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Volumn 113, Issue 2, 2012, Pages 233-247

Prolidase function in proline metabolism and its medical and biotechnological applications

Author keywords

Biotechnology; Degradation; Diagnosis; Enzymes; Peptides

Indexed keywords

BIOCHEMISTRY; BIOTECHNOLOGY; CELLS; CYTOLOGY; DIAGNOSIS; ENZYMES; HYDROXYPROLINE; MAMMALS; METABOLISM;

EID: 84864003886     PISSN: 13645072     EISSN: 13652672     Source Type: Journal    
DOI: 10.1111/j.1365-2672.2012.05310.x     Document Type: Review
Times cited : (79)

References (87)
  • 1
    • 0034072118 scopus 로고    scopus 로고
    • Plasma prolidase may be an index of liver fibrosis in the rat
    • Abraham, P., Wilfred, G. and Ramakrishna, B. (2000) Plasma prolidase may be an index of liver fibrosis in the rat. Clin Chim Acta295, 199-202.
    • (2000) Clin Chim Acta , vol.295 , pp. 199-202
    • Abraham, P.1    Wilfred, G.2    Ramakrishna, B.3
  • 2
    • 84962427422 scopus 로고    scopus 로고
    • Can human prolidase enzyme use different metals for full catalytic activity?
    • Alberto, M.E., Leopoldini, M. and Russo, N. (2011) Can human prolidase enzyme use different metals for full catalytic activity?Inorg Chem50, 3394-3403.
    • (2011) Inorg Chem , vol.50 , pp. 3394-3403
    • Alberto, M.E.1    Leopoldini, M.2    Russo, N.3
  • 3
    • 33846298900 scopus 로고    scopus 로고
    • Increased oxidative stress and its relation with collagen metabolism in knee osteoarthritis
    • Altindag, O., Erel, O., Aksoy, N., Selek, S., Celik, H. and Karaoglanoglu, M. (2007) Increased oxidative stress and its relation with collagen metabolism in knee osteoarthritis. Rheumatol Int27, 339-344.
    • (2007) Rheumatol Int , vol.27 , pp. 339-344
    • Altindag, O.1    Erel, O.2    Aksoy, N.3    Selek, S.4    Celik, H.5    Karaoglanoglu, M.6
  • 5
    • 73449125189 scopus 로고    scopus 로고
    • Serum prolidase activity and oxidative status in patients with stage I endometrial cancer
    • Arioz, D.T., Camuzcuoglu, H., Toy, H., Kurt, S., Celik, H. and Aksoy, N. (2009) Serum prolidase activity and oxidative status in patients with stage I endometrial cancer. Int J Gynecol Cancer19, 1244-1247.
    • (2009) Int J Gynecol Cancer , vol.19 , pp. 1244-1247
    • Arioz, D.T.1    Camuzcuoglu, H.2    Toy, H.3    Kurt, S.4    Celik, H.5    Aksoy, N.6
  • 8
    • 63149180910 scopus 로고    scopus 로고
    • Serum prolidase activity and oxidative status in patients with bronchial asthma
    • Cakmak, A., Zeyrek, D., Atas, A., Celik, H., Aksoy, N. and Erel, O. (2009) Serum prolidase activity and oxidative status in patients with bronchial asthma. J Clin Lab Anal23, 132-138.
    • (2009) J Clin Lab Anal , vol.23 , pp. 132-138
    • Cakmak, A.1    Zeyrek, D.2    Atas, A.3    Celik, H.4    Aksoy, N.5    Erel, O.6
  • 9
    • 75749126542 scopus 로고    scopus 로고
    • Prolidase activity and oxidative status in patients with thalassemia major
    • Cakmak, A., Soker, M., Koc, A. and Aksoy, N. (2010) Prolidase activity and oxidative status in patients with thalassemia major. J Clin Lab Anal24, 6-11.
    • (2010) J Clin Lab Anal , vol.24 , pp. 6-11
    • Cakmak, A.1    Soker, M.2    Koc, A.3    Aksoy, N.4
  • 10
    • 33745917058 scopus 로고    scopus 로고
    • Enhanced prolidase activity and decreased collagen content in breast cancer tissue
    • Cechowska-Pasko, M., Palka, J. and Wojtukiewicz, M.Z. (2006) Enhanced prolidase activity and decreased collagen content in breast cancer tissue. Int J Exp Pathol87, 289-296.
    • (2006) Int J Exp Pathol , vol.87 , pp. 289-296
    • Cechowska-Pasko, M.1    Palka, J.2    Wojtukiewicz, M.Z.3
  • 12
    • 0027292250 scopus 로고
    • Purification and properties of a highly active organophosphorus acid anhydrolase from Alteromonas undina
    • Cheng, T.C., Harvey, S.P. and Stroup, A.N. (1993) Purification and properties of a highly active organophosphorus acid anhydrolase from Alteromonas undina. Appl Environ Microbiol59, 3138-3140.
    • (1993) Appl Environ Microbiol , vol.59 , pp. 3138-3140
    • Cheng, T.C.1    Harvey, S.P.2    Stroup, A.N.3
  • 13
    • 4344597151 scopus 로고    scopus 로고
    • Acetylsalicylic acid as a potential regulator of prolidase-convertible pro-drugs in control and neoplastic cells
    • Chrzanowski, K., Bielawska, A., Bielawski, K., Palka, J. and Wolczynski, S. (2004) Acetylsalicylic acid as a potential regulator of prolidase-convertible pro-drugs in control and neoplastic cells. Farmaco59, 679-684.
    • (2004) Farmaco , vol.59 , pp. 679-684
    • Chrzanowski, K.1    Bielawska, A.2    Bielawski, K.3    Palka, J.4    Wolczynski, S.5
  • 14
    • 34547501895 scopus 로고    scopus 로고
    • Chitosan glutamate nanoparticles for protein delivery: development and effect on prolidase stability
    • Colonna, C., Conti, B., Perugini, P., Pavanetto, F., Modena, T., Dorati, R. and Genta, I. (2007) Chitosan glutamate nanoparticles for protein delivery: development and effect on prolidase stability. J Microencapsul24, 553-564.
    • (2007) J Microencapsul , vol.24 , pp. 553-564
    • Colonna, C.1    Conti, B.2    Perugini, P.3    Pavanetto, F.4    Modena, T.5    Dorati, R.6    Genta, I.7
  • 16
    • 44449150161 scopus 로고    scopus 로고
    • Site-directed PEGylation as successful approach to improve the enzyme replacement in the case of prolidase
    • Colonna, C., Conti, B., Perugini, P., Pavanetto, F., Modena, T., Dorati, R., Iadarola, P. and Genta, I. (2008b) Site-directed PEGylation as successful approach to improve the enzyme replacement in the case of prolidase. Int J Pharm358, 230-237.
    • (2008) Int J Pharm , vol.358 , pp. 230-237
    • Colonna, C.1    Conti, B.2    Perugini, P.3    Pavanetto, F.4    Modena, T.5    Dorati, R.6    Iadarola, P.7    Genta, I.8
  • 17
    • 0036095439 scopus 로고    scopus 로고
    • Accelerating cheese proteolysis by enriching Lactococcus lactis proteolytic system with lactobacilli peptidases
    • Courtin, P., Nardi, M., Wegmann, U., Joutsjoki, V., Ogier, J.C., Gripon, J.C., Palva, A., Henrich, B. et al. (2002) Accelerating cheese proteolysis by enriching Lactococcus lactis proteolytic system with lactobacilli peptidases. Int Dairy J12, 447-454.
    • (2002) Int Dairy J , vol.12 , pp. 447-454
    • Courtin, P.1    Nardi, M.2    Wegmann, U.3    Joutsjoki, V.4    Ogier, J.C.5    Gripon, J.C.6    Palva, A.7    Henrich, B.8
  • 19
    • 0026073674 scopus 로고
    • Purification and properties of an organophosphorus acid anhydrase from a halophilic bacterial isolate
    • DeFrank, J.J. and Cheng, T.C. (1991) Purification and properties of an organophosphorus acid anhydrase from a halophilic bacterial isolate. J Bacteriol173, 1938-1943.
    • (1991) J Bacteriol , vol.173 , pp. 1938-1943
    • DeFrank, J.J.1    Cheng, T.C.2
  • 20
    • 34548187261 scopus 로고    scopus 로고
    • Serum prolidase activity in patients with hypertension and its relation with left ventricular hypertrophy
    • Demirbag, R., Yildiz, A., Gur, M., Yilmaz, R., Elci, K. and Aksoy, N. (2007) Serum prolidase activity in patients with hypertension and its relation with left ventricular hypertrophy. Clin Biochem40, 1020-1025.
    • (2007) Clin Biochem , vol.40 , pp. 1020-1025
    • Demirbag, R.1    Yildiz, A.2    Gur, M.3    Yilmaz, R.4    Elci, K.5    Aksoy, N.6
  • 21
    • 27544463117 scopus 로고    scopus 로고
    • Characterization of the dinuclear metal center of Pyrococcus furiosus prolidase by analysis of targeted mutants
    • Du, X., Tove, S., Kast-Hutcheson, K. and Grunden, A.M. (2005) Characterization of the dinuclear metal center of Pyrococcus furiosus prolidase by analysis of targeted mutants. FEBS Lett579, 6140-6146.
    • (2005) FEBS Lett , vol.579 , pp. 6140-6146
    • Du, X.1    Tove, S.2    Kast-Hutcheson, K.3    Grunden, A.M.4
  • 22
    • 33645805481 scopus 로고    scopus 로고
    • Elevated prolidase activity in keloids: correlation with type I collagen turnover
    • Duong, H.S., Zhang, Q.Z., Le, A.D., Kelly, A.P., Kamdar, R. and Messadi, D.V. (2006) Elevated prolidase activity in keloids: correlation with type I collagen turnover. Br J Dermatol154, 820-828.
    • (2006) Br J Dermatol , vol.154 , pp. 820-828
    • Duong, H.S.1    Zhang, Q.Z.2    Le, A.D.3    Kelly, A.P.4    Kamdar, R.5    Messadi, D.V.6
  • 24
    • 0343488762 scopus 로고    scopus 로고
    • Purification and characterization of a prolidase from Lactobacillus casei subsp. casei IFPL 731
    • Fernandez-Espla, M.D., Martin-Hernandez, M.C. and Fox, P.F. (1997) Purification and characterization of a prolidase from Lactobacillus casei subsp. casei IFPL 731. Appl Environ Microbiol63, 314-316.
    • (1997) Appl Environ Microbiol , vol.63 , pp. 314-316
    • Fernandez-Espla, M.D.1    Martin-Hernandez, M.C.2    Fox, P.F.3
  • 25
    • 78751505102 scopus 로고    scopus 로고
    • Prolidase activity dysregulation and its correlation with oxidative-antioxidative status in chronic obstructive pulmonary disease
    • Gencer, M., Aksoy, N., Dagli, E.C., Uzer, E., Aksoy, S., Selek, S., Celik, H. and Cakir, H. (2011) Prolidase activity dysregulation and its correlation with oxidative-antioxidative status in chronic obstructive pulmonary disease. J Clin Lab Anal25, 8-13.
    • (2011) J Clin Lab Anal , vol.25 , pp. 8-13
    • Gencer, M.1    Aksoy, N.2    Dagli, E.C.3    Uzer, E.4    Aksoy, S.5    Selek, S.6    Celik, H.7    Cakir, H.8
  • 27
    • 0031705698 scopus 로고    scopus 로고
    • Characterization of native and recombinant forms of an unusual cobalt-dependent proline dipeptidase (prolidase) from the hyperthermophilic archaeon Pyrococcus furiosus
    • Ghosh, M., Grunden, A.M., Dunn, D.M., Weiss, R. and Adams, M.W. (1998) Characterization of native and recombinant forms of an unusual cobalt-dependent proline dipeptidase (prolidase) from the hyperthermophilic archaeon Pyrococcus furiosus. J Bacteriol180, 4781-4789.
    • (1998) J Bacteriol , vol.180 , pp. 4781-4789
    • Ghosh, M.1    Grunden, A.M.2    Dunn, D.M.3    Weiss, R.4    Adams, M.W.5
  • 28
    • 0030200482 scopus 로고    scopus 로고
    • Bacterial aminopeptidases: properties and functions
    • Gonzales, T. and Robert-Baudouy, J. (1996) Bacterial aminopeptidases: properties and functions. FEMS Microbiol Rev18, 319-344.
    • (1996) FEMS Microbiol Rev , vol.18 , pp. 319-344
    • Gonzales, T.1    Robert-Baudouy, J.2
  • 30
    • 0036236169 scopus 로고    scopus 로고
    • Cloning of a prolidase gene from Aspergillus nidulans and characterisation of its product
    • Jalving, R., Bron, P., Kester, H.C., Visser, J. and Schaap, P.J. (2002) Cloning of a prolidase gene from Aspergillus nidulans and characterisation of its product. Mol Genet Genomics267, 218-222.
    • (2002) Mol Genet Genomics , vol.267 , pp. 218-222
    • Jalving, R.1    Bron, P.2    Kester, H.C.3    Visser, J.4    Schaap, P.J.5
  • 31
    • 0035937593 scopus 로고    scopus 로고
    • Polysaccharide colloidal particles as delivery systems for macromolecules
    • Janes, K.A., Calvo, P. and Alonso, M.J. (2001) Polysaccharide colloidal particles as delivery systems for macromolecules. Adv Drug Deliv Rev47, 83-97.
    • (2001) Adv Drug Deliv Rev , vol.47 , pp. 83-97
    • Janes, K.A.1    Calvo, P.2    Alonso, M.J.3
  • 32
    • 84855568394 scopus 로고    scopus 로고
    • Crystal structural and functional analysis of the putative dipeptidase from Pyrococcus horikoshii OT3
    • Jeyakanthan, J., Takada, K., Sawano, M., Ogasahara, K., Mizutani, H., Yokoyama, S. and Yutani, K. (2009) Crystal structural and functional analysis of the putative dipeptidase from Pyrococcus horikoshii OT3. J Biophys2009, doi: .
    • (2009) J Biophys , vol.2009
    • Jeyakanthan, J.1    Takada, K.2    Sawano, M.3    Ogasahara, K.4    Mizutani, H.5    Yokoyama, S.6    Yutani, K.7
  • 33
    • 33646759204 scopus 로고    scopus 로고
    • The effects of different treatments on prolidase and antioxidant enzyme activities in patients with bronchial asthma
    • Kaleli, S., Akkaya, A., Akdogan, M. and Gultekin, F. (2006) The effects of different treatments on prolidase and antioxidant enzyme activities in patients with bronchial asthma. Environ Toxicol Pharmacol22, 35-39.
    • (2006) Environ Toxicol Pharmacol , vol.22 , pp. 35-39
    • Kaleli, S.1    Akkaya, A.2    Akdogan, M.3    Gultekin, F.4
  • 34
    • 0034519945 scopus 로고    scopus 로고
    • Collagen metabolism disturbances are accompanied by an increase in prolidase activity in lung carcinoma planoepitheliale
    • Karna, E., Surazynski, A. and Palka, J. (2000) Collagen metabolism disturbances are accompanied by an increase in prolidase activity in lung carcinoma planoepitheliale. Int J Exp Pathol81, 341-347.
    • (2000) Int J Exp Pathol , vol.81 , pp. 341-347
    • Karna, E.1    Surazynski, A.2    Palka, J.3
  • 35
    • 85027935482 scopus 로고    scopus 로고
    • Thrombin-dependent modulation of beta1-integrin-mediated signaling up-regulates prolidase and HIF-1alpha through p-FAK in colorectal cancer cells
    • Karna, E., Szoka, L. and Palka, J. (2012) Thrombin-dependent modulation of beta1-integrin-mediated signaling up-regulates prolidase and HIF-1alpha through p-FAK in colorectal cancer cells. Mol Cell Biochem361, 235-241.
    • (2012) Mol Cell Biochem , vol.361 , pp. 235-241
    • Karna, E.1    Szoka, L.2    Palka, J.3
  • 37
    • 34250881554 scopus 로고    scopus 로고
    • Prolidase isoenzymes in the rat: their organ distribution, developmental change and specific inhibitors
    • Liu, G., Nakayama, K., Awata, S., Tang, S., Kitaoka, N., Manabe, M. and Kodama, H. (2007) Prolidase isoenzymes in the rat: their organ distribution, developmental change and specific inhibitors. Pediatr Res62, 54-59.
    • (2007) Pediatr Res , vol.62 , pp. 54-59
    • Liu, G.1    Nakayama, K.2    Awata, S.3    Tang, S.4    Kitaoka, N.5    Manabe, M.6    Kodama, H.7
  • 38
    • 0036882401 scopus 로고    scopus 로고
    • Metalloaminopeptidases: common functional themes in disparate structural surroundings
    • Lowther, W.T. and Matthews, B.W. (2002) Metalloaminopeptidases: common functional themes in disparate structural surroundings. Chem Rev102, 4581-4608.
    • (2002) Chem Rev , vol.102 , pp. 4581-4608
    • Lowther, W.T.1    Matthews, B.W.2
  • 41
    • 20444394385 scopus 로고    scopus 로고
    • N-benzyloxycarbonyl-L-proline: an in vitro and in vivo inhibitor of prolidase
    • Lupi, A., Rossi, A., Vaghi, P., Gallanti, A., Cetta, G. and Forlino, A. (2005) N-benzyloxycarbonyl-L-proline: an in vitro and in vivo inhibitor of prolidase. Biochim Biophys Acta1744, 157-163.
    • (2005) Biochim Biophys Acta , vol.1744 , pp. 157-163
    • Lupi, A.1    Rossi, A.2    Vaghi, P.3    Gallanti, A.4    Cetta, G.5    Forlino, A.6
  • 42
    • 33751104177 scopus 로고    scopus 로고
    • Human recombinant prolidase from eukaryotic and prokaryotic sources. Expression, purification, characterization and long-term stability studies
    • Lupi, A., Della Torre, S., Campari, E., Tenni, R., Cetta, G., Rossi, A. and Forlino, A. (2006) Human recombinant prolidase from eukaryotic and prokaryotic sources. Expression, purification, characterization and long-term stability studies. FEBS J273, 5466-5478.
    • (2006) FEBS J , vol.273 , pp. 5466-5478
    • Lupi, A.1    Della Torre, S.2    Campari, E.3    Tenni, R.4    Cetta, G.5    Rossi, A.6    Forlino, A.7
  • 43
    • 53849106854 scopus 로고    scopus 로고
    • Human prolidase and prolidase deficiency: an overview on the characterization of the enzyme involved in proline recycling and on the effects of its mutations
    • Lupi, A., Tenni, R., Rossi, A., Cetta, G. and Forlino, A. (2008) Human prolidase and prolidase deficiency: an overview on the characterization of the enzyme involved in proline recycling and on the effects of its mutations. Amino Acids35, 739-752.
    • (2008) Amino Acids , vol.35 , pp. 739-752
    • Lupi, A.1    Tenni, R.2    Rossi, A.3    Cetta, G.4    Forlino, A.5
  • 45
    • 0020535118 scopus 로고
    • Degradation of proline peptides in peptidase-deficient strains of Salmonella typhimurium
    • Miller, C.G. and Green, L. (1983) Degradation of proline peptides in peptidase-deficient strains of Salmonella typhimurium. J Bacteriol153, 350-356.
    • (1983) J Bacteriol , vol.153 , pp. 350-356
    • Miller, C.G.1    Green, L.2
  • 47
    • 14644445992 scopus 로고    scopus 로고
    • Prolidase, a potential enzyme target for melanoma: design of proline-containing dipeptide-like prodrugs
    • Mittal, S., Song, X., Vig, B.S., Landowski, C.P., Kim, I., Hilfinger, J.M. and Amidon, G.L. (2005) Prolidase, a potential enzyme target for melanoma: design of proline-containing dipeptide-like prodrugs. Mol Pharm2, 37-46.
    • (2005) Mol Pharm , vol.2 , pp. 37-46
    • Mittal, S.1    Song, X.2    Vig, B.S.3    Landowski, C.P.4    Kim, I.5    Hilfinger, J.M.6    Amidon, G.L.7
  • 48
    • 34249874620 scopus 로고    scopus 로고
    • Proline prodrug of melphalan targeted to prolidase, a prodrug activating enzyme overexpressed in melanoma
    • Mittal, S., Song, X., Vig, B.S. and Amidon, G.L. (2007) Proline prodrug of melphalan targeted to prolidase, a prodrug activating enzyme overexpressed in melanoma. Pharm Res24, 1290-1298.
    • (2007) Pharm Res , vol.24 , pp. 1290-1298
    • Mittal, S.1    Song, X.2    Vig, B.S.3    Amidon, G.L.4
  • 49
    • 0033060731 scopus 로고    scopus 로고
    • Characterization of a prolidase from Lactobacillus delbrueckii subsp. bulgaricus CNRZ 397 with an unusual regulation of biosynthesis
    • Morel, F., Frot-Coutaz, J., Aubel, D., Portalier, R. and Atlan, D. (1999) Characterization of a prolidase from Lactobacillus delbrueckii subsp. bulgaricus CNRZ 397 with an unusual regulation of biosynthesis. Microbiology145(Pt 2), 137-146.
    • (1999) Microbiology , vol.145 , Issue.PART 2 , pp. 137-146
    • Morel, F.1    Frot-Coutaz, J.2    Aubel, D.3    Portalier, R.4    Atlan, D.5
  • 50
    • 0021341954 scopus 로고
    • Plasma prolidase activity: a possible index of collagen catabolism in chronic liver disease
    • Myara, I., Myara, A., Mangeot, M., Fabre, M., Charpentier, C. and Lemonnier, A. (1984) Plasma prolidase activity: a possible index of collagen catabolism in chronic liver disease. Clin Chem30, 211-215.
    • (1984) Clin Chem , vol.30 , pp. 211-215
    • Myara, I.1    Myara, A.2    Mangeot, M.3    Fabre, M.4    Charpentier, C.5    Lemonnier, A.6
  • 51
    • 0035011379 scopus 로고    scopus 로고
    • A study of prolidase in mothers, their newborn babies and in non-pregnant controls
    • Namiduru, E.S., Ozdemir, Y., Kutlar, I. and Ersoy, U. (2001) A study of prolidase in mothers, their newborn babies and in non-pregnant controls. Arch Gynecol Obstet265, 73-75.
    • (2001) Arch Gynecol Obstet , vol.265 , pp. 73-75
    • Namiduru, E.S.1    Ozdemir, Y.2    Kutlar, I.3    Ersoy, U.4
  • 52
    • 0027440247 scopus 로고
    • Activation by nitric oxide of an oxidative-stress response that defends Escherichia coli against activated macrophages
    • Nunoshiba, T., Derojas-Walker, T., Wishnok, J.S., Tannenbaum, S.R. and Demple, B. (1993) Activation by nitric oxide of an oxidative-stress response that defends Escherichia coli against activated macrophages. Proc Natl Acad Sci USA90, 9993-9997.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 9993-9997
    • Nunoshiba, T.1    Derojas-Walker, T.2    Wishnok, J.S.3    Tannenbaum, S.R.4    Demple, B.5
  • 53
    • 0016787671 scopus 로고
    • Purification and characterization of an aminoacyl proline hydrolase from guinea-pig intestinal mucosa
    • O'Cuinn, G. and Fottrell, P.F. (1975) Purification and characterization of an aminoacyl proline hydrolase from guinea-pig intestinal mucosa. Biochim Biophys Acta391, 388-395.
    • (1975) Biochim Biophys Acta , vol.391 , pp. 388-395
    • O'Cuinn, G.1    Fottrell, P.F.2
  • 54
    • 0025058744 scopus 로고
    • Characterization of prolidase I and II from erythrocytes of a control, a patient with prolidase deficiency and her mother
    • Ohhashi, T., Ohno, T., Arata, J., Sugahara, K. and Kodama, H. (1990) Characterization of prolidase I and II from erythrocytes of a control, a patient with prolidase deficiency and her mother. Clin Chim Acta187, 1-9.
    • (1990) Clin Chim Acta , vol.187 , pp. 1-9
    • Ohhashi, T.1    Ohno, T.2    Arata, J.3    Sugahara, K.4    Kodama, H.5
  • 57
    • 19944428610 scopus 로고    scopus 로고
    • Intracellular delivery of liposome-encapsulated prolidase in cultured fibroblasts from prolidase-deficient patients
    • Perugini, P., Hassan, K., Genta, I., Modena, T., Pavanetto, F., Cetta, G., Zanone, C., Iadarola, P. et al. (2005) Intracellular delivery of liposome-encapsulated prolidase in cultured fibroblasts from prolidase-deficient patients. J Control Release102, 181-190.
    • (2005) J Control Release , vol.102 , pp. 181-190
    • Perugini, P.1    Hassan, K.2    Genta, I.3    Modena, T.4    Pavanetto, F.5    Cetta, G.6    Zanone, C.7    Iadarola, P.8
  • 58
    • 0033859548 scopus 로고    scopus 로고
    • Long circulating liposomes encapsulating organophosphorus acid anhydrolase in diisopropyl fluorophosphate antagonism
    • Petrikovics, I., Cheng, T.C., Papahadjopoulos, D., Hong, K., Yin, R., DeFrank, J.J., Jaing, J., Song, Z.H. et al. (2000a) Long circulating liposomes encapsulating organophosphorus acid anhydrolase in diisopropyl fluorophosphate antagonism. Toxicol Sci57, 16-21.
    • (2000) Toxicol Sci , vol.57 , pp. 16-21
    • Petrikovics, I.1    Cheng, T.C.2    Papahadjopoulos, D.3    Hong, K.4    Yin, R.5    DeFrank, J.J.6    Jaing, J.7    Song, Z.H.8
  • 60
    • 53849096017 scopus 로고    scopus 로고
    • The metabolism of proline, a stress substrate, modulates carcinogenic pathways
    • Phang, J.M., Donald, S.P., Pandhare, J. and Liu, Y. (2008) The metabolism of proline, a stress substrate, modulates carcinogenic pathways. Amino Acids35, 681-690.
    • (2008) Amino Acids , vol.35 , pp. 681-690
    • Phang, J.M.1    Donald, S.P.2    Pandhare, J.3    Liu, Y.4
  • 61
    • 77955619986 scopus 로고    scopus 로고
    • Proline metabolism and microenvironmental stress
    • Phang, J.M., Liu, W. and Zabirnyk, O. (2010) Proline metabolism and microenvironmental stress. Annu Rev Nutr30, 441-463.
    • (2010) Annu Rev Nutr , vol.30 , pp. 441-463
    • Phang, J.M.1    Liu, W.2    Zabirnyk, O.3
  • 63
    • 79851513447 scopus 로고    scopus 로고
    • Prolidase activity and its diagnostic performance in bipolar disorder
    • Selek, S., Altindag, A., Saracoglu, G., Celik, H. and Aksoy, N. (2011) Prolidase activity and its diagnostic performance in bipolar disorder. J Affect Disord129, 84-86.
    • (2011) J Affect Disord , vol.129 , pp. 84-86
    • Selek, S.1    Altindag, A.2    Saracoglu, G.3    Celik, H.4    Aksoy, N.5
  • 66
    • 58649088219 scopus 로고    scopus 로고
    • Organophosphorus-degrading bacteria: ecology and industrial applications
    • Singh, B.K. (2009) Organophosphorus-degrading bacteria: ecology and industrial applications. Nat Rev Microbiol7, 156-164.
    • (2009) Nat Rev Microbiol , vol.7 , pp. 156-164
    • Singh, B.K.1
  • 68
    • 28144453502 scopus 로고    scopus 로고
    • Nitric oxide regulates prolidase activity by serine/threonine phosphorylation
    • Surazynski, A., Liu, Y., Miltyk, W. and Phang, J.M. (2005) Nitric oxide regulates prolidase activity by serine/threonine phosphorylation. J Cell Biochem96, 1086-1094.
    • (2005) J Cell Biochem , vol.96 , pp. 1086-1094
    • Surazynski, A.1    Liu, Y.2    Miltyk, W.3    Phang, J.M.4
  • 70
    • 53849108847 scopus 로고    scopus 로고
    • Prolidase-dependent regulation of collagen biosynthesis
    • Surazynski, A., Miltyk, W., Palka, J. and Phang, J.M. (2008b) Prolidase-dependent regulation of collagen biosynthesis. Amino Acids35, 731-738.
    • (2008) Amino Acids , vol.35 , pp. 731-738
    • Surazynski, A.1    Miltyk, W.2    Palka, J.3    Phang, J.M.4
  • 71
    • 0025295191 scopus 로고
    • Structural organization of the gene for human prolidase (peptidase D) and demonstration of a partial gene deletion in a patient with prolidase deficiency
    • Tanoue, A., Endo, F. and Matsuda, I. (1990) Structural organization of the gene for human prolidase (peptidase D) and demonstration of a partial gene deletion in a patient with prolidase deficiency. J Biol Chem265, 11306-11311.
    • (1990) J Biol Chem , vol.265 , pp. 11306-11311
    • Tanoue, A.1    Endo, F.2    Matsuda, I.3
  • 72
    • 78651067662 scopus 로고    scopus 로고
    • Hydrolysis of organophosphorus compounds by microbial enzymes
    • Theriot, C.M. and Grunden, A.M. (2010) Hydrolysis of organophosphorus compounds by microbial enzymes. Appl Microbiol Biotechnol89, 35-43.
    • (2010) Appl Microbiol Biotechnol , vol.89 , pp. 35-43
    • Theriot, C.M.1    Grunden, A.M.2
  • 73
    • 78651067662 scopus 로고    scopus 로고
    • Hydrolysis of organophosphorus compounds by microbial enzymes
    • Theriot, C.M. and Grunden, A.M. (2011) Hydrolysis of organophosphorus compounds by microbial enzymes. Appl Microbiol Biotechnol89, 35-43.
    • (2011) Appl Microbiol Biotechnol , vol.89 , pp. 35-43
    • Theriot, C.M.1    Grunden, A.M.2
  • 74
    • 65449160143 scopus 로고    scopus 로고
    • Biotechnological applications of recombinant microbial prolidases
    • Theriot, C.M., Tove, S.R. and Grunden, A.M. (2009) Biotechnological applications of recombinant microbial prolidases. Adv Appl Microbiol68, 99-132.
    • (2009) Adv Appl Microbiol , vol.68 , pp. 99-132
    • Theriot, C.M.1    Tove, S.R.2    Grunden, A.M.3
  • 75
    • 77955521279 scopus 로고    scopus 로고
    • Improving the catalytic activity of hyperthermophilic Pyrococcus prolidases for detoxification of organophosphorus nerve agents over a broad range of temperatures
    • Theriot, C.M., Du, X., Tove, S.R. and Grunden, A.M. (2010a) Improving the catalytic activity of hyperthermophilic Pyrococcus prolidases for detoxification of organophosphorus nerve agents over a broad range of temperatures. Appl Microbiol Biotechnol87, 1715-1726.
    • (2010) Appl Microbiol Biotechnol , vol.87 , pp. 1715-1726
    • Theriot, C.M.1    Du, X.2    Tove, S.R.3    Grunden, A.M.4
  • 76
    • 77149166621 scopus 로고    scopus 로고
    • Characterization of two proline dipeptidases (prolidases) from the hyperthermophilic archaeon Pyrococcus horikoshii
    • Theriot, C.M., Tove, S.R. and Grunden, A.M. (2010b) Characterization of two proline dipeptidases (prolidases) from the hyperthermophilic archaeon Pyrococcus horikoshii. Appl Microbiol Biotechnol86, 177-188.
    • (2010) Appl Microbiol Biotechnol , vol.86 , pp. 177-188
    • Theriot, C.M.1    Tove, S.R.2    Grunden, A.M.3
  • 77
    • 84855606895 scopus 로고    scopus 로고
    • Improving the catalytic activity of hyperthermophilic Pyrococcus horikoshii prolidase for detoxification of organophosphorus nerve agents over a broad range of temperatures
    • Theriot, C.M., Semcer, R.L., Shah, S.S. and Grunden, A.M. (2011) Improving the catalytic activity of hyperthermophilic Pyrococcus horikoshii prolidase for detoxification of organophosphorus nerve agents over a broad range of temperatures. Archaea2011, 565127.
    • (2011) Archaea , vol.2011 , pp. 565127
    • Theriot, C.M.1    Semcer, R.L.2    Shah, S.S.3    Grunden, A.M.4
  • 78
    • 70849104207 scopus 로고    scopus 로고
    • Decreased serum prolidase activity and increased oxidative stress in early pregnancy loss
    • Toy, H., Camuzcuoglu, H., Camuzcuoglu, A., Celik, H. and Aksoy, N. (2010) Decreased serum prolidase activity and increased oxidative stress in early pregnancy loss. Gynecol Obstet Invest69, 122-127.
    • (2010) Gynecol Obstet Invest , vol.69 , pp. 122-127
    • Toy, H.1    Camuzcuoglu, H.2    Camuzcuoglu, A.3    Celik, H.4    Aksoy, N.5
  • 79
    • 69249224445 scopus 로고    scopus 로고
    • Characterization of prolidase I and II purified from normal human erythrocytes: comparison with prolidase in erythrocytes from a patient with prolidase deficiency
    • Uramatsu, S., Liu, G., Yang, Q., Uramatsu, M., Chi, H., Lu, J., Yamashita, K. and Kodama, H. (2009) Characterization of prolidase I and II purified from normal human erythrocytes: comparison with prolidase in erythrocytes from a patient with prolidase deficiency. Amino Acids37, 543-551.
    • (2009) Amino Acids , vol.37 , pp. 543-551
    • Uramatsu, S.1    Liu, G.2    Yang, Q.3    Uramatsu, M.4    Chi, H.5    Lu, J.6    Yamashita, K.7    Kodama, H.8
  • 80
    • 32244437411 scopus 로고    scopus 로고
    • The role of emerging techniques in the investigation of prolidase deficiency: from diagnosis to the development of a possible therapeutical approach
    • Viglio, S., Annovazzi, L., Conti, B., Genta, I., Perugini, P., Zanone, C., Casado, B., Cetta, G. et al. (2006) The role of emerging techniques in the investigation of prolidase deficiency: from diagnosis to the development of a possible therapeutical approach. J Chromatogr B Analyt Technol Biomed Life Sci832, 1-8.
    • (2006) J Chromatogr B Analyt Technol Biomed Life Sci , vol.832 , pp. 1-8
    • Viglio, S.1    Annovazzi, L.2    Conti, B.3    Genta, I.4    Perugini, P.5    Zanone, C.6    Casado, B.7    Cetta, G.8
  • 81
    • 79956108868 scopus 로고    scopus 로고
    • Comparison of prolidase enzyme activities of maternal serum and placental tissue in patients with early pregnancy failure
    • Vural, M., Toy, H., Camuzcuoglu, H. and Aksoy, N. (2011) Comparison of prolidase enzyme activities of maternal serum and placental tissue in patients with early pregnancy failure. Arch Gynecol Obstet283, 953-958.
    • (2011) Arch Gynecol Obstet , vol.283 , pp. 953-958
    • Vural, M.1    Toy, H.2    Camuzcuoglu, H.3    Aksoy, N.4
  • 82
    • 74949127023 scopus 로고    scopus 로고
    • Structural insights into the dual activities of the nerve agent degrading organophosphate anhydrolase/prolidase
    • Vyas, N.K., Nickitenko, A., Rastogi, V.K., Shah, S.S. and Quiocho, F.A. (2010) Structural insights into the dual activities of the nerve agent degrading organophosphate anhydrolase/prolidase. Biochemistry49, 547-559.
    • (2010) Biochemistry , vol.49 , pp. 547-559
    • Vyas, N.K.1    Nickitenko, A.2    Rastogi, V.K.3    Shah, S.S.4    Quiocho, F.A.5
  • 83
    • 0031616843 scopus 로고    scopus 로고
    • Purification and properties of soman-hydrolyzing enzyme from human liver
    • Wang, Q., Sun, M., Zhang, H. and Huang, C. (1998) Purification and properties of soman-hydrolyzing enzyme from human liver. J Biochem Mol Toxicol12, 213-217.
    • (1998) J Biochem Mol Toxicol , vol.12 , pp. 213-217
    • Wang, Q.1    Sun, M.2    Zhang, H.3    Huang, C.4
  • 84
    • 79954451437 scopus 로고    scopus 로고
    • Proline and hydroxyproline metabolism: implications for animal and human nutrition
    • Wu, G., Bazer, F.W., Burghardt, R.C., Johnson, G.A., Kim, S.W., Knabe, D.A., Li, P., Li, X. et al. (2011) Proline and hydroxyproline metabolism: implications for animal and human nutrition. Amino Acids40, 1053-1063.
    • (2011) Amino Acids , vol.40 , pp. 1053-1063
    • Wu, G.1    Bazer, F.W.2    Burghardt, R.C.3    Johnson, G.A.4    Kim, S.W.5    Knabe, D.A.6    Li, P.7    Li, X.8
  • 85
    • 37849015455 scopus 로고    scopus 로고
    • Characterization of recombinant prolidase from Lactococcus lactis- changes in substrate specificity by metal cations, and allosteric behavior of the peptidase
    • Yang, S.I. and Tanaka, T. (2008) Characterization of recombinant prolidase from Lactococcus lactis- changes in substrate specificity by metal cations, and allosteric behavior of the peptidase. FEBS J275, 271-280.
    • (2008) FEBS J , vol.275 , pp. 271-280
    • Yang, S.I.1    Tanaka, T.2
  • 86
    • 0021065999 scopus 로고
    • Prolidase from bovine intestine: purification and characterization
    • Yoshimoto, T., Matsubara, F., Kawano, E. and Tsuru, D. (1983) Prolidase from bovine intestine: purification and characterization. J Biochem94, 1889-1896.
    • (1983) J Biochem , vol.94 , pp. 1889-1896
    • Yoshimoto, T.1    Matsubara, F.2    Kawano, E.3    Tsuru, D.4
  • 87
    • 0002566165 scopus 로고
    • Prolidase deficiency: biochemical study of erythrocyte and skin fibroblast prolidase activity in Italian patients
    • Zanaboni, G., Dyne, K.M., Rossi, A., Monafo, V. and Cetta, G. (1994) Prolidase deficiency: biochemical study of erythrocyte and skin fibroblast prolidase activity in Italian patients. Haematologica79, 13-18.
    • (1994) Haematologica , vol.79 , pp. 13-18
    • Zanaboni, G.1    Dyne, K.M.2    Rossi, A.3    Monafo, V.4    Cetta, G.5


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