular machinery for lysosom biogenesis. BioEssays. 2001;23:333-343.
    • (2001) BioEssays , vol.23 , pp. 333-343
    • Mullins, C.1    Bonifacino, J.S.2
  • 16
    • 0024312845 scopus 로고
    • Biosynthesis of lysosomal endopeptidases
    • Erickon AH. Biosynthesis of lysosomal endopeptidases. J Cell Biochem. 1989;40:31-41.
    • (1989) J Cell Biochem , vol.40 , pp. 31-41
    • Erickon, A.H.1
  • 17
    • 0026747027 scopus 로고
    • Development of gel staining techniques for detecting the secretion of procathepsin D (52-kDa protein) in MCF-7 human breast cabcer cells
    • Krishman V, Narasimahan TR, Safe S. Development of gel staining techniques for detecting the secretion of procathepsin D (52-kDa protein) in MCF-7 human breast cabcer cells. Anal Biochem. 1992;204:137-142.
    • (1992) Anal Biochem , vol.204 , pp. 137-142
    • Krishman, V.1    Narasimahan, T.R.2    Safe, S.3
  • 18
    • 0024364949 scopus 로고
    • Mamose 6-phosphate receptors and lysosomal enzyme tergeting
    • Dahmus NH, Label P, Kornfeld S. Mamose 6-phosphate receptors and lysosomal enzyme tergeting. J Biol Chem. 1989;264:12115-12118.
    • (1989) J Biol Chem , vol.264 , pp. 12115-12118
    • Dahmus, N.H.1    Label, P.2    Kornfeld, S.3
  • 19
    • 0027530694 scopus 로고
    • Procathepsin D cannot autoactivate to cathepsin D at acid pH
    • Larsen LB, Boisen A, Petersen TE. Procathepsin D cannot autoactivate to cathepsin D at acid pH. FEBS Lett. 1993;319:54-58.
    • (1993) FEBS Lett , vol.319 , pp. 54-58
    • Larsen, L.B.1    Boisen, A.2    Petersen, T.E.3
  • 20
  • 21
    • 53249132917 scopus 로고    scopus 로고
    • Purification and characterization of cathepsin D for human breast tissue
    • Wright LM, Levy ES, Patel NP, Alhadeff JA. Purification and characterization of cathepsin D for human breast tissue. J Prot Chem. 1997;16:171-181.
    • (1997) J Prot Chem , vol.16 , pp. 171-181
    • Wright, L.M.1    Levy, E.S.2    Patel, N.P.3    Alhadeff, J.A.4
  • 23
    • 0024412693 scopus 로고
    • The selectivity of cathepsin D suggests an involvement of the T-cell epitopes
    • van Noort JM, van der Drift ACM. The selectivity of cathepsin D suggests an involvement of the T-cell epitopes. J Biol Chem. 1989;264:14159-14164.
    • (1989) J Biol Chem , vol.264 , pp. 14159-14164
    • van Noort, J.M.1    van der Drift, A.C.M.2
  • 24
    • 0017303597 scopus 로고
    • Purification and properties of cathepsin D from porcine spleen
    • Cunningham M, Tang J. Purification and properties of cathepsin D from porcine spleen. J Biol Chem. 1972;251: 4528-4536.
    • (1972) J Biol Chem , vol.251 , pp. 4528-4536
    • Cunningham, M.1    Tang, J.2
  • 27
    • 0026555037 scopus 로고
    • Proteases and proteolysis in the lysosome
    • Bohley P, Seglen PO. Proteases and proteolysis in the lysosome. Experientia. 1992;48:151-157.
    • (1992) Experientia , vol.48 , pp. 151-157
    • Bohley, P.1    Seglen, P.O.2
  • 28
    • 0023943263 scopus 로고
    • Cathepsin D is membraneassociated in macrophage endosomes
    • Diment S, Leech MS, Stahl PD. Cathepsin D is membraneassociated in macrophage endosomes. J Biol Chem. 1988;263:6901-6907.
    • (1988) J Biol Chem , vol.263 , pp. 6901-6907
    • Diment, S.1    Leech, M.S.2    Stahl, P.D.3
  • 30
    • 0016503357 scopus 로고
    • Proteolytic degradation of hemoglobin-haptoglobin complex by lysosomal enzymes from rat liver
    • Kimura H, Tsudzuki T, Murachi T. Proteolytic degradation of hemoglobin-haptoglobin complex by lysosomal enzymes from rat liver. J Biochem. 1975;77:909-912.
    • (1975) J Biochem , vol.77 , pp. 909-912
    • Kimura, H.1    Tsudzuki, T.2    Murachi, T.3
  • 32
    • 0017257365 scopus 로고    scopus 로고
    • Dean RT, Barrett AJ. Essays in biochemistry ed. PN Campbell WN Aldrige. Acad Press NY. 1976;12:1-40.
    • Dean RT, Barrett AJ. Essays in biochemistry ed. PN Campbell WN Aldrige. Acad Press NY. 1976;12:1-40.
  • 33
    • 0017893358 scopus 로고
    • Purification and properties of an acid protease from human asciric fluid
    • Esumi H, Sato S, Sugimura T, Okasaki N. Purification and properties of an acid protease from human asciric fluid. Biochim Biophys Acta. 1978;523:191-197.
    • (1978) Biochim Biophys Acta , vol.523 , pp. 191-197
    • Esumi, H.1    Sato, S.2    Sugimura, T.3    Okasaki, N.4
  • 34
    • 0015251844 scopus 로고
    • Diagnostic value of urinary enzyme determination
    • Raab WP. Diagnostic value of urinary enzyme determination. Clin Chem. 1972;18:5-25.
    • (1972) Clin Chem , vol.18 , pp. 5-25
    • Raab, W.P.1
  • 35
    • 0020012016 scopus 로고
    • Blood platelets - a source of cathepsin D activity in the serum
    • Ostrowska H, Worowski K. Blood platelets - a source of cathepsin D activity in the serum. Acta Haematol Pol. 1982;13:13-16.
    • (1982) Acta Haematol Pol , vol.13 , pp. 13-16
    • Ostrowska, H.1    Worowski, K.2
  • 36
    • 77049229661 scopus 로고
    • Tissue fractionation studies. 6. Intracellular distribution patterns of enzymes in rat-liver tissue
    • De Duve C, Pressman BC, Gianetto R, Wattiaux R, Appelmans F. Tissue fractionation studies. 6. Intracellular distribution patterns of enzymes in rat-liver tissue. Biochem J. 1955;60:604-617.
    • (1955) Biochem J , vol.60 , pp. 604-617
    • De Duve, C.1    Pressman, B.C.2    Gianetto, R.3    Wattiaux, R.4    Appelmans, F.5
  • 38
    • 0015761108 scopus 로고
    • The influence of autolysis and homogenization techniques on the stability of preparations of subcellular fractions
    • Panusz H. The influence of autolysis and homogenization techniques on the stability of preparations of subcellular fractions. Ann Acad Med Lodzensis. 1973;14,suppl.10:157-161.
    • (1973) Ann Acad Med Lodzensis , vol.14 , Issue.SUPPL.10 , pp. 157-161
    • Panusz, H.1
  • 39
    • 0015392860 scopus 로고
    • Simple appartus for pulverization and rapid quantitative transfer of frozen tissue
    • Ladinsky H, Consolo S, Sanvito A. Simple appartus for pulverization and rapid quantitative transfer of frozen tissue. Anal Biochem. 1972;49:294-297.
    • (1972) Anal Biochem , vol.49 , pp. 294-297
    • Ladinsky, H.1    Consolo, S.2    Sanvito, A.3
  • 40
    • 73549092902 scopus 로고    scopus 로고
    • CertiPrep handblook of sample preparation and handling
    • Obenauf RH. SPEX CertiPrep handblook of sample preparation and handling. SPEX GertiPrep Inc Metuchen NJ USA. 2002:26-54.
    • (2002) SPEX GertiPrep Inc Metuchen NJ USA , pp. 26-54
    • Obenauf, R.S.1
  • 41
    • 85009339178 scopus 로고
    • Decrease of tissue respiration, activity of oxoglutarate dehydrogenase and level of sulfhydryl groups in acute acrylonitrile intoxication in rats
    • Wiśniewska-Knypl JM, Knobloch K, Jabłońska J, Ruta U. Decrease of tissue respiration, activity of oxoglutarate dehydrogenase and level of sulfhydryl groups in acute acrylonitrile intoxication in rats. Med Pracy. 1970;21:544-549.
    • (1970) Med Pracy , vol.21 , pp. 544-549
    • Wiśniewska-Knypl, J.M.1    Knobloch, K.2    Jabłońska, J.3    Ruta, U.4
  • 42
    • 0030630367 scopus 로고    scopus 로고
    • Chyczewski L, Płoński A, Chyczewska E, Furman M, Ostrowska H, Niklinacute;ski J, Kozłowski M. Activity and tissue localization of cathepsin D in non small cell lung cancer. Ann Acad Med Bialostoc. 1997;42suppl1:217-229.
    • Chyczewski L, Płoński A, Chyczewska E, Furman M, Ostrowska H, Niklinacute;ski J, Kozłowski M. Activity and tissue localization of cathepsin D in non small cell lung cancer. Ann Acad Med Bialostoc. 1997;42suppl1:217-229.
  • 43
    • 0025743395 scopus 로고
    • Procathepsin L and D are membrane-bound in acidic microsomal vesicles
    • McIntyre GF, Erickson AH. Procathepsin L and D are membrane-bound in acidic microsomal vesicles. J Biol Chem. 1991;266:15438-15445.
    • (1991) J Biol Chem , vol.266 , pp. 15438-15445
    • McIntyre, G.F.1    Erickson, A.H.2
  • 44
    • 85009321456 scopus 로고    scopus 로고
    • Beaufay H. Methods for the isolation of lysosomes, in lysosomes a laboratory handbook, ed JT Dindle. North-Holland Publ Comp Amsterdam. 1972:1-32.
    • Beaufay H. Methods for the isolation of lysosomes, in lysosomes a laboratory handbook, ed JT Dindle. North-Holland Publ Comp Amsterdam. 1972:1-32.
  • 45
    • 0014288490 scopus 로고
    • The large-scale separation of peroxisomes, mitochondria, and lysosomes from the livers of rats injected with triton WR-1339
    • Leeighton F, Paole B, Beaufay H, Baudhuin P, Coffey JW, Fowler S, de Duve C. The large-scale separation of peroxisomes, mitochondria, and lysosomes from the livers of rats injected with triton WR-1339. J Cell Biol. 1968;37:482.
    • (1968) J Cell Biol , vol.37 , pp. 482
    • Leeighton, F.1    Paole, B.2    Beaufay, H.3    Baudhuin, P.4    Coffey, J.W.5    Fowler, S.6    de Duve, C.7
  • 46
    • 0025239273 scopus 로고
    • Isolation of subcellular organelles
    • Storrie B, Madden EA. Isolation of subcellular organelles. Meth Enzymol. 1990;182:203-225.
    • (1990) Meth Enzymol , vol.182 , pp. 203-225
    • Storrie, B.1    Madden, E.A.2
  • 47
    • 0030333936 scopus 로고    scopus 로고
    • Activity of enzymes of varions subcellular localization in cytosol obtained after cell organelle precipitation at pH 5,0
    • Gacko M, Głowiński J, Skrzydlewska E, Worowska A, Głowiński S. Activity of enzymes of varions subcellular localization in cytosol obtained after cell organelle precipitation at pH 5,0. Ann Acad Med Białostocensis. 1996;41:341-346.
    • (1996) Ann Acad Med Białostocensis , vol.41 , pp. 341-346
    • Gacko, M.1    Głowiński, J.2    Skrzydlewska, E.3    Worowska, A.4    Głowiński, S.5
  • 48
    • 38849187424 scopus 로고
    • Determination of the activity of enzyme inactivated during catalytic process
    • Sznajd J, Naskalski J. Determination of the activity of enzyme inactivated during catalytic process. Diagn Lab. 1978;14:127-133.
    • (1978) Diagn Lab , vol.14 , pp. 127-133
    • Sznajd, J.1    Naskalski, J.2
  • 49
    • 85009321459 scopus 로고    scopus 로고
    • Turk V, Lah T, Kregar I. Cathepsin D, cathepsin E. In ed HU Bergmeyer Methods of enzymatic analysis. Verlag Chemie Weinheim. 1984:211-222.
    • Turk V, Lah T, Kregar I. Cathepsin D, cathepsin E. In ed HU Bergmeyer Methods of enzymatic analysis. Verlag Chemie Weinheim. 1984:211-222.
  • 51
    • 2642714342 scopus 로고
    • Fluorescence probe measurement of the intralysosomal pH in living cell and the perturbation of pH by various agents
    • Okhuma S, Poole B. Fluorescence probe measurement of the intralysosomal pH in living cell and the perturbation of pH by various agents. Proc Natt acad Sci USA. 1978;75:3327-3331.
    • (1978) Proc Natt acad Sci USA , vol.75 , pp. 3327-3331
    • Okhuma, S.1    Poole, B.2
  • 52
    • 0027381284 scopus 로고
    • Acidification of rat liver lysosomes: Quantitation and comparision with endosomes
    • Van Dyke RW. Acidification of rat liver lysosomes: quantitation and comparision with endosomes. Am J Physiol. 1993;165:C901-C917.
    • (1993) Am J Physiol , vol.165
    • Van Dyke, R.W.1
  • 53
    • 0028296812 scopus 로고
    • Multiple function of pro-parts aspartic proteinase zymogenes
    • Koelsch G, Mares M, Metcalf P, Fusek M. Multiple function of pro-parts aspartic proteinase zymogenes. FEBS Lett. 1994;343:6-10.
    • (1994) FEBS Lett , vol.343 , pp. 6-10
    • Koelsch, G.1    Mares, M.2    Metcalf, P.3    Fusek, M.4
  • 54
    • 33845963935 scopus 로고    scopus 로고
    • Cathepsin D propeptide: Mechanism and regulation of its interaction with the catalitic core
    • Masa M, Maresova L, Vondrasek J, Horn M, Jezek J, Mares M. Cathepsin D propeptide: mechanism and regulation of its interaction with the catalitic core. Biochemistry. 2006;45:15474-15482.
    • (2006) Biochemistry , vol.45 , pp. 15474-15482
    • Masa, M.1    Maresova, L.2    Vondrasek, J.3    Horn, M.4    Jezek, J.5    Mares, M.6
  • 55
    • 0014466860 scopus 로고
    • Lysosomal enzyme changes in growing and regressing mammary tumors
    • Shamberger RJ. Lysosomal enzyme changes in growing and regressing mammary tumors, Biochem J. 1969;111:375-383.
    • (1969) Biochem J , vol.111 , pp. 375-383
    • Shamberger, R.J.1
  • 56
    • 0017091634 scopus 로고
    • Mode od inhibition of acid proteases by pepstatin
    • Marciniszyn J, Hartsuch JA, Tang J. Mode od inhibition of acid proteases by pepstatin. J Biol Chem. 1976;25:7088-7094.
    • (1976) J Biol Chem , vol.25 , pp. 7088-7094
    • Marciniszyn, J.1    Hartsuch, J.A.2    Tang, J.3
  • 57
    • 0017112615 scopus 로고
    • La cathepsin D de rate de cheval. II. Etude de quelques properietes enzymatique
    • Ducastaing A, Azanza JL, Raymund J, Robin JM, Greach P. La cathepsin D de rate de cheval. II. Etude de quelques properietes enzymatique. Biochemie. 1972;58:783-791.
    • (1972) Biochemie , vol.58 , pp. 783-791
    • Ducastaing, A.1    Azanza, J.L.2    Raymund, J.3    Robin, J.M.4    Greach, P.5
  • 58
    • 0020578295 scopus 로고
    • Molecular forms of beta-hexosaminidase and cathepasin D in serum and urine of health subjects and patients with elevated acticity of lysosomal enzymes
    • Zuhlsdorf M, Imort M, Hasilik A, Von Fidura K. Molecular forms of beta-hexosaminidase and cathepasin D in serum and urine of health subjects and patients with elevated acticity of lysosomal enzymes. Biochem J. 1983;213:733-740.
    • (1983) Biochem J , vol.213 , pp. 733-740
    • Zuhlsdorf, M.1    Imort, M.2    Hasilik, A.3    Von Fidura, K.4
  • 59
    • 73549113765 scopus 로고
    • Concentration of the biological fluids
    • Zwierz K, Zych J. Concentration of the biological fluids. Diagn Lab. 1971;7:127-130.
    • (1971) Diagn Lab , vol.7 , pp. 127-130
    • Zwierz, K.1    Zych, J.2
  • 60
    • 73549123433 scopus 로고
    • Poradnik chemika analityka
    • Ciba J. Poradnik chemika analityka. Wyd N-T Warszawa. 1989;1:107.
    • (1989) Wyd N-T Warszawa , vol.1 , pp. 107
    • Ciba, J.1
  • 61
    • 0031670902 scopus 로고    scopus 로고
    • Conformational switching in an aspartic proteinase
    • Lee AY, Gulnik SV, Erickson JW. Conformational switching in an aspartic proteinase. Nat Struct Biol. 1998;5:866-871.
    • (1998) Nat Struct Biol , vol.5 , pp. 866-871
    • Lee, A.Y.1    Gulnik, S.V.2    Erickson, J.W.3
  • 62
    • 0032079894 scopus 로고    scopus 로고
    • Molecular cloning, expression and characterization of an Ascaris inhibitor for pepsin and cathepsin E
    • Kageyama T. Molecular cloning, expression and characterization of an Ascaris inhibitor for pepsin and cathepsin E. Eur J Biochem. 1998;253:804-809.
    • (1998) Eur J Biochem , vol.253 , pp. 804-809
    • Kageyama, T.1
  • 63
    • 0035914328 scopus 로고    scopus 로고
    • Hemoglobin-degradation, aspartic proteases of blood-fleeding parasites: Substrate specificity revealed by homology models
    • Brinkworth RI, Prociv P, Loukas A, Brindley PJ. Hemoglobin-degradation, aspartic proteases of blood-fleeding parasites: substrate specificity revealed by homology models. J Biol Chem. 2001; 276:38844-38851.
    • (2001) J Biol Chem , vol.276 , pp. 38844-38851
    • Brinkworth, R.I.1    Prociv, P.2    Loukas, A.3    Brindley, P.J.4
  • 64
    • 0021811506 scopus 로고
    • Degradation of peptidase and proteins of different size by homogenates of human MRC5 lung fibroblasts
    • Wharton SA, Hipkiss AR. Degradation of peptidase and proteins of different size by homogenates of human MRC5 lung fibroblasts. FEBS Lett. 1985;184:249-253.
    • (1985) FEBS Lett , vol.184 , pp. 249-253
    • Wharton, S.A.1    Hipkiss, A.R.2
  • 65
    • 0032577211 scopus 로고    scopus 로고
    • Cathepsin D is a good candidate for the specific release of stable hemorphin from hemoglobin in vivo: VV-hemorphin - 7
    • Fruitier I, Gareau I, Piat JM. Cathepsin D is a good candidate for the specific release of stable hemorphin from hemoglobin in vivo: VV-hemorphin - 7. Biochem Biophys Res Commun. 1998;246:719-724.
    • (1998) Biochem Biophys Res Commun , vol.246 , pp. 719-724
    • Fruitier, I.1    Gareau, I.2    Piat, J.M.3
  • 66
    • 0032584670 scopus 로고    scopus 로고
    • Normal and abnormal protein subunit interaction in hemoglobins
    • Manning JM, Dumoulin A, Li X, Manning LR. Normal and abnormal protein subunit interaction in hemoglobins. J Biol Chem. 1998;173:19359-19362.
    • (1998) J Biol Chem , vol.173 , pp. 19359-19362
    • Manning, J.M.1    Dumoulin, A.2    Li, X.3    Manning, L.R.4
  • 67
    • 0014670514 scopus 로고
    • Preparation and properties of alfa- and beta-chains human hemoglobin
    • Geraci G, Parkhurst LJ, Gibson QH. Preparation and properties of alfa- and beta-chains human hemoglobin. J Biol Chem. 1969;244:46664-4667.
    • (1969) J Biol Chem , vol.244 , pp. 46664-54667
    • Geraci, G.1    Parkhurst, L.J.2    Gibson, Q.H.3
  • 68
    • 0014853439 scopus 로고
    • The effect of urea upon the activity measurement of cod muscle cathepsin with hemoglobin substrate
    • Wojtowicz MB, Odense P. The effect of urea upon the activity measurement of cod muscle cathepsin with hemoglobin substrate. Can J Biochem. 1970;48:1050-1053.
    • (1970) Can J Biochem , vol.48 , pp. 1050-1053
    • Wojtowicz, M.B.1    Odense, P.2
  • 70
    • 0022881317 scopus 로고
    • The azocaseinurea-pepstatin assay discriminates between lysosomal proteinases
    • Wiederanders B, Kirschke H, Scharper S. The azocaseinurea-pepstatin assay discriminates between lysosomal proteinases. Biomed. Biochim. Acta. 1986;45:1477-1483.
    • (1986) Biomed. Biochim. Acta , vol.45 , pp. 1477-1483
    • Wiederanders, B.1    Kirschke, H.2    Scharper, S.3
  • 71
    • 49749194276 scopus 로고
    • Studies on the structure of hemoglobin. I. Physiococchemical properties of human globin
    • Rossi-Fanelli A, Antonioni E, Caputo A. Studies on the structure of hemoglobin. I. Physiococchemical properties of human globin. Biochem Biophys Acta. 1958;30:608-615.
    • (1958) Biochem Biophys Acta , vol.30 , pp. 608-615
    • Rossi-Fanelli, A.1    Antonioni, E.2    Caputo, A.3
  • 72
    • 0004508416 scopus 로고
    • Preparation, properties and specific recombination of alpha-beta-globin subunits
    • Winterhalter KH, Huehns ER. Preparation, properties and specific recombination of alpha-beta-globin subunits. J Biol Chem. 1964;239:3699-3702.
    • (1964) J Biol Chem , vol.239 , pp. 3699-3702
    • Winterhalter, K.H.1    Huehns, E.R.2
  • 73
    • 0345169971 scopus 로고    scopus 로고
    • Preparation and characterization of dimeric bovine hemoglobin tetramers
    • Hu T, Li DX, Su ZG. Preparation and characterization of dimeric bovine hemoglobin tetramers. J Prot Chem. 2003;22:411-416.
    • (2003) J Prot Chem , vol.22 , pp. 411-416
    • Hu, T.1    Li, D.X.2    Su, Z.G.3
  • 74
    • 0019327122 scopus 로고
    • Isolated parenchymal, Kupfter and endothelial rat liver cells charactericed by their lysosomal enzyme content
    • Knook DL, Steyster EC. Isolated parenchymal, Kupfter and endothelial rat liver cells charactericed by their lysosomal enzyme content. Biochem Biophys Res Commun. 1980;96:250-257.
    • (1980) Biochem Biophys Res Commun , vol.96 , pp. 250-257
    • Knook, D.L.1    Steyster, E.C.2
  • 75
    • 0022992976 scopus 로고
    • Spectrophotometric determination of tryptophan and tyrosine in peptides and proteins based on new color reactions
    • Chrastil J. Spectrophotometric determination of tryptophan and tyrosine in peptides and proteins based on new color reactions. Anal Biochem. 1986;158:443-446.
    • (1986) Anal Biochem , vol.158 , pp. 443-446
    • Chrastil, J.1
  • 76
    • 9844248112 scopus 로고
    • Characterictics of thyroid lysosomal cathepsin
    • Balasubramanin K, Deiss WP. Characterictics of thyroid lysosomal cathepsin. Biochem Biophys Acta. 1965;110:564-575.
    • (1965) Biochem Biophys Acta , vol.110 , pp. 564-575
    • Balasubramanin, K.1    Deiss, W.P.2
  • 77
    • 0014006559 scopus 로고
    • Use of casein in assays for proteolytic activity in tissue extracts: A warning
    • Marrink J, Gruber M. Use of casein in assays for proteolytic activity in tissue extracts: a warning. Biochim Biophys Acta. 1966;118:438-439.
    • (1966) Biochim Biophys Acta , vol.118 , pp. 438-439
    • Marrink, J.1    Gruber, M.2
  • 78
    • 0041649014 scopus 로고
    • Study of a proteolytic enzyme from rabbit spleen
    • Lapresle C, Webb T. Study of a proteolytic enzyme from rabbit spleen. Biochem J. 1960;76:538-549.
    • (1960) Biochem J , vol.76 , pp. 538-549
    • Lapresle, C.1    Webb, T.2
  • 79
    • 34249723575 scopus 로고
    • The Lowry modyfication of the Folin reagent for determination of proteinase activity
    • McDonald CE, Chen LL. The Lowry modyfication of the Folin reagent for determination of proteinase activity. Anal Biochem. 1965;10:175-177.
    • (1965) Anal Biochem , vol.10 , pp. 175-177
    • McDonald, C.E.1    Chen, L.L.2
  • 80
    • 0015392927 scopus 로고
    • A sensitive fluorometric assay for the determination of cathepsin D
    • Mednis A, Remold HG. A sensitive fluorometric assay for the determination of cathepsin D. Anal Biochem. 1972;49:114-138.
    • (1972) Anal Biochem , vol.49 , pp. 114-138
    • Mednis, A.1    Remold, H.G.2
  • 82
    • 0018828701 scopus 로고
    • Proteins iodinated by chloramine-T method appear to be degraded at an abnormally rapid rate ofter endocytosis
    • Opresko L, Wiley HS, Wallace RA. Proteins iodinated by chloramine-T method appear to be degraded at an abnormally rapid rate ofter endocytosis. Proc Natt Acad Sci USA. 1980;77:1556-1560.
    • (1980) Proc Natt Acad Sci USA , vol.77 , pp. 1556-1560
    • Opresko, L.1    Wiley, H.S.2    Wallace, R.A.3
  • 83
    • 0021048523 scopus 로고
    • Cathepsin D from human brain: Purification and multiple froms
    • Azaryan A, Akopyan T, Buniatian H. Cathepsin D from human brain: purification and multiple froms. Biomed Biochim Acta. 1983;42:1237-1246.
    • (1983) Biomed Biochim Acta , vol.42 , pp. 1237-1246
    • Azaryan, A.1    Akopyan, T.2    Buniatian, H.3
  • 84
    • 0014809294 scopus 로고
    • Fluorescein-hemoglobin as a substrate for cathepsin D and other proteases
    • De Lumen BO, Tappel AL. Fluorescein-hemoglobin as a substrate for cathepsin D and other proteases. Anal Biochem. 1970;36:22-29.
    • (1970) Anal Biochem , vol.36 , pp. 22-29
    • De Lumen, B.O.1    Tappel, A.L.2
  • 85
    • 0015877315 scopus 로고
    • Afluorescent assay for proteolytic enzymes
    • Schwabe C. Afluorescent assay for proteolytic enzymes. Anal Biochem. 1973;53:484-490.
    • (1973) Anal Biochem , vol.53 , pp. 484-490
    • Schwabe, C.1
  • 87
    • 0021738226 scopus 로고
    • Fluoroescein isothiocynate laboled casein assay for proteolytic enzyme
    • Twining SS. Fluoroescein isothiocynate laboled casein assay for proteolytic enzyme. Anal Biochem. 1984;143:30-34.
    • (1984) Anal Biochem , vol.143 , pp. 30-34
    • Twining, S.S.1
  • 88
    • 0035137916 scopus 로고    scopus 로고
    • Macromolecular chromogenic substrates for measuring proteinase activity
    • Hortin GL, Warshawsky I, Laude-Sharp M. Macromolecular chromogenic substrates for measuring proteinase activity. Clin Chem. 2001;47:215-222.
    • (2001) Clin Chem , vol.47 , pp. 215-222
    • Hortin, G.L.1    Warshawsky, I.2    Laude-Sharp, M.3
  • 89
    • 0018523233 scopus 로고
    • Afluorescamine-based sensitive method for the assay of proteinases, capable of detecting the initial cleavage step of a protein
    • Garesse R, Castell JV, Vallejo CG, Marco R. Afluorescamine-based sensitive method for the assay of proteinases, capable of detecting the initial cleavage step of a protein. Eur J Biochem. 1979;99:253-259.
    • (1979) Eur J Biochem , vol.99 , pp. 253-259
    • Garesse, R.1    Castell, J.V.2    Vallejo, C.G.3    Marco, R.4
  • 90
    • 0015090666 scopus 로고
    • Assay of proteolytic enzyme activity using a 14C- labelled hemoglobin
    • Roth JS, Losty T, Wierbicki E. Assay of proteolytic enzyme activity using a 14C- labelled hemoglobin. Anal Biochem. 1971;42:214-221.
    • (1971) Anal Biochem , vol.42 , pp. 214-221
    • Roth, J.S.1    Losty, T.2    Wierbicki, E.3
  • 91
    • 0015228193 scopus 로고
    • Methyl-14C-glycinated hemoglobin as a substrate for proteases
    • Williams HR, Lin TY. Methyl-14C-glycinated hemoglobin as a substrate for proteases. Biochim Biophys Acta. 1971;250:603-607.
    • (1971) Biochim Biophys Acta , vol.250 , pp. 603-607
    • Williams, H.R.1    Lin, T.Y.2
  • 92
    • 73549109614 scopus 로고
    • Tritium labelling of proteins to high specific radioactivity by reductive methylation
    • Tack BF, Dean J, Eilat D. Tritium labelling of proteins to high specific radioactivity by reductive methylation. J Biol Chem. 1980;193:265-272.
    • (1980) J Biol Chem , vol.193 , pp. 265-272
    • Tack, B.F.1    Dean, J.2    Eilat, D.3
  • 93
    • 0030471874 scopus 로고    scopus 로고
    • Determination of cathepsin S and E in various tissues and cell of rat, monkey, and man by the assay with beta-endorphin and substrate P as substrate
    • Kageyama T, Moriyama A, Kato T, Sano M, Yonezawa S. Determination of cathepsin S and E in various tissues and cell of rat, monkey, and man by the assay with beta-endorphin and substrate P as substrate. Zool Sci. 1996;13:693-698.
    • (1996) Zool Sci , vol.13 , pp. 693-698
    • Kageyama, T.1    Moriyama, A.2    Kato, T.3    Sano, M.4    Yonezawa, S.5
  • 94
    • 0014387961 scopus 로고
    • Cathepsin activity in normal and dystrophic human muscle
    • Pennington RJ, Roninsosn JE. Cathepsin activity in normal and dystrophic human muscle. Enzym Biol Clin. 1968;9:175-182.
    • (1968) Enzym Biol Clin , vol.9 , pp. 175-182
    • Pennington, R.J.1    Roninsosn, J.E.2
  • 95
    • 0017227412 scopus 로고
    • Automated determination of proteolytic enzymes and of amino nitrogen by use of trinitrobenenesulfonic acid (TNBS)
    • Adams CA, Robberts TC, Butler KC. Automated determination of proteolytic enzymes and of amino nitrogen by use of trinitrobenenesulfonic acid (TNBS). Anal Biochem. 1976;70:181-186.
    • (1976) Anal Biochem , vol.70 , pp. 181-186
    • Adams, C.A.1    Robberts, T.C.2    Butler, K.C.3
  • 96
    • 0033104198 scopus 로고    scopus 로고
    • Protease and protease inhibitor assays using biotinylated casein coated on a solid phase
    • Gan ZB, Marquardt RR, Xiao H. Protease and protease inhibitor assays using biotinylated casein coated on a solid phase. Anal Biochem. 1999;268:151-156.
    • (1999) Anal Biochem , vol.268 , pp. 151-156
    • Gan, Z.B.1    Marquardt, R.R.2    Xiao, H.3
  • 98
    • 0015168544 scopus 로고
    • Intracellular protein breakdown. I. Activity determination of endopeptudases using protein substrates
    • Langer J, Ansorge S, Bohley P, Kirschke H, Hanson H. Intracellular protein breakdown. I. Activity determination of endopeptudases using protein substrates. Acta Biol Med Germ. 1971;26:935-951.
    • (1971) Acta Biol Med Germ , vol.26 , pp. 935-951
    • Langer, J.1    Ansorge, S.2    Bohley, P.3    Kirschke, H.4    Hanson, H.5
  • 99
    • 0021175656 scopus 로고
    • A modified micromethod for determination of cathepsin activity in blood serum
    • Kucharz E. A modified micromethod for determination of cathepsin activity in blood serum. Z Med Labor Diagn. 1984;25:282-284.
    • (1984) Z Med Labor Diagn , vol.25 , pp. 282-284
    • Kucharz, E.1
  • 101
    • 0015591073 scopus 로고
    • The action of cathepsin D in human articular cartilage on proteoglycans
    • Sapolsky AJ, Altman RD, Woessner JF, Howell DS. The action of cathepsin D in human articular cartilage on proteoglycans. J Clin Invest. 1973;52:624-633.
    • (1973) J Clin Invest , vol.52 , pp. 624-633
    • Sapolsky, A.J.1    Altman, R.D.2    Woessner, J.F.3    Howell, D.S.4
  • 102
    • 0016367566 scopus 로고
    • Neutral proteases and cathepsin D in human articular cartilage
    • Sapolsky AJ, Howell DS, Woessner JF. Neutral proteases and cathepsin D in human articular cartilage. J Clin Invest. 1974;53:1044-1074.
    • (1974) J Clin Invest , vol.53 , pp. 1044-1074
    • Sapolsky, A.J.1    Howell, D.S.2    Woessner, J.F.3
  • 103
    • 0021648082 scopus 로고
    • Susceptibility of different types of collagen to the action of cathepsin D
    • Pałka J, Bańkowski E, Worowski K. Susceptibility of different types of collagen to the action of cathepsin D. Ann Acad Med Biaslostoc. 1984;29:53-58.
    • (1984) Ann Acad Med Biaslostoc , vol.29 , pp. 53-58
    • Pałka, J.1    Bańkowski, E.2    Worowski, K.3
  • 104
    • 0014758581 scopus 로고
    • The use of tannin of the examination of the digestion process of casein and fibrinogen by plazmin and for the preparation of the polypeptide and products of proteolysis
    • Meybaum-Katzenellenbogen W, Kołaczkowska M. The use of tannin of the examination of the digestion process of casein and fibrinogen by plazmin and for the preparation of the polypeptide and products of proteolysis. Acta Physiol Pol. 1970;21:235-242.
    • (1970) Acta Physiol Pol , vol.21 , pp. 235-242
    • Meybaum-Katzenellenbogen, W.1    Kołaczkowska, M.2
  • 105
    • 0033571025 scopus 로고    scopus 로고
    • 96-well plate assays for measuring collagenase activity using 3H-acetylated collagen
    • Koshy PT, Rowan AD, Life PF, Cawston TE. 96-well plate assays for measuring collagenase activity using 3H-acetylated collagen. Anal Biochem. 1999;275:202-207.
    • (1999) Anal Biochem , vol.275 , pp. 202-207
    • Koshy, P.T.1    Rowan, A.D.2    Life, P.F.3    Cawston, T.E.4
  • 106
    • 0344804711 scopus 로고
    • Servey of methods used for proteolytic enzymes activity determination
    • Fukal L, Kas J, Vodrazka Z. Servey of methods used for proteolytic enzymes activity determination. Biochem Clin Bohemoslov. 1985;14:109-120.
    • (1985) Biochem Clin Bohemoslov , vol.14 , pp. 109-120
    • Fukal, L.1    Kas, J.2    Vodrazka, Z.3
  • 107
    • 0002166092 scopus 로고
    • Acomparison of two proteinases from Bacillus subtilis
    • Ottesen M, Spector A. Acomparison of two proteinases from Bacillus subtilis. Comp Rend Trav Lab Carlsberg. 1960;32:6-68.
    • (1960) Comp Rend Trav Lab Carlsberg , vol.32 , pp. 6-68
    • Ottesen, M.1    Spector, A.2
  • 108
    • 0006254485 scopus 로고
    • On the specifity and inhibition of cathepsin Dand B
    • ed. AJ Barrett, JT Dingle. North-Holland Publ Comp, Amsterdam
    • Keilova H. On the specifity and inhibition of cathepsin Dand B, in: Tissue proteinases, ed. AJ Barrett, JT Dingle. North-Holland Publ Comp, Amsterdam. 1971:45-67.
    • (1971) Tissue proteinases , pp. 45-67
    • Keilova, H.1
  • 109
    • 0020684585 scopus 로고
    • Contribution of histochemistry to the development of the proteolitic enzyme detection system in diagnostic medicine
    • Smith RF. Contribution of histochemistry to the development of the proteolitic enzyme detection system in diagnostic medicine. J. Histochem Cytochem. 1983;31:199-209.
    • (1983) J. Histochem Cytochem , vol.31 , pp. 199-209
    • Smith, R.F.1
  • 110
    • 0015011652 scopus 로고
    • The comparative specificity of acid proteinases
    • Voynick JM, Fruton JS. The comparative specificity of acid proteinases. Proc Natl Acad Sci USA. 1971;68:257-259.
    • (1971) Proc Natl Acad Sci USA , vol.68 , pp. 257-259
    • Voynick, J.M.1    Fruton, J.S.2
  • 113
    • 0016914760 scopus 로고
    • The mechanism of the catalytic action of pepsin and related acid proteinases
    • Fruton JS. The mechanism of the catalytic action of pepsin and related acid proteinases. Adr Enzymol. 1976;44:1-36.
    • (1976) Adr Enzymol , vol.44 , pp. 1-36
    • Fruton, J.S.1
  • 114
    • 0018854696 scopus 로고
    • Specificity of brain cathepsin D: Cleavage of model peptides containing the susceptible Phe-Phe regions of myelin basic protein
    • Marks N, Benuck M, Hashim G. Specificity of brain cathepsin D: cleavage of model peptides containing the susceptible Phe-Phe regions of myelin basic protein. J Neurosci Res. 1980;5:217-223.
    • (1980) J Neurosci Res , vol.5 , pp. 217-223
    • Marks, N.1    Benuck, M.2    Hashim, G.3
  • 115
    • 0020625618 scopus 로고
    • An improved cathepsin-D substrate and assay procedure
    • Agarwal N, Rich DH. An improved cathepsin-D substrate and assay procedure. Anal Biochem. 1983;130:158-165.
    • (1983) Anal Biochem , vol.130 , pp. 158-165
    • Agarwal, N.1    Rich, D.H.2
  • 116
  • 117
    • 0020507595 scopus 로고
    • Chromophoric peptide substrates for activity determination of animal aspartic proteinases in the presence of their zymogens: A movel assay
    • Pohl J, Baudys M, Kostka V. Chromophoric peptide substrates for activity determination of animal aspartic proteinases in the presence of their zymogens: a movel assay. Anal Biochem. 1983;133:104-109.
    • (1983) Anal Biochem , vol.133 , pp. 104-109
    • Pohl, J.1    Baudys, M.2    Kostka, V.3
  • 118
    • 0021415850 scopus 로고
    • The synthesis, purification, and evaluation of a new chromophoric substrate for pepsin and other aspartyl proteases
    • Dunn BM, Kammermann B, Mc Curry K. The synthesis, purification, and evaluation of a new chromophoric substrate for pepsin and other aspartyl proteases. Anal Biochem. 1984;138:68-73.
    • (1984) Anal Biochem , vol.138 , pp. 68-73
    • Dunn, B.M.1    Kammermann, B.2    Mc Curry, K.3
  • 119
    • 0022386865 scopus 로고
    • Design, synthesis and analysis of new synthetic substrates for the aspartic proteinases
    • Dunn BM, Kay J. Design, synthesis and analysis of new synthetic substrates for the aspartic proteinases. Biochem Soc Transact. 1985;13:1041-1043.
    • (1985) Biochem Soc Transact , vol.13 , pp. 1041-1043
    • Dunn, B.M.1    Kay, J.2
  • 120
    • 0022766162 scopus 로고
    • A systematic series of synthetic chromophoric substrates for aspartic proteinases
    • Dunn BM, Jiminez M, Parten BF, Valler MJ, Rolph J, Kay J. A systematic series of synthetic chromophoric substrates for aspartic proteinases. Biochem J. 1986;237:899-906.
    • (1986) Biochem J , vol.237 , pp. 899-906
    • Dunn, B.M.1    Jiminez, M.2    Parten, B.F.3    Valler, M.J.4    Rolph, J.5    Kay, J.6
  • 122
    • 0027400775 scopus 로고
    • Exploration of subsite binding specificity of human cathepsin D through kinetics and rule-based molecular modeling
    • Scarborough PE, Guruprasad K, Topham C, Richo GR, Conner GE, Blundell TL, Dunn BM. Exploration of subsite binding specificity of human cathepsin D through kinetics and rule-based molecular modeling. Prot Sci. 1993;2:269-276.
    • (1993) Prot Sci , vol.2 , pp. 269-276
    • Scarborough, P.E.1    Guruprasad, K.2    Topham, C.3    Richo, G.R.4    Conner, G.E.5    Blundell, T.L.6    Dunn, B.M.7
  • 123
    • 0030464091 scopus 로고    scopus 로고
    • Muscle aspartyl protease (cathepsin D) activity: Delection using a chromo-phoric substrate and relation to wasting in DBA/2 mice implanted with leukemic L1210 tumor cells
    • Bolger GT, Jaramillo J. Muscle aspartyl protease (cathepsin D) activity: delection using a chromo-phoric substrate and relation to wasting in DBA/2 mice implanted with leukemic L1210 tumor cells. Canad J Physiol Pharmacol. 1996;74:1141-1148.
    • (1996) Canad J Physiol Pharmacol , vol.74 , pp. 1141-1148
    • Bolger, G.T.1    Jaramillo, J.2
  • 125
    • 0015175154 scopus 로고
    • Studies on pituitary cathepsin D with artificial substrates
    • Reinharz A, Roth M. Studies on pituitary cathepsin D with artificial substrates. Enzyme. 1971;12:458-466.
    • (1971) Enzyme , vol.12 , pp. 458-466
    • Reinharz, A.1    Roth, M.2
  • 127
    • 0021710313 scopus 로고
    • A sensitive procedure for determination of cathepsin D activity in alveolar and peritonal macrophages
    • Orlowski M, Orlowski R, Chang JC, Wilk E, Lesser M. A sensitive procedure for determination of cathepsin D activity in alveolar and peritonal macrophages. Mol Cell Biochem. 1984;64:155-164.
    • (1984) Mol Cell Biochem , vol.64 , pp. 155-164
    • Orlowski, M.1    Orlowski, R.2    Chang, J.C.3    Wilk, E.4    Lesser, M.5
  • 128
    • 0021230431 scopus 로고
    • Renin cleavage of a human kidney renin substrate analogous to human angiotensinogen, H-Asp-Arg-Val-Tyr- Ile-His-Pro-Phe-His-Leu-Val-Ile-His-Ser-OH, that is human renin specific and is resistant to cathepsin D
    • Poe M, Wu JK, Lin TY, Bull NY, Slater EE. Renin cleavage of a human kidney renin substrate analogous to human angiotensinogen, H-Asp-Arg-Val-Tyr- Ile-His-Pro-Phe-His-Leu-Val-Ile-His-Ser-OH, that is human renin specific and is resistant to cathepsin D. Anal Biochem. 1984;140:459-467.
    • (1984) Anal Biochem , vol.140 , pp. 459-467
    • Poe, M.1    Wu, J.K.2    Lin, T.Y.3    Bull, N.Y.4    Slater, E.E.5
  • 129
    • 0023187066 scopus 로고
    • Comperative enzymatic studies of human renin acting on pure natural or synthetic substrates
    • Cumin F, Le-Nguyen D, Castro B, Menard J, Corvol P. Comperative enzymatic studies of human renin acting on pure natural or synthetic substrates. Biochim Biophys Acta. 1987;913:10-19.
    • (1987) Biochim Biophys Acta , vol.913 , pp. 10-19
    • Cumin, F.1    Le-Nguyen, D.2    Castro, B.3    Menard, J.4    Corvol, P.5
  • 130
    • 0023233119 scopus 로고
    • Comparison of angiotensinogen and tetradecapeptide as substrates for human renin. Substrate dependence of the mode of inhibition of renin by a statine- containing hexapeptide
    • Stammers DK, Dann JG, Harris CJ, Smith DR. Comparison of angiotensinogen and tetradecapeptide as substrates for human renin. Substrate dependence of the mode of inhibition of renin by a statine- containing hexapeptide. Arch Biochem Biophys. 1987;258:413-420.
    • (1987) Arch Biochem Biophys , vol.258 , pp. 413-420
    • Stammers, D.K.1    Dann, J.G.2    Harris, C.J.3    Smith, D.R.4
  • 131
    • 0029132730 scopus 로고    scopus 로고
    • Adenis A, Huet G, Zerimech F, Hecquet B, Balduyck M, Peyrat JP. Cathepsin B, L and D activities in colorectal carcinomas: relationship with clinico-pathological parameters. Canc Lett. 1995;96:267-275.
    • Adenis A, Huet G, Zerimech F, Hecquet B, Balduyck M, Peyrat JP. Cathepsin B, L and D activities in colorectal carcinomas: relationship with clinico-pathological parameters. Canc Lett. 1995;96:267-275.
  • 132
    • 0030850908 scopus 로고    scopus 로고
    • Western immunoblotting and enzymatic activity analysis of cathepsin D in human breast cancer cell lines of different invasive potential. Regulation by 17β-estradiol, tamoxifen and ICI 182,780
    • Couissi D, Dubois V, Remacle C, Schonne E, Trouet A. Western immunoblotting and enzymatic activity analysis of cathepsin D in human breast cancer cell lines of different invasive potential. Regulation by 17β-estradiol, tamoxifen and ICI 182,780. Clin Exp Metastasis. 1997;15:349-360.
    • (1997) Clin Exp Metastasis , vol.15 , pp. 349-360
    • Couissi, D.1    Dubois, V.2    Remacle, C.3    Schonne, E.4    Trouet, A.5
  • 134
    • 0022922314 scopus 로고
    • Schistosoma japonicum: Ultra-structural localization of a hemoglobinase using mercury labelled pepstatin
    • Bogitsh BJ, Kirshner KF. Schistosoma japonicum: ultra-structural localization of a hemoglobinase using mercury labelled pepstatin. Exp Parasitol. 1986;62:211-215.
    • (1986) Exp Parasitol , vol.62 , pp. 211-215
    • Bogitsh, B.J.1    Kirshner, K.F.2
  • 136
    • 0029953972 scopus 로고    scopus 로고
    • Self-activation of recombinant human lysosomal procathepsin D at a newly engineered cleavage junction, "short" pseudocathepsin D
    • Beyer BM, Dunn BM. Self-activation of recombinant human lysosomal procathepsin D at a newly engineered cleavage junction, "short" pseudocathepsin D. J Biol Chem. 1996;271:15590-15596.
    • (1996) J Biol Chem , vol.271 , pp. 15590-15596
    • Beyer, B.M.1    Dunn, B.M.2
  • 139
    • 0032170893 scopus 로고    scopus 로고
    • Cathepsin substrates as cleavable peptide linkers in bioconjugates, selected from a fluorescence quench combinatorial libray
    • Peterson JJ, Meares CF. Cathepsin substrates as cleavable peptide linkers in bioconjugates, selected from a fluorescence quench combinatorial libray. Bioconjug Chem. 1998;9:618-626.
    • (1998) Bioconjug Chem , vol.9 , pp. 618-626
    • Peterson, J.J.1    Meares, C.F.2
  • 140
    • 0032746069 scopus 로고    scopus 로고
    • Developmental expression od cathepsin D aspartic protease in Schistosoma japonicum
    • Verity CK, McManus DP, Brindley PJ. Developmental expression od cathepsin D aspartic protease in Schistosoma japonicum. Int J Parasitol. 1999;29:1819-1824.
    • (1999) Int J Parasitol , vol.29 , pp. 1819-1824
    • Verity, C.K.1    McManus, D.P.2    Brindley, P.J.3
  • 141
    • 0032790483 scopus 로고    scopus 로고
    • Characterization of new fluorogenic substrates for the rapid and sensitive assay of cathepsin E and cathepsin D
    • Yasuda Y, Kageyama T, Akamine A, Shibata M, Kominami E, Uchiyama Y, Yamamoto K. Characterization of new fluorogenic substrates for the rapid and sensitive assay of cathepsin E and cathepsin D. J Biochem. 1999;125:1137-1143.
    • (1999) J Biochem , vol.125 , pp. 1137-1143
    • Yasuda, Y.1    Kageyama, T.2    Akamine, A.3    Shibata, M.4    Kominami, E.5    Uchiyama, Y.6    Yamamoto, K.7
  • 143
    • 0035846971 scopus 로고    scopus 로고
    • Substrate specificity of human cathepsin D using internally quenched fluorescent peptides derived from reactive site loop of kallistatin
    • Pimenta DC, Oliveira A, Juliano MA, Juliano L. Substrate specificity of human cathepsin D using internally quenched fluorescent peptides derived from reactive site loop of kallistatin. Biochem biophys Acta. 2001;1544:113-122.
    • (2001) Biochem biophys Acta , vol.1544 , pp. 113-122
    • Pimenta, D.C.1    Oliveira, A.2    Juliano, M.A.3    Juliano, L.4
  • 144
    • 1842422074 scopus 로고    scopus 로고
    • Todarepsin, a new cathepsin D from hepatopancreas of Japanese common squid (Todarodes pacificus)
    • Part B
    • Komai T, Kawabata C, Amano M, Lee BR, Ichishima E. Todarepsin, a new cathepsin D from hepatopancreas of Japanese common squid (Todarodes pacificus). Biochem Physiol Part B. 2004;137:373-382.
    • (2004) Biochem Physiol , vol.137 , pp. 373-382
    • Komai, T.1    Kawabata, C.2    Amano, M.3    Lee, B.R.4    Ichishima, E.5
  • 145
    • 14844311944 scopus 로고    scopus 로고
    • Biotinylated fluorescent peptide substrates for the sensitive and specific determination of cathepsin D activity
    • Baechle D, Cansier A, Fischer R, Brandenburg J, Burster T, Driessen C, Kalbacher H. Biotinylated fluorescent peptide substrates for the sensitive and specific determination of cathepsin D activity. J Pept Sci. 2005;11:166-175.
    • (2005) J Pept Sci , vol.11 , pp. 166-175
    • Baechle, D.1    Cansier, A.2    Fischer, R.3    Brandenburg, J.4    Burster, T.5    Driessen, C.6    Kalbacher, H.7
  • 146
    • 0021076892 scopus 로고
    • Immunoelectron microscopic localization. of cathepsin D in lysosomes of rat nerve
    • Yokata S, Atsumi S. Immunoelectron microscopic localization. of cathepsin D in lysosomes of rat nerve. Histochemistry. 1983;79:345-352.
    • (1983) Histochemistry , vol.79 , pp. 345-352
    • Yokata, S.1    Atsumi, S.2
  • 147
    • 0018787714 scopus 로고
    • Inhibition of cathepsin D by syntetic oligopeptides
    • Lin TY, Williams HR. Inhibition of cathepsin D by syntetic oligopeptides. J Biol Chem. 1979;254:11875-11883.
    • (1979) J Biol Chem , vol.254 , pp. 11875-11883
    • Lin, T.Y.1    Williams, H.R.2
  • 148
    • 0033018967 scopus 로고    scopus 로고
    • Chromogenic and fluorogenic glycosylated and acetylglycosylated peptides as substrates for serine, thiol and aspartyl protease
    • Juliano MA, Filira F, Gobbo M, Rocchi R, Del Nery E, Juliano L. Chromogenic and fluorogenic glycosylated and acetylglycosylated peptides as substrates for serine, thiol and aspartyl protease. J Peptide Res. 1999;53:109-119.
    • (1999) J Peptide Res , vol.53 , pp. 109-119
    • Juliano, M.A.1    Filira, F.2    Gobbo, M.3    Rocchi, R.4    Del Nery, E.5    Juliano, L.6
  • 149
    • 0029026723 scopus 로고
    • Active-site titration of peptidases
    • Knight CG. Active-site titration of peptidases. Meth Enzymol. 1995;248:85-101.
    • (1995) Meth Enzymol , vol.248 , pp. 85-101
    • Knight, C.G.1
  • 150
    • 0030799193 scopus 로고    scopus 로고
    • Determination of pepstatin-sensitive carboxyl proteases by using pepstatinyldansyldiaminopropane (dansyl-pepstatin) as an active site titrant
    • Yonezawa H, Uchikoba T, Kaneda M. Determination of pepstatin-sensitive carboxyl proteases by using pepstatinyldansyldiaminopropane (dansyl-pepstatin) as an active site titrant. J Biochem. 1997;122:294-299.
    • (1997) J Biochem , vol.122 , pp. 294-299
    • Yonezawa, H.1    Uchikoba, T.2    Kaneda, M.3
  • 151
    • 0019755211 scopus 로고
    • Immunological studies of tissue proteinases
    • Pole AR. Immunological studies of tissue proteinases. Sub-cell Biochem. 1981;8:311-356.
    • (1981) Sub-cell Biochem , vol.8 , pp. 311-356
    • Pole, A.R.1
  • 152
    • 9444250436 scopus 로고    scopus 로고
    • Tumminello FM, Leto G, Pizzolanti G, Candiloro V, Crescimanno M, Crosta L, Flandina C, Montalto G, Soresi M, Carroccio A, Bascone F, Ruggeri I, Ippolito S, Gebbia N. Cathepsin D, B and L circulating levels as prognostic markers of malignant progression. Anticanc Res. 1996;16:2315-2320.
    • Tumminello FM, Leto G, Pizzolanti G, Candiloro V, Crescimanno M, Crosta L, Flandina C, Montalto G, Soresi M, Carroccio A, Bascone F, Ruggeri I, Ippolito S, Gebbia N. Cathepsin D, B and L circulating levels as prognostic markers of malignant progression. Anticanc Res. 1996;16:2315-2320.
  • 153
  • 155
    • 0342571059 scopus 로고
    • Antibodies to enzymes and their use, with specific reference to cathepsin D and other lysosomal enzymes
    • ed. Dingle JT. North Holland Elsevier Amsterdam
    • Weston PD, Poole AR. Antibodies to enzymes and their use, with specific reference to cathepsin D and other lysosomal enzymes. In: Lysosomes in biology and pathology, ed. Dingle JT. North Holland Elsevier Amsterdam. 1973;3:425-464.
    • (1973) Lysosomes in biology and pathology , vol.3 , pp. 425-464
    • Weston, P.D.1    Poole, A.R.2
  • 156
    • 0016836644 scopus 로고
    • Influence of starvation on the activities and localization of cathepsin D and other lysosomal enzymes in hearts of rabbits and mice
    • Wildenthal K, Poole AR, Dingle JT. Influence of starvation on the activities and localization of cathepsin D and other lysosomal enzymes in hearts of rabbits and mice. J Mol Cell Cardiol. 1975;7:841-855
    • (1975) J Mol Cell Cardiol , vol.7 , pp. 841-855
    • Wildenthal, K.1    Poole, A.R.2    Dingle, J.T.3
  • 157
    • 0033990363 scopus 로고    scopus 로고
    • A procathepsin D specific monoclonal antibody that recognizes procathepsin D but not cathepsin D
    • Kopitar-Jerala N, Turk V. A procathepsin D specific monoclonal antibody that recognizes procathepsin D but not cathepsin D. Immunol Lett. 1999;70:211-212.
    • (1999) Immunol Lett , vol.70 , pp. 211-212
    • Kopitar-Jerala, N.1    Turk, V.2
  • 159
    • 0015071117 scopus 로고
    • Characteristics of immunoinhibition and the confirmation of a role in cartilage breakdown
    • Dingle JT, Barrett AJ, Weston PD. Cathepsin D. Characteristics of immunoinhibition and the confirmation of a role in cartilage breakdown. Biochem J. 1971;123:1-13.
    • (1971) Biochem J , vol.123 , pp. 1-13
    • Dingle, J.T.1    Barrett, A.J.2    Weston, P.D.3    Cathepsin, D.4
  • 160
    • 73549106299 scopus 로고
    • The effect of antibodies on activity of enzymes
    • Koj A. The effect of antibodies on activity of enzymes. Zesz Nauk UJ. 1976;435:55-66.
    • (1976) Zesz Nauk UJ , vol.435 , pp. 55-66
    • Koj, A.1
  • 161
    • 0028787794 scopus 로고
    • Comparison of cathepsin D determinations in human carcinomas by enzyme immunoassay and immunoradiometric assay
    • Shaheen RM, Miseljic S, Doering DL, Wittliff JL. Comparison of cathepsin D determinations in human carcinomas by enzyme immunoassay and immunoradiometric assay. J Clin Lab Anal. 1995;9:351-358.
    • (1995) J Clin Lab Anal , vol.9 , pp. 351-358
    • Shaheen, R.M.1    Miseljic, S.2    Doering, D.L.3    Wittliff, J.L.4
  • 162
    • 0017572454 scopus 로고
    • The role of lysosomal enzymes in protein degradation in different types of rat liver cells
    • Knook DL. The role of lysosomal enzymes in protein degradation in different types of rat liver cells. Acta Biol Med Germ. 1977;36:1747-1752.
    • (1977) Acta Biol Med Germ , vol.36 , pp. 1747-1752
    • Knook, D.L.1
  • 163
    • 0019723198 scopus 로고
    • Identification and possible regulation of muscle cell lysosomal protease activity by exogenous protease inhibitors
    • Stauber WT, Gauthier F, Ong SH. Identification and possible regulation of muscle cell lysosomal protease activity by exogenous protease inhibitors. Acta Biol Med Germ. 1981;40:1317-1322.
    • (1981) Acta Biol Med Germ , vol.40 , pp. 1317-1322
    • Stauber, W.T.1    Gauthier, F.2    Ong, S.H.3
  • 166
    • 0024332791 scopus 로고
    • Quantitation and immunohistochemical localization of cathepsins E and D in rat tissues and blood cells
    • Sakai H, Saku T, Kato Y, Yamamoto K. Quantitation and immunohistochemical localization of cathepsins E and D in rat tissues and blood cells. Biochim Biophys Acta. 1989;991:367-375.
    • (1989) Biochim Biophys Acta , vol.991 , pp. 367-375
    • Sakai, H.1    Saku, T.2    Kato, Y.3    Yamamoto, K.4
  • 167
    • 0030058244 scopus 로고    scopus 로고
    • Prognostic value of cathepsin D in breast cancer: Comparison of immunohistochemical and immunoradiometric detection methods
    • Gohring UJ, Scharl A, Thelen U, Ahr A, Crombach G, Titius BR. Prognostic value of cathepsin D in breast cancer: comparison of immunohistochemical and immunoradiometric detection methods. J Clin Pathol. 1996;49:57-64.
    • (1996) J Clin Pathol , vol.49 , pp. 57-64
    • Gohring, U.J.1    Scharl, A.2    Thelen, U.3    Ahr, A.4    Crombach, G.5    Titius, B.R.6
  • 168
    • 0029815541 scopus 로고    scopus 로고
    • Immunolocalization of cathepsin D in pneumocytes of normal human lung and in pulmonary fibrosis
    • Kasper M, Lackie P, Haase M, Schuh D, Müller M. Immunolocalization of cathepsin D in pneumocytes of normal human lung and in pulmonary fibrosis. Virchows Arch. 1996;428:207-215.
    • (1996) Virchows Arch , vol.428 , pp. 207-215
    • Kasper, M.1    Lackie, P.2    Haase, M.3    Schuh, D.4    Müller, M.5
  • 169
    • 0031845006 scopus 로고    scopus 로고
    • Immunocytochemical evaluation of gastric mucosal cathepsin D in peptic ulcer
    • Długosz A, Chosia M. Immunocytochemical evaluation of gastric mucosal cathepsin D in peptic ulcer. Pol J Pathol. 1998;49:77-82.
    • (1998) Pol J Pathol , vol.49 , pp. 77-82
    • Długosz, A.1    Chosia, M.2
  • 170
    • 0042378751 scopus 로고    scopus 로고
    • Cathepsin D expression in normal, hyperplastic and malignant endometrial tissue: An immunohistochemical analysis
    • Mylonas J, Makovitzky J, Richer DU, Jeschke U, Briese V, Friese K. Cathepsin D expression in normal, hyperplastic and malignant endometrial tissue: an immunohistochemical analysis. Acta Histochem. 2003;105:245-252.
    • (2003) Acta Histochem , vol.105 , pp. 245-252
    • Mylonas, J.1    Makovitzky, J.2    Richer, D.U.3    Jeschke, U.4    Briese, V.5    Friese, K.6
  • 171
    • 0019775299 scopus 로고
    • Bimane-labelled pepstatin, a fluorescent probe for the subcellular location of cathepsin D
    • Matthews ITW, Decker RS, Knight CG. Bimane-labelled pepstatin, a fluorescent probe for the subcellular location of cathepsin D. Biochem J. 1981;199:611-617.
    • (1981) Biochem J , vol.199 , pp. 611-617
    • Matthews, I.T.W.1    Decker, R.S.2    Knight, C.G.3
  • 172
    • 0018849168 scopus 로고
    • Resistance to ischemic damage in hearts of starved rabbits. Correlation with lysosomal alternations and delayed release of cathepsin D
    • Decker RS, Crie JS, Poolet AR, Dingle JT, Wildenthal K. Resistance to ischemic damage in hearts of starved rabbits. Correlation with lysosomal alternations and delayed release of cathepsin D. Lab. Invest. 1980;43:197-2007.
    • (1980) Lab. Invest , vol.43 , pp. 197-2007
    • Decker, R.S.1    Crie, J.S.2    Poolet, A.R.3    Dingle, J.T.4    Wildenthal, K.5
  • 173
    • 73549097263 scopus 로고
    • Histoand cytochemical studies of cathepsin D using a specific inhibitor- pepstatin
    • Yamato S, Hirabayashi Y, Uematsu H, Sugihara H. Histoand cytochemical studies of cathepsin D using a specific inhibitor- pepstatin. J Histochem Cytochem. 1982;30:597-599.
    • (1982) J Histochem Cytochem , vol.30 , pp. 597-599
    • Yamato, S.1    Hirabayashi, Y.2    Uematsu, H.3    Sugihara, H.4
  • 174
    • 84907125501 scopus 로고
    • An improved procedure for the histochemical demonstration of cathepsin D by the mercury-labeled pepstatin method
    • Yamato S, Hirabayashi Y, Sugihara H. An improved procedure for the histochemical demonstration of cathepsin D by the mercury-labeled pepstatin method. Stain Technol. 1984;59:113-120.
    • (1984) Stain Technol , vol.59 , pp. 113-120
    • Yamato, S.1    Hirabayashi, Y.2    Sugihara, H.3
  • 175
    • 0023039303 scopus 로고
    • The AMeX method a simplified technique of tissue processing and paraffin embedding with improved preservation of antigens for immunostaining
    • Sato Y, Mukai K, Watanabe S, Gotoh M, Shimosato Y. The AMeX method a simplified technique of tissue processing and paraffin embedding with improved preservation of antigens for immunostaining. Am J Pathol. 1986;125:431-435.
    • (1986) Am J Pathol , vol.125 , pp. 431-435
    • Sato, Y.1    Mukai, K.2    Watanabe, S.3    Gotoh, M.4    Shimosato, Y.5
  • 176
  • 177
    • 0019423594 scopus 로고
    • Use of avidin-biotin-peroxidase complex (ABC) in immunoperoxidase techniques: A comparison between ABC and unlabeled antibody (PAP) procedures
    • Hsu SM, Raine L, Fanger H. Use of avidin-biotin-peroxidase complex (ABC) in immunoperoxidase techniques: a comparison between ABC and unlabeled antibody (PAP) procedures. J Histochem Cytochem. 1981;29:577-580.
    • (1981) J Histochem Cytochem , vol.29 , pp. 577-580
    • Hsu, S.M.1    Raine, L.2    Fanger, H.3
  • 178
  • 179
    • 0021029449 scopus 로고
    • Conformation and protease binding activity of binary and ternary human alpha 2-macroglobulin-protease complexes
    • Gonias SL, Pizzo SV. Conformation and protease binding activity of binary and ternary human alpha 2-macroglobulin-protease complexes. J Biol Chem. 1983;258:14682-14692.
    • (1983) J Biol Chem , vol.258 , pp. 14682-14692
    • Gonias, S.L.1    Pizzo, S.V.2
  • 180
    • 28244494664 scopus 로고
    • Interaction of cathepsin D and pepsin with a2-macroglobulin
    • ed. Kostka V. Walter de Gruyter Berlin
    • Lah T, Vihar M, Turk V. Interaction of cathepsin D and pepsin with a2-macroglobulin. In: Aspartic proteinases and their inhibitors, ed. Kostka V. Walter de Gruyter Berlin. 1985:485-490.
    • (1985) Aspartic proteinases and their inhibitors , pp. 485-490
    • Lah, T.1    Vihar, M.2    Turk, V.3
  • 181
    • 0015896128 scopus 로고
    • The interaction of a2-macroglobulin with proteinases. Characteristics and specificity of the reaction, and a hypothesis concerning its molecular mechanism
    • Barrett AJ, Starkey PM. The interaction of a2-macroglobulin with proteinases. Characteristics and specificity of the reaction, and a hypothesis concerning its molecular mechanism. Biochem J. 1973;133:709-724.
    • (1973) Biochem J , vol.133 , pp. 709-724
    • Barrett, A.J.1    Starkey, P.M.2
  • 182
    • 0024519316 scopus 로고
    • Inhibition of aspartic proteinases by a2-macroglobulin
    • Thomas DJ, Richards AD, Kay J. Inhibition of aspartic proteinases by a2-macroglobulin. Biochem J. 1989;259:905-907.
    • (1989) Biochem J , vol.259 , pp. 905-907
    • Thomas, D.J.1    Richards, A.D.2    Kay, J.3
  • 183
    • 1642484414 scopus 로고
    • Alpha-2-macroglobulin: Reference values in serum and plasma with a chromogenic substrate (chromozym TRY)
    • Witt I, Tritschler W, Bablok W. Alpha-2-macroglobulin: reference values in serum and plasma with a chromogenic substrate (chromozym TRY). J Clin Chem Biochem. 1981;19:877-878.
    • (1981) J Clin Chem Biochem , vol.19 , pp. 877-878
    • Witt, I.1    Tritschler, W.2    Bablok, W.3
  • 185
    • 0021672321 scopus 로고
    • Detection of a2-macroglobulin-associated proteases in the plasma of patients with rheumatoid arthritis
    • Gaspar A, Skosey JL, Sequeira W, Teodorescu M. Detection of a2-macroglobulin-associated proteases in the plasma of patients with rheumatoid arthritis. Clin Chem. 1984;30:1517-1522.
    • (1984) Clin Chem , vol.30 , pp. 1517-1522
    • Gaspar, A.1    Skosey, J.L.2    Sequeira, W.3    Teodorescu, M.4
  • 186
    • 3843076999 scopus 로고
    • The unique nature of the interaction of a2-macroglobulin with proteinases
    • ed. Fritz H, Tschesche H, Greene LG, Truscheit E. Springer-Verlag Berlin
    • Barrett AJ, Starkey PM, Munn EA. The unique nature of the interaction of a2-macroglobulin with proteinases. In: Proteinases inhibitors, ed. Fritz H, Tschesche H, Greene LG, Truscheit E. Springer-Verlag Berlin. 1974:72-77.
    • (1974) Proteinases inhibitors , pp. 72-77
    • Barrett, A.J.1    Starkey, P.M.2    Munn, E.A.3
  • 187
    • 0018647589 scopus 로고
    • Characterization of alkylamine-sensitive site in a2-macroglobulin
    • Swenson RP, Howard JB. Characterization of alkylamine-sensitive site in a2-macroglobulin. Proc Natl Acad Sci USA. 1979;7614:4313-4316.
    • (1979) Proc Natl Acad Sci USA , vol.7614 , pp. 4313-4316
    • Swenson, R.P.1    Howard, J.B.2
  • 188
    • 0015689310 scopus 로고
    • Study on the plasmatic elimination of the a2-macroglobulin proteinase complexes
    • Blatrix C, Amouch P, Drouet J, Steinbuch M. Study on the plasmatic elimination of the a2-macroglobulin proteinase complexes. Path Biol. 1973;21:11-14.
    • (1973) Path Biol , vol.21 , pp. 11-14
    • Blatrix, C.1    Amouch, P.2    Drouet, J.3    Steinbuch, M.4
  • 190
    • 85009304345 scopus 로고    scopus 로고
    • Karwowska A, Gacko M, Worowska A. Aktywność proteolityczna i hamowanie aktywnooeci katepsyny D przez z nasion soczewicy. Bromat Chem Toksykol. 2008;41:in press.
    • Karwowska A, Gacko M, Worowska A. Aktywność proteolityczna i hamowanie aktywnooeci katepsyny D przez z nasion soczewicy. Bromat Chem Toksykol. 2008;41:in press.
  • 191
    • 73549106778 scopus 로고    scopus 로고
    • Inhibition of pepsin activity and cathepsin D activity by seed extracts of plants consumed by human
    • Karwowska A, Gacko M, Worowska M. Inhibition of pepsin activity and cathepsin D activity by seed extracts of plants consumed by human. Bromat Chem Toksykol. 2008;41:258-261.
    • (2008) Bromat Chem Toksykol , vol.41 , pp. 258-261
    • Karwowska, A.1    Gacko, M.2    Worowska, M.3
  • 192
    • 0015326896 scopus 로고
    • The inhibition of tissue acid proteinases by pepstatin
    • Barrett AJ, Dingle JT. The inhibition of tissue acid proteinases by pepstatin. Biochem J. 1972;127:439-441.
    • (1972) Biochem J , vol.127 , pp. 439-441
    • Barrett, A.J.1    Dingle, J.T.2
  • 193
    • 0015861774 scopus 로고
    • Relationship between the inhibition constant (Ki) and the concentration of inhibitor which causes 50 percent inhibitions (I50) of on enzymatic reaction
    • Chang Y, Prusoff WH. Relationship between the inhibition constant (Ki) and the concentration of inhibitor which causes 50 percent inhibitions (I50) of on enzymatic reaction. Biochem Pharmacol. 1973;22:3099-3108.
    • (1973) Biochem Pharmacol , vol.22 , pp. 3099-3108
    • Chang, Y.1    Prusoff, W.H.2
  • 194
    • 0027480953 scopus 로고
    • Pepstatins: Aspartic proteinase inhibitors having potential therapeutic applications
    • Tumminello FM, Bernacki RJ, Gebbia N, Leto G. Pepstatins: aspartic proteinase inhibitors having potential therapeutic applications. Med Res Rev. 1993;13:199-208.
    • (1993) Med Res Rev , vol.13 , pp. 199-208
    • Tumminello, F.M.1    Bernacki, R.J.2    Gebbia, N.3    Leto, G.4
  • 195
    • 0016234396 scopus 로고
    • Kinetics of irreversible enzyme inhibition by an unstable inhibitor
    • Rakitzis ET. Kinetics of irreversible enzyme inhibition by an unstable inhibitor. Biochem J. 1974;141:601-603.
    • (1974) Biochem J , vol.141 , pp. 601-603
    • Rakitzis, E.T.1
  • 196
    • 33645346169 scopus 로고
    • Studies on the mung bean trypsin inhibitor
    • ed. Bradshaw RA, Hill RL, Tang J. Acad Press NY
    • Chi CW, Lo SS, Tan FL, Zhang YS, Chu HM. Studies on the mung bean trypsin inhibitor. In: Proteins in biology and medicine, ed. Bradshaw RA, Hill RL, Tang J. Acad Press NY. 1982:341-362.
    • (1982) Proteins in biology and medicine , pp. 341-362
    • Chi, C.W.1    Lo, S.S.2    Tan, F.L.3    Zhang, Y.S.4    Chu, H.M.5
  • 197
    • 0018569867 scopus 로고
    • The action of potato inhibitors on activation of zymogen forms of digestive system proteases
    • Worowski K, Gabrylewicz A, Roszkowska W, Bajko K. The action of potato inhibitors on activation of zymogen forms of digestive system proteases. Acta Hepato-Gastroenterol. 1979;26:413-416.
    • (1979) Acta Hepato-Gastroenterol , vol.26 , pp. 413-416
    • Worowski, K.1    Gabrylewicz, A.2    Roszkowska, W.3    Bajko, K.4
  • 198
    • 4644287416 scopus 로고    scopus 로고
    • Red wine polyphenolic compounds strongly inhibit pro-matrix metalloproteinase-2 expression and its activation in response to thrombin via direct inhibition of membrane type 1-matrix metalloproteinase in vascular smooth muscle cells
    • Oak MH, El Bedoui J, Anglard P, Schini-Kerth VB. Red wine polyphenolic compounds strongly inhibit pro-matrix metalloproteinase-2 expression and its activation in response to thrombin via direct inhibition of membrane type 1-matrix metalloproteinase in vascular smooth muscle cells. Circulation. 2004;110:1861-1867.
    • (2004) Circulation , vol.110 , pp. 1861-1867
    • Oak, M.H.1    El Bedoui, J.2    Anglard, P.3    Schini-Kerth, V.B.4
  • 199
    • 73549112648 scopus 로고
    • Residual bodies and cellular defecation
    • ed. Dingle JT. North-Holland Publ Comp Amsterdam-London
    • Daems WT, Wisse E, Brederoo P. Residual bodies and cellular defecation. In: Lysosomes a laboratory handbook, ed. Dingle JT. North-Holland Publ Comp Amsterdam-London. 1972:183-189.
    • (1972) Lysosomes a laboratory handbook , pp. 183-189
    • Daems, W.T.1    Wisse, E.2    Brederoo, P.3
  • 200
    • 0004266608 scopus 로고
    • Plenum Press NY
    • Holtzman E. Lysosomes. Plenum Press NY. 1989:25-92.
    • (1989) Lysosomes , pp. 25-92
    • Holtzman, E.1
  • 202
    • 0017072383 scopus 로고
    • Correlation of plasma lysosomal enzyme levels with hepatic reticuloendothelial function after trauma
    • Loegering DJ, Kaplan JE, Saba TM. Correlation of plasma lysosomal enzyme levels with hepatic reticuloendothelial function after trauma. Proc Soc Exp Biol Med. 1976;152:42-46.
    • (1976) Proc Soc Exp Biol Med , vol.152 , pp. 42-46
    • Loegering, D.J.1    Kaplan, J.E.2    Saba, T.M.3
  • 203
    • 0026530280 scopus 로고
    • Cathepsin D in the malignant progression of neoplastic diseases (review)
    • Leto G, Gebbia N, Rausa L, Tumminello FM. Cathepsin D in the malignant progression of neoplastic diseases (review). Anticanc Res. 1992;12:235-248.
    • (1992) Anticanc Res , vol.12 , pp. 235-248
    • Leto, G.1    Gebbia, N.2    Rausa, L.3    Tumminello, F.M.4
  • 204
    • 2942711855 scopus 로고    scopus 로고
    • Cathepsin D expression levels in nongynecological solid tumors: Clinical and therapeutic implications
    • Leto G, Tumminello FM, Crescimanno M, Flandina C, Gebbia N. Cathepsin D expression levels in nongynecological solid tumors: Clinical and therapeutic implications. Clin Exp Metastas. 2004;21:91-106.
    • (2004) Clin Exp Metastas , vol.21 , pp. 91-106
    • Leto, G.1    Tumminello, F.M.2    Crescimanno, M.3    Flandina, C.4    Gebbia, N.5
  • 205
    • 0029021787 scopus 로고
    • Tissue cathepsin as tumor markers
    • Schwartz MK. Tissue cathepsin as tumor markers. Clin Chim Acta. 1995;237:67-78.
    • (1995) Clin Chim Acta , vol.237 , pp. 67-78
    • Schwartz, M.K.1
  • 206
    • 0014837519 scopus 로고
    • Autoradiographic study on the site of uptake of the haptoglobin-hemoglobin complex
    • Wada T, Ohara H, Watanabe K, Kinoshita H, Yachi A. Autoradiographic study on the site of uptake of the haptoglobin-hemoglobin complex. J Reticuloendothel Soc. 1970;8:185-193.
    • (1970) J Reticuloendothel Soc , vol.8 , pp. 185-193
    • Wada, T.1    Ohara, H.2    Watanabe, K.3    Kinoshita, H.4    Yachi, A.5
  • 207
    • 0017757964 scopus 로고
    • Cathepsin clearance from the circulation and reticuloendothelial function
    • Loegering DJ, Carr FK, Saba TM. Cathepsin clearance from the circulation and reticuloendothelial function. Exp Mol Pathol. 1977;27:277-283.
    • (1977) Exp Mol Pathol , vol.27 , pp. 277-283
    • Loegering, D.J.1    Carr, F.K.2    Saba, T.M.3
  • 208
    • 0017651253 scopus 로고
    • The effects of purified cathepsin D infusions in intact animals
    • Mason MS, Wangensteen SL. The effects of purified cathepsin D infusions in intact animals. Am J Surg. 1977;134:278-282.
    • (1977) Am J Surg , vol.134 , pp. 278-282
    • Mason, M.S.1    Wangensteen, S.L.2
  • 209
    • 0014964342 scopus 로고
    • Comparative studies regarding different ways of expression of enzymatic activity
    • de Alaniz MJT, de Gomez Dumm IN, Brenner RR. Comparative studies regarding different ways of expression of enzymatic activity. Enzymologia. 1970;38:85-88.
    • (1970) Enzymologia , vol.38 , pp. 85-88
    • de Alaniz, M.J.T.1    de Gomez Dumm, I.N.2    Brenner, R.R.3
  • 210
    • 0014708923 scopus 로고
    • The meaning of enzyme activity measurements in human tissues
    • Frei J. The meaning of enzyme activity measurements in human tissues. Enzymol Biol Clin. 1970;11:3-7.
    • (1970) Enzymol Biol Clin , vol.11 , pp. 3-7
    • Frei, J.1
  • 211
    • 0021362115 scopus 로고    scopus 로고
    • Fiszer-Szafarz DNA and protein content as cellular biochemical parameters. A discussion with two examples: acid phosphatase and cathepsin D in rat liver and hepatoma and acid phosphatase in human breast normal tissue and adenocarcinoma. Anal Biochem. 1984;138:255-258.
    • Fiszer-Szafarz DNA and protein content as cellular biochemical parameters. A discussion with two examples: acid phosphatase and cathepsin D in rat liver and hepatoma and acid phosphatase in human breast normal tissue and adenocarcinoma. Anal Biochem. 1984;138:255-258.
  • 213
    • 38649115735 scopus 로고    scopus 로고
    • Kay J, Tatnell PJ. Cathepsin E. In: Handbook of proteolytic enzymes, ed. Barrett AJ, Rawling ND, Woessner JF. Elsevier Amsterdam. 2004;1:33-38.
    • Kay J, Tatnell PJ. Cathepsin E. In: Handbook of proteolytic enzymes, ed. Barrett AJ, Rawling ND, Woessner JF. Elsevier Amsterdam. 2004;1:33-38.
  • 214
    • 38649116012 scopus 로고    scopus 로고
    • Zaidi N, Kalbacher H. Cathepsin E: a mini review. Biochem Biophys Res Commun. 2008;367:517-522.
    • Zaidi N, Kalbacher H. Cathepsin E: a mini review. Biochem Biophys Res Commun. 2008;367:517-522.
  • 215
    • 0022274452 scopus 로고
    • The interaction of aspartic proteinases with naturally-occurring inhibitors from actinomycetes and Ascaris lumbricoides
    • Valler MJ, Kay J, Aoyagi T, Dunn BM. The interaction of aspartic proteinases with naturally-occurring inhibitors from actinomycetes and Ascaris lumbricoides. J Enzyme Inhib. 1985;1:77-82.
    • (1985) J Enzyme Inhib , vol.1 , pp. 77-82
    • Valler, M.J.1    Kay, J.2    Aoyagi, T.3    Dunn, B.M.4
  • 217
    • 0019170989 scopus 로고
    • Enzymes of lysosomal origin in human plasma and serum: Assay conditions and parameters influencing the assay
    • Lombardo A, Caimi L, Marchesini S, Goi GC, Tettamanti G. Enzymes of lysosomal origin in human plasma and serum: assay conditions and parameters influencing the assay. Clin Chim Acta. 1980;108:337-346.
    • (1980) Clin Chim Acta , vol.108 , pp. 337-346
    • Lombardo, A.1    Caimi, L.2    Marchesini, S.3    Goi, G.C.4    Tettamanti, G.5
  • 220
    • 0037600728 scopus 로고    scopus 로고
    • Characterization of cheese proteolysis by capillary electrophoresis and reverse-phase HPLC analyses of peptides
    • Molina E, Ramos M, Cifuentes A, Lopez-Fandino R. Characterization of cheese proteolysis by capillary electrophoresis and reverse-phase HPLC analyses of peptides. Z Lebensm Unters Forsch. 1998;206:259-263.
    • (1998) Z Lebensm Unters Forsch , vol.206 , pp. 259-263
    • Molina, E.1    Ramos, M.2    Cifuentes, A.3    Lopez-Fandino, R.4
  • 221
    • 0030576587 scopus 로고    scopus 로고
    • Analysis of cathepsin D from breast tissues by capillary electrophoresis
    • Shihabi ZK, Kute TE. Analysis of cathepsin D from breast tissues by capillary electrophoresis. J. Chromat B. 1996;683:125-131.
    • (1996) J. Chromat B , vol.683 , pp. 125-131
    • Shihabi, Z.K.1    Kute, T.E.2
  • 222
    • 0032727822 scopus 로고    scopus 로고
    • Capillary electrophoretic determination of cathepsin D activity using Oregon Green-labeled hemoglobin
    • Chu Q, Jones S, Zeece M. Capillary electrophoretic determination of cathepsin D activity using Oregon Green-labeled hemoglobin. Electrophoresis. 1999;20:2945-2951.
    • (1999) Electrophoresis , vol.20 , pp. 2945-2951
    • Chu, Q.1    Jones, S.2    Zeece, M.3
  • 223
    • 0041743253 scopus 로고    scopus 로고
    • Determination of cathepsin D activity in MCF-7 cells by capillary zone electrophoresis with on-column sample stacking
    • Fu S, Chu SG, Qin ZF, Xu XB. Determination of cathepsin D activity in MCF-7 cells by capillary zone electrophoresis with on-column sample stacking. Chromatographia. 2003;58:73-78.
    • (2003) Chromatographia , vol.58 , pp. 73-78
    • Fu, S.1    Chu, S.G.2    Qin, Z.F.3    Xu, X.B.4
  • 224
    • 0033200238 scopus 로고    scopus 로고
    • Preparation of a cathepsin D sensitive near-infrared fluorescence probe for imaging
    • Tung CH, Bredow S, Mahmood U, Weissleder R. Preparation of a cathepsin D sensitive near-infrared fluorescence probe for imaging. Bioconjugate Chem. 1999;10:892-896.
    • (1999) Bioconjugate Chem , vol.10 , pp. 892-896
    • Tung, C.H.1    Bredow, S.2    Mahmood, U.3    Weissleder, R.4
  • 225
    • 0017702291 scopus 로고
    • Flow cytometric measurement of peptidases with use of 5-nitrosalicylaldehyde and 4-methoxy-b-naphthylamine derivatives
    • Dolbeare FA, Smith RE. Flow cytometric measurement of peptidases with use of 5-nitrosalicylaldehyde and 4-methoxy-b-naphthylamine derivatives. Clin Chem. 1977;23:1485-1491.
    • (1977) Clin Chem , vol.23 , pp. 1485-1491
    • Dolbeare, F.A.1    Smith, R.E.2
  • 230
    • 0028181494 scopus 로고
    • Cathepsin D by western blotting and immunohistochemistry: Failure to confirm correlations with prognosis in node-negative breast cancer
    • Ravdin PM, Tandon AK, Allred DC. Cathepsin D by western blotting and immunohistochemistry: failure to confirm correlations with prognosis in node-negative breast cancer. J Clin Oncol. 1994;12:468-474.
    • (1994) J Clin Oncol , vol.12 , pp. 468-474
    • Ravdin, P.M.1    Tandon, A.K.2    Allred, D.C.3
  • 231
    • 0028115873 scopus 로고
    • Western blotting and enzymatic activity analysis of cathepsin D in breast tissue and sera of patients with breast cancer and benign breast disease and of normal controls
    • Schultz DC, Bazel S, Wright LM, Tucker S, Lange MK, Tachovsky T, Longo S, Alhadeff JA. Western blotting and enzymatic activity analysis of cathepsin D in breast tissue and sera of patients with breast cancer and benign breast disease and of normal controls. Canc Res. 1994;54:48-54.
    • (1994) Canc Res , vol.54 , pp. 48-54
    • Schultz, D.C.1    Bazel, S.2    Wright, L.M.3    Tucker, S.4    Lange, M.K.5    Tachovsky, T.6    Longo, S.7    Alhadeff, J.A.8
  • 233
    • 0021988418 scopus 로고
    • Immunocytochemical localization of cathepsin D in lysosomes of cortical collecting tubule cells of the rat kidney
    • Yokota S, Tsuji H, Kato K. Immunocytochemical localization of cathepsin D in lysosomes of cortical collecting tubule cells of the rat kidney. J Histochem Cytochem. 1985;33:191-200.
    • (1985) J Histochem Cytochem , vol.33 , pp. 191-200
    • Yokota, S.1    Tsuji, H.2    Kato, K.3
  • 234
    • 0019497034 scopus 로고
    • Immunofluorescent localization of cathepsin B and D in human fibroblasts
    • Mort JS, Poole AR, Decker RS. Immunofluorescent localization of cathepsin B and D in human fibroblasts. J Histochem Cytochem. 1981;29:649-657.
    • (1981) J Histochem Cytochem , vol.29 , pp. 649-657
    • Mort, J.S.1    Poole, A.R.2    Decker, R.S.3
  • 235
    • 0020358964 scopus 로고
    • Electron microscopic visualization of cathepsin D using mercury-labeled pepstatin as an enzyme inhibitor
    • Yamato S, Hirabayashi Y, Sugihara H, Uematsu H. Electron microscopic visualization of cathepsin D using mercury-labeled pepstatin as an enzyme inhibitor. J Histochem Cytochem. 1982;30:1228-1234.
    • (1982) J Histochem Cytochem , vol.30 , pp. 1228-1234
    • Yamato, S.1    Hirabayashi, Y.2    Sugihara, H.3    Uematsu, H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.