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Volumn 43, Issue 6, 2013, Pages 501-509

A digestive prolyl carboxypeptidase in Tenebrio molitor larvae

Author keywords

Digestive peptidase; Insect digestion; Prolyl carboxypeptidase; Stored product pest; Tenebrio molitor

Indexed keywords

CARBOXYPEPTIDASE; PROCOLLAGEN PROLINE 2 OXOGLUTARATE 4 DIOXYGENASE;

EID: 84876729046     PISSN: 09651748     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ibmb.2013.02.009     Document Type: Article
Times cited : (20)

References (60)
  • 3
    • 84864801579 scopus 로고    scopus 로고
    • The 3D structure and function of digestive cathepsin L-like proteinases of Tenebrio molitor larval midgut
    • Beton D., Guzzo C.R., Ribeiro A.F., Farah C.S., Terra W.R. The 3D structure and function of digestive cathepsin L-like proteinases of Tenebrio molitor larval midgut. Insect Biochem. Mol. Biol. 2012, 42:655-664.
    • (2012) Insect Biochem. Mol. Biol. , vol.42 , pp. 655-664
    • Beton, D.1    Guzzo, C.R.2    Ribeiro, A.F.3    Farah, C.S.4    Terra, W.R.5
  • 4
    • 0032822537 scopus 로고    scopus 로고
    • Specificity, anchoring, and subsites in the active center of a microvillar aminopeptidase purified from Tenebrio molitor (Coleoptera) midgut cells
    • Cristofoletti P.T., Terra W.R. Specificity, anchoring, and subsites in the active center of a microvillar aminopeptidase purified from Tenebrio molitor (Coleoptera) midgut cells. Insect Biochem. Mol. Biol. 1999, 29:807-819.
    • (1999) Insect Biochem. Mol. Biol. , vol.29 , pp. 807-819
    • Cristofoletti, P.T.1    Terra, W.R.2
  • 5
    • 0034660032 scopus 로고    scopus 로고
    • The role of amino acid residues in the active site of a midgut microvillar aminopeptidase from the beetle Tenebrio molitor
    • Cristofoletti P.T., Terra W.R. The role of amino acid residues in the active site of a midgut microvillar aminopeptidase from the beetle Tenebrio molitor. Biochim. Biophys. Acta 2000, 1479:185-195.
    • (2000) Biochim. Biophys. Acta , vol.1479 , pp. 185-195
    • Cristofoletti, P.T.1    Terra, W.R.2
  • 6
    • 23844481908 scopus 로고    scopus 로고
    • The cathepsin L-like proteinases from the midgut of Tenebrio molitor larvae: sequence, properties, immunocytochemical localization and function
    • Cristofoletti P.T., Ribeiro A.F., Terra W.R. The cathepsin L-like proteinases from the midgut of Tenebrio molitor larvae: sequence, properties, immunocytochemical localization and function. Insect Biochem. Mol. Biol. 2005, 35:883-901.
    • (2005) Insect Biochem. Mol. Biol. , vol.35 , pp. 883-901
    • Cristofoletti, P.T.1    Ribeiro, A.F.2    Terra, W.R.3
  • 8
    • 78651463641 scopus 로고    scopus 로고
    • New aspects of melanocortin signaling: a role for PRCP in α-MSH degradation
    • Diano S. New aspects of melanocortin signaling: a role for PRCP in α-MSH degradation. Front. Neuroendocrinol. 2011, 32:70-83.
    • (2011) Front. Neuroendocrinol. , vol.32 , pp. 70-83
    • Diano, S.1
  • 9
    • 78951493361 scopus 로고    scopus 로고
    • Prolylcarboxypeptidase regulates proliferation, autophagy, and resistance to 4-hydroxytamoxifen-induced cytotoxicity in estrogen receptor-positive breast cancer cells
    • Duan L., Motchoulski N., Danzer B., Davidovich I., Shariat-Madar Z., Levenson V.V. Prolylcarboxypeptidase regulates proliferation, autophagy, and resistance to 4-hydroxytamoxifen-induced cytotoxicity in estrogen receptor-positive breast cancer cells. J. Biol. Chem. 2011, 286:2864-2876.
    • (2011) J. Biol. Chem. , vol.286 , pp. 2864-2876
    • Duan, L.1    Motchoulski, N.2    Danzer, B.3    Davidovich, I.4    Shariat-Madar, Z.5    Levenson, V.V.6
  • 10
    • 34548643151 scopus 로고    scopus 로고
    • Digestive peptidases in Tenebrio molitor and possibility of use to treat celiac disease
    • Elpidina E.N., Goptar I.A. Digestive peptidases in Tenebrio molitor and possibility of use to treat celiac disease. Entomol. Res. 2007, 37:139-147.
    • (2007) Entomol. Res. , vol.37 , pp. 139-147
    • Elpidina, E.N.1    Goptar, I.A.2
  • 12
    • 50549163362 scopus 로고
    • The preparation and properties of two new chromogenic substrates of trypsin
    • Erlanger B.F., Kokowsky N., Cohen W. The preparation and properties of two new chromogenic substrates of trypsin. Arch. Biochem. Biophys. 1961, 95:271-278.
    • (1961) Arch. Biochem. Biophys. , vol.95 , pp. 271-278
    • Erlanger, B.F.1    Kokowsky, N.2    Cohen, W.3
  • 13
    • 0000779897 scopus 로고
    • Digestive enzymes associated with the glycocalyx, microvillar membranes and secretory vesicles from midgut cells of Tenebrio molitor larvae
    • Ferreira C., Bellinello G.L., Ribeiro A.F., Terra W.R. Digestive enzymes associated with the glycocalyx, microvillar membranes and secretory vesicles from midgut cells of Tenebrio molitor larvae. Insect Biochem. 1990, 20:839-847.
    • (1990) Insect Biochem. , vol.20 , pp. 839-847
    • Ferreira, C.1    Bellinello, G.L.2    Ribeiro, A.F.3    Terra, W.R.4
  • 14
    • 0000321512 scopus 로고
    • Tampone universale di Britton e Robinson a forza ionica constante
    • Frugoni J.A.C. Tampone universale di Britton e Robinson a forza ionica constante. Gazz. Chem. Ital. 1957, 87:403-407.
    • (1957) Gazz. Chem. Ital. , vol.87 , pp. 403-407
    • Frugoni, J.A.C.1
  • 18
    • 79953810491 scopus 로고    scopus 로고
    • PRCP: a key role to blood vessel homeostasis
    • Hagedorn M. PRCP: a key role to blood vessel homeostasis. Blood 2011, 117:3705-3706.
    • (2011) Blood , vol.117 , pp. 3705-3706
    • Hagedorn, M.1
  • 19
    • 84862528349 scopus 로고    scopus 로고
    • Deletion of prolyl carboxypeptidase attenuates the metabolic effects of diet-induced obesity
    • Jeong J.K., Szabo G., Raso G.M., Meli R., Diano S. Deletion of prolyl carboxypeptidase attenuates the metabolic effects of diet-induced obesity. Am. J. Physiol. Endocrinol. Metab. 2012, 302:E1502-E1510.
    • (2012) Am. J. Physiol. Endocrinol. Metab. , vol.302
    • Jeong, J.K.1    Szabo, G.2    Raso, G.M.3    Meli, R.4    Diano, S.5
  • 20
    • 0015924308 scopus 로고
    • Purification of lysosomal prolycarboxypeptidase angiotensinase C
    • Kakimoto T., Oshima G., Yeh H.S., Erdös E.G. Purification of lysosomal prolycarboxypeptidase angiotensinase C. Biochim. Biophys. Acta 1973, 302:178-182.
    • (1973) Biochim. Biophys. Acta , vol.302 , pp. 178-182
    • Kakimoto, T.1    Oshima, G.2    Yeh, H.S.3    Erdös, E.G.4
  • 21
    • 77954311687 scopus 로고    scopus 로고
    • The plasma bradykinin-forming pathways and its interrelationships with complement
    • Kaplan A.P., Ghebrehiwet B. The plasma bradykinin-forming pathways and its interrelationships with complement. Mol. Immunol. 2010, 47:2161-2169.
    • (2010) Mol. Immunol. , vol.47 , pp. 2161-2169
    • Kaplan, A.P.1    Ghebrehiwet, B.2
  • 22
    • 0019515695 scopus 로고
    • Prolylcarboxypeptidase (angiotensinase C) in human lung and cultured cells
    • Kumamoto K., Stewart T.A., Johnson A.R., Erdos E.G. Prolylcarboxypeptidase (angiotensinase C) in human lung and cultured cells. J. Clin. Invest. 1981, 67:210-215.
    • (1981) J. Clin. Invest. , vol.67 , pp. 210-215
    • Kumamoto, K.1    Stewart, T.A.2    Johnson, A.R.3    Erdos, E.G.4
  • 27
    • 0020198680 scopus 로고
    • Electrophoresis buffers for polyacrylamide gels at various pH
    • McLellan T. Electrophoresis buffers for polyacrylamide gels at various pH. Anal. Biochem. 1982, 126:94-99.
    • (1982) Anal. Biochem. , vol.126 , pp. 94-99
    • McLellan, T.1
  • 28
    • 61849136631 scopus 로고    scopus 로고
    • Upregulation of prolylcarboxypeptidase (PRCP) in lipopolysaccharide (LPS) treated endothelium promotes inflammation
    • Ngo M.L., Mahdi F., Kolte D., Shariat-Madar Z. Upregulation of prolylcarboxypeptidase (PRCP) in lipopolysaccharide (LPS) treated endothelium promotes inflammation. J. Inflamm. 2009, 6:3.
    • (2009) J. Inflamm. , vol.6 , pp. 3
    • Ngo, M.L.1    Mahdi, F.2    Kolte, D.3    Shariat-Madar, Z.4
  • 29
    • 0002511466 scopus 로고    scopus 로고
    • GeneDoc: analysis and visualization of genetic variation
    • Nicholas K.B., Nicholas H.B., Deerfield D.W. GeneDoc: analysis and visualization of genetic variation. Embnew News 1997, 4:14.
    • (1997) Embnew News , vol.4 , pp. 14
    • Nicholas, K.B.1    Nicholas, H.B.2    Deerfield, D.W.3
  • 30
    • 0018126802 scopus 로고
    • Purification and properties of prolylcarboxypeptidase (angiotensinase C) from human kidney
    • Odya C.E., Marinkovic D.V., Hammon K.J., Stewart T.A., Erdos E.G. Purification and properties of prolylcarboxypeptidase (angiotensinase C) from human kidney. J. Biol. Chem. 1978, 253:5927-5931.
    • (1978) J. Biol. Chem. , vol.253 , pp. 5927-5931
    • Odya, C.E.1    Marinkovic, D.V.2    Hammon, K.J.3    Stewart, T.A.4    Erdos, E.G.5
  • 31
    • 84864411085 scopus 로고    scopus 로고
    • Bacillus thuringiensis Cry3Aa protoxin intoxication of Tenebrio molitor induces widespread changes in the expression of serine peptidase transcripts
    • Oppert B., Martynov A.G., Elpidina E.N. Bacillus thuringiensis Cry3Aa protoxin intoxication of Tenebrio molitor induces widespread changes in the expression of serine peptidase transcripts. Comp. Biochem. Physiol. 2012, 7D:233-242.
    • (2012) Comp. Biochem. Physiol. , vol.7 D , pp. 233-242
    • Oppert, B.1    Martynov, A.G.2    Elpidina, E.N.3
  • 32
    • 84876738689 scopus 로고
    • Humana Press, Totowa, N.J., Walker, J.M., Series Editor
    • Peptide Synthesis Protocols Methods in Molecular Biology 1994, vol. 35:321. Humana Press, Totowa, N.J., Walker, J.M., Series Editor.
    • (1994) Methods in Molecular Biology , vol.35 , pp. 321
    • Peptide Synthesis Protocols1
  • 33
    • 80053345905 scopus 로고    scopus 로고
    • SignalP 4.0: discriminating signal peptides from transmembrane regions
    • Petersen T.N., Brunak S., von Heijne G., Nielsen H. SignalP 4.0: discriminating signal peptides from transmembrane regions. Nat. Methods 2011, 8:785-786.
    • (2011) Nat. Methods , vol.8 , pp. 785-786
    • Petersen, T.N.1    Brunak, S.2    von Heijne, G.3    Nielsen, H.4
  • 34
    • 34447644452 scopus 로고    scopus 로고
    • Sequence analysis and molecular characterization of larval midgut cDNA transcripts encoding peptidases from the yellow mealworm, Tenebrio molitor
    • Prabhakar S., Chen M.S., Elpidina E.N., Vinokurov K.S., Smith C.M., Marshall J., Oppert B. Sequence analysis and molecular characterization of larval midgut cDNA transcripts encoding peptidases from the yellow mealworm, Tenebrio molitor. Insect Mol. Biol. 2007, 16:455-468.
    • (2007) Insect Mol. Biol. , vol.16 , pp. 455-468
    • Prabhakar, S.1    Chen, M.S.2    Elpidina, E.N.3    Vinokurov, K.S.4    Smith, C.M.5    Marshall, J.6    Oppert, B.7
  • 37
    • 0037124049 scopus 로고    scopus 로고
    • Identification and characterization of prolylcarboxypeptidase as an endothelial cell prekallikrein activator
    • Shariat-Madar Z., Mahdi F., Schmaier A.H. Identification and characterization of prolylcarboxypeptidase as an endothelial cell prekallikrein activator. J. Biol. Chem. 2002, 277:17962-17969.
    • (2002) J. Biol. Chem. , vol.277 , pp. 17962-17969
    • Shariat-Madar, Z.1    Mahdi, F.2    Schmaier, A.H.3
  • 38
    • 2942525155 scopus 로고    scopus 로고
    • Recombinant prolylcarboxypeptidase activates plasma prekallikrein
    • Shariat-Madar Z., Mahdi F., Schmaier A.H. Recombinant prolylcarboxypeptidase activates plasma prekallikrein. Blood 2004, 103:4554-4561.
    • (2004) Blood , vol.103 , pp. 4554-4561
    • Shariat-Madar, Z.1    Mahdi, F.2    Schmaier, A.H.3
  • 40
    • 0036010140 scopus 로고    scopus 로고
    • Cereal seed storage proteins: structures, properties and role in grain utilization
    • Shewry P.R., Halford N.G. Cereal seed storage proteins: structures, properties and role in grain utilization. J. Exp. Bot. 2002, 53:947-958.
    • (2002) J. Exp. Bot. , vol.53 , pp. 947-958
    • Shewry, P.R.1    Halford, N.G.2
  • 41
    • 0025357314 scopus 로고
    • The prolamin storage proteins of cereal seeds: structure and evolution
    • Shewry P.R., Tatham A.S. The prolamin storage proteins of cereal seeds: structure and evolution. Biochem. J. 1990, 267:1-12.
    • (1990) Biochem. J. , vol.267 , pp. 1-12
    • Shewry, P.R.1    Tatham, A.S.2
  • 43
    • 11844271256 scopus 로고
    • L-Pyroglutamyl-L-phenylalanyl-L-alanyne p-nitroanilide - a chromogenic substrate of thiol proteinases
    • Russian inventor's certificate no. 1198082, (in Russian)
    • Stepanov V.M., Lysogorskaya E.N., Filippova I.Yu, Oksenoit E.S., Lyublinskaya L.A. L-Pyroglutamyl-L-phenylalanyl-L-alanyne p-nitroanilide - a chromogenic substrate of thiol proteinases. Byul. Izobr. 1985, 46. Russian inventor's certificate no. 1198082, (in Russian).
    • (1985) Byul. Izobr. , vol.46
    • Stepanov, V.M.1    Lysogorskaya, E.N.2    Filippova, I.3    Oksenoit, E.S.4    Lyublinskaya, L.A.5
  • 44
    • 85007742553 scopus 로고
    • Prolylcarboxypeptidase (angiotensinase C): purification and characterization of the enzyme from Xanthomonas maltophilia
    • Suga K., Ito K., Tsuru D., Yoshimoto T. Prolylcarboxypeptidase (angiotensinase C): purification and characterization of the enzyme from Xanthomonas maltophilia. Biosci. Biotechnol. Biochem. 1995, 59:298-301.
    • (1995) Biosci. Biotechnol. Biochem. , vol.59 , pp. 298-301
    • Suga, K.1    Ito, K.2    Tsuru, D.3    Yoshimoto, T.4
  • 45
    • 0029103020 scopus 로고
    • High-performance liquid chromatographic determination of prolylcarboxypeptidase activity in monkey kidney
    • Suzawa Y., Hiraoka B.Y., Harada M., Deguchi T. High-performance liquid chromatographic determination of prolylcarboxypeptidase activity in monkey kidney. J. Chromatogr. B Biomed. Appl. 1995, 670:152-156.
    • (1995) J. Chromatogr. B Biomed. Appl. , vol.670 , pp. 152-156
    • Suzawa, Y.1    Hiraoka, B.Y.2    Harada, M.3    Deguchi, T.4
  • 46
    • 0028197445 scopus 로고
    • Angiotensin II 1 receptor-mediated contraction of pulmonary artery and its modulation by prolylcarboxypeptidase
    • Tamaoki J., Sugimoto F., Tagaya E., Isono K., Chiyotani A., Konno K. Angiotensin II 1 receptor-mediated contraction of pulmonary artery and its modulation by prolylcarboxypeptidase. J. Appl. Physiol. 1994, 76:1439-1444.
    • (1994) J. Appl. Physiol. , vol.76 , pp. 1439-1444
    • Tamaoki, J.1    Sugimoto, F.2    Tagaya, E.3    Isono, K.4    Chiyotani, A.5    Konno, K.6
  • 47
    • 0027169659 scopus 로고
    • Sequencing and cloning of human prolylcarboxypeptidase (angiotensinase C). Similarity to both serine carboxypeptidase and prolylendopeptidase families
    • Tan F., Morris P.W., Skidgel R.A., Erdos E.G. Sequencing and cloning of human prolylcarboxypeptidase (angiotensinase C). Similarity to both serine carboxypeptidase and prolylendopeptidase families. J. Biol. Chem. 1993, 268:16631-16638.
    • (1993) J. Biol. Chem. , vol.268 , pp. 16631-16638
    • Tan, F.1    Morris, P.W.2    Skidgel, R.A.3    Erdos, E.G.4
  • 48
    • 0029977174 scopus 로고    scopus 로고
    • Midgut proteinases in three divergent species of Coleoptera. The major cysteine peptidase activity is cathepsin L
    • Terra W.R., Cristofoletti P.T. Midgut proteinases in three divergent species of Coleoptera. The major cysteine peptidase activity is cathepsin L. Comp. Biochem. Physiol. 1996, 113B:725-730.
    • (1996) Comp. Biochem. Physiol. , vol.113 B , pp. 725-730
    • Terra, W.R.1    Cristofoletti, P.T.2
  • 49
    • 0027999854 scopus 로고
    • Insect digestive enzymes: properties, compartmentalization and function
    • Terra W.R., Ferreira C. Insect digestive enzymes: properties, compartmentalization and function. Comp. Biochem. Physiol. 1994, 109B:1-62.
    • (1994) Comp. Biochem. Physiol. , vol.109 B , pp. 1-62
    • Terra, W.R.1    Ferreira, C.2
  • 50
    • 0000655616 scopus 로고
    • Phylogenetic consideration of insect digestion. Disaccharidases and the spatial organization of digestion in the Tenebrio molitor larvae
    • Terra W.R., Ferreira C., Bastos F. Phylogenetic consideration of insect digestion. Disaccharidases and the spatial organization of digestion in the Tenebrio molitor larvae. Insect Biochem. 1985, 15:443-449.
    • (1985) Insect Biochem. , vol.15 , pp. 443-449
    • Terra, W.R.1    Ferreira, C.2    Bastos, F.3
  • 51
    • 25444434111 scopus 로고    scopus 로고
    • Digestive proteinases of yellow mealworm (Tenebrio molitor) larvae: purification and characterization of a trypsin-like proteinase
    • Tsybina T.A., Dunaevsky Y.E., Belozersky M.A., Zhuzhikov D.P., Oppert B., Elpidina E.N. Digestive proteinases of yellow mealworm (Tenebrio molitor) larvae: purification and characterization of a trypsin-like proteinase. Biochemistry (Moscow) 2005, 70:370-377.
    • (2005) Biochemistry (Moscow) , vol.70 , pp. 370-377
    • Tsybina, T.A.1    Dunaevsky, Y.E.2    Belozersky, M.A.3    Zhuzhikov, D.P.4    Oppert, B.5    Elpidina, E.N.6
  • 54
    • 11844301660 scopus 로고    scopus 로고
    • An overlay technique for postelectrophoretic analysis of proteinase spectra in complex mixtures using p-nitroanilide substrates
    • Vinokurov K.S., Oppert B., Elpidina E.N. An overlay technique for postelectrophoretic analysis of proteinase spectra in complex mixtures using p-nitroanilide substrates. Anal. Biochem. 2005, 337:164-166.
    • (2005) Anal. Biochem. , vol.337 , pp. 164-166
    • Vinokurov, K.S.1    Oppert, B.2    Elpidina, E.N.3
  • 59
    • 78649361585 scopus 로고    scopus 로고
    • Identification and expression profile of multiple genes in response to magnesium exposure in Culex quinquefasciatus larvae
    • Zhao L., Becnel J.J., Clark G.G., Linthicum K.J., Chen J., Jin X. Identification and expression profile of multiple genes in response to magnesium exposure in Culex quinquefasciatus larvae. J. Med. Entomol. 2010, 47:1053-1061.
    • (2010) J. Med. Entomol. , vol.47 , pp. 1053-1061
    • Zhao, L.1    Becnel, J.J.2    Clark, G.G.3    Linthicum, K.J.4    Chen, J.5    Jin, X.6
  • 60
    • 0035046755 scopus 로고    scopus 로고
    • Reverse transcriptase template switching, a SMART approach for full-length cDNA library construction
    • Zhu Y.Y., Machleder E.M., Chenchik A., Li R., Siebert P.D. Reverse transcriptase template switching, a SMART approach for full-length cDNA library construction. Biotechniques 2001, 30:892-897.
    • (2001) Biotechniques , vol.30 , pp. 892-897
    • Zhu, Y.Y.1    Machleder, E.M.2    Chenchik, A.3    Li, R.4    Siebert, P.D.5


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