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Volumn 271, Issue 11, 2004, Pages 2101-2106

Angiotensin-converting enzyme inhibition studies by natural leech inhibitors by capiliary electrophoresis and competition assay

Author keywords

Capillary electrophoresis; Invertebrate; Leech; Natural angiotensin converting inhibitor

Indexed keywords

DIPEPTIDYL CARBOXYPEPTIDASE; NEUROPEPTIDE;

EID: 2942541143     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.2004.04116.x     Document Type: Article
Times cited : (4)

References (36)
  • 1
    • 0028863980 scopus 로고
    • Recent advances in knowledge of the structure and function of the angiotensin I converting enzyme
    • Corvol, P., Michaud, A., Soubrier, F. & Williams, T.A. (1995) Recent advances in knowledge of the structure and function of the angiotensin I converting enzyme. J. Hypertens. Suppl. 13, S3-S10.
    • (1995) J. Hypertens. Suppl. , vol.13
    • Corvol, P.1    Michaud, A.2    Soubrier, F.3    Williams, T.A.4
  • 2
    • 0029202910 scopus 로고
    • Role of the renin-angiotensin system in blood pressure regulation and in human hypertension: New insights from molecular genetics
    • Corvol, P., Jeunemaitre, X., Charru, A., Kotelevtsev, Y. & Soubrier, F. (1995) Role of the renin-angiotensin system in blood pressure regulation and in human hypertension: new insights from molecular genetics. Recent Prog. Horm Res. 50, 287-308.
    • (1995) Recent Prog. Horm Res. , vol.50 , pp. 287-308
    • Corvol, P.1    Jeunemaitre, X.2    Charru, A.3    Kotelevtsev, Y.4    Soubrier, F.5
  • 3
    • 0036239324 scopus 로고    scopus 로고
    • New aspects on angiotensin-converting enzyme: From gene to disease
    • Baudin, B. (2002) New aspects on angiotensin-converting enzyme: from gene to disease. Clin. Chem. Laboratory Med. 40, 256-265.
    • (2002) Clin. Chem. Laboratory Med. , vol.40 , pp. 256-265
    • Baudin, B.1
  • 4
    • 0035809801 scopus 로고    scopus 로고
    • Characterization of immunoreactive acetyl-Ser-Asp-Lys-Pro in human plasma and urine by liquid chromatography-electrospray mass spectrometry
    • Junot, C., Pruvost, A., Creminon, C., Grognet, J.M., Benech, H. & Ezan, E. (2001) Characterization of immunoreactive acetyl-Ser-Asp-Lys-Pro in human plasma and urine by liquid chromatography-electrospray mass spectrometry. J. Chromatogr. B Biomed Sci. Appl. 752, 69-75.
    • (2001) J. Chromatogr. B Biomed Sci. Appl. , vol.752 , pp. 69-75
    • Junot, C.1    Pruvost, A.2    Creminon, C.3    Grognet, J.M.4    Benech, H.5    Ezan, E.6
  • 5
    • 0033915245 scopus 로고    scopus 로고
    • Properties and human origin of two angiotensin-I-converting enzyme inhibitory peptides isolated from a tryptic hydrolysate of human serum albumin
    • Nakagomi, K., Ebisu, H., Sadakane, Y., Fujii, N., Akizawa, T. & Tanimura, T. (2000) Properties and human origin of two angiotensin-I-converting enzyme inhibitory peptides isolated from a tryptic hydrolysate of human serum albumin. Biol. Pharm. Bull. 23, 879-883.
    • (2000) Biol. Pharm. Bull. , vol.23 , pp. 879-883
    • Nakagomi, K.1    Ebisu, H.2    Sadakane, Y.3    Fujii, N.4    Akizawa, T.5    Tanimura, T.6
  • 6
    • 0029044093 scopus 로고
    • Effect of ACE inhibitors on the quality of life of patients with heart failure
    • Rector, T.S. (1995) Effect of ACE inhibitors on the quality of life of patients with heart failure. Coron Artery Dis. 6, 310-314.
    • (1995) Coron Artery Dis. , vol.6 , pp. 310-314
    • Rector, T.S.1
  • 7
    • 0242569193 scopus 로고    scopus 로고
    • Angiotensin-converting enzyme-2 (ACE2). Comparative modeling of the active site, specificity requirements, and chloride dependence
    • Guy, J.L., Jackson, R.M., Acharya, K.R., Sturrock, E.D., Hooper, N.M. & Turner, A.J. (2003) Angiotensin-converting enzyme-2 (ACE2). Comparative modeling of the active site, specificity requirements, and chloride dependence, Biochemistry 42, 13185-13192.
    • (2003) Biochemistry , vol.42 , pp. 13185-13192
    • Guy, J.L.1    Jackson, R.M.2    Acharya, K.R.3    Sturrock, E.D.4    Hooper, N.M.5    Turner, A.J.6
  • 10
    • 0042490795 scopus 로고    scopus 로고
    • Roles of the two active sites of somatic angiotensin-converting enzyme in the cleavage of angiotensin I and bradykinin: Insights from selective inhibitors
    • Georgiadis, D., Beau, F., Czarny, B., Cotton, J., Yiotakis, A. & Dive, V. (2003) Roles of the two active sites of somatic angiotensin-converting enzyme in the cleavage of angiotensin I and bradykinin: insights from selective inhibitors. Circ Res. 93, 148-154.
    • (2003) Circ. Res. , vol.93 , pp. 148-154
    • Georgiadis, D.1    Beau, F.2    Czarny, B.3    Cotton, J.4    Yiotakis, A.5    Dive, V.6
  • 11
    • 0030910559 scopus 로고    scopus 로고
    • Investigation of inhibition angiotensin-converting enzyme (ACE) activity and opioid activity of two hemorphins, LVV-hemorphin-5 and VV-hemorphin-5, isolated from a defined peptic hydrolysate of bovine hemoglobin
    • Zhao, Q. & Piot, J.M. (1997) Investigation of inhibition angiotensin-converting enzyme (ACE) activity and opioid activity of two hemorphins, LVV-hemorphin-5 and VV-hemorphin-5, isolated from a defined peptic hydrolysate of bovine hemoglobin. Neuropeptides. 31, 147-153.
    • (1997) Neuropeptides , vol.31 , pp. 147-153
    • Zhao, Q.1    Piot, J.M.2
  • 12
    • 0025784716 scopus 로고
    • Hemorphins derived from hemoglobin have an inhibitory action on angiotensin converting enzyme activity
    • Lantz, I., Glamsta, E.L., Talback, L. & Nyberg, F. (1991) Hemorphins derived from hemoglobin have an inhibitory action on angiotensin converting enzyme activity. FEBS Lett. 287, 39-41.
    • (1991) FEBS Lett. , vol.287 , pp. 39-41
    • Lantz, I.1    Glamsta, E.L.2    Talback, L.3    Nyberg, F.4
  • 13
    • 0035079504 scopus 로고    scopus 로고
    • Plasma angiotensin II, renin activity and serum angiotensin-converting enzyme activity in non-insulin dependent diabetes mellitus patients with diabetic nephropathy
    • Nicola, W., Sidhom, G., El Khyat, Z., Ibrahim, S., Salah, A. & El Sayed, A. (2001) Plasma angiotensin II, renin activity and serum angiotensin-converting enzyme activity in non-insulin dependent diabetes mellitus patients with diabetic nephropathy. Endocr J. 48, 25-31.
    • (2001) Endocr. J. , vol.48 , pp. 25-31
    • Nicola, W.1    Sidhom, G.2    El Khyat, Z.3    Ibrahim, S.4    Salah, A.5    El Sayed, A.6
  • 14
    • 0035407641 scopus 로고    scopus 로고
    • Captopril, a specific inhibitor of angiotensin converting enzyme, enhances both trypsin and vitellogenin titers in the grey fleshfly Neobellieria bullata
    • Vandingenen, A., Hens, K., Macours, N., Zhu, W., Janssen, I., Breuer, M., De Loof, A. & Huybrechts, R. (2001) Captopril, a specific inhibitor of angiotensin converting enzyme, enhances both trypsin and vitellogenin titers in the grey fleshfly Neobellieria bullata, Arch. Insect Biochem. Physiol. 47, 161-167.
    • (2001) Arch. Insect Biochem. Physiol. , vol.47 , pp. 161-167
    • Vandingenen, A.1    Hens, K.2    Macours, N.3    Zhu, W.4    Janssen, I.5    Breuer, M.6    De Loof, A.7    Huybrechts, R.8
  • 15
    • 0036805623 scopus 로고    scopus 로고
    • Isolation and characterization of an angiotensin converting enzyme substrate from vitellogenic ovaries of Neobellieria bullata
    • Vandingenen, A., Hens, K., Baggerman, G., Macours, N., Schoofs, L., De Loof, A. & Huybrechts, R. (2002) Isolation and characterization of an angiotensin converting enzyme substrate from vitellogenic ovaries of Neobellieria bullata. Peptides. 23, 1853.
    • (2002) Peptides , vol.23 , pp. 1853
    • Vandingenen, A.1    Hens, K.2    Baggerman, G.3    Macours, N.4    Schoofs, L.5    De Loof, A.6    Huybrechts, R.7
  • 16
    • 0035186967 scopus 로고    scopus 로고
    • In vitro degradation of the Neb-Trypsin modulating oostatic factor (Neb-TMOF) in gut luminal content and hemolymph of the grey fleshfly Neobellieria Bullata
    • Zhu, W., Vandingenen, A., Huybrechts, R., Baggerman, G., De Loof, A.C.P.P., Velentza, A. & Breuer, M. (2001) In vitro degradation of the Neb-Trypsin modulating oostatic factor (Neb-TMOF) in gut luminal content and hemolymph of the grey fleshfly Neobellieria Bullata. Insect Biochem. Mol Biol. 31, 87-95.
    • (2001) Insect Biochem. Mol. Biol. , vol.31 , pp. 87-95
    • Zhu, W.1    Vandingenen, A.2    Huybrechts, R.3    Baggerman, G.4    De Loof, A.C.P.P.5    Velentza, A.6    Breuer, M.7
  • 17
    • 0022789038 scopus 로고
    • Evidence of apparent vasopressin and oxytocin peptides in the brain of the leech Rhynchobdelle Theromyzon tessulatum (O.F.M.)
    • Malecha, J., Tramu, G., Cardon, C. & Verger-Bocquet, M. (1986) Evidence of apparent vasopressin and oxytocin peptides in the brain of the leech Rhynchobdelle Theromyzon tessulatum (O.F.M.). General Comp Endocrinol 64, 13-20.
    • (1986) General Comp. Endocrinol. , vol.64 , pp. 13-20
    • Malecha, J.1    Tramu, G.2    Cardon, C.3    Verger-Bocquet, M.4
  • 18
    • 0020730776 scopus 로고
    • Osmoregulation in Hirudinea Rhynchobdellida Theromyzon tessulatum (O.F.M.). Experimental localization of the secretory zone of a regulation factor of water balance
    • Malecha, J. (1983) Osmoregulation in Hirudinea Rhynchobdellida Theromyzon tessulatum (O.F.M.). Experimental localization of the secretory zone of a regulation factor of water balance. Gen. Comp. Endocrinol. 49, 344-351.
    • (1983) Gen. Comp. Endocrinol. , vol.49 , pp. 344-351
    • Malecha, J.1
  • 19
    • 0025864499 scopus 로고
    • Yolk protein in leech. Identification, purification and characterization of vitellin and vitellogenin
    • Baert, J.L., Britel, M., Slomianny, M.C., Delbart, C., Fournet, B., Sautiere, P. & Malecha, J. (1991) Yolk protein in leech. Identification, purification and characterization of vitellin and vitellogenin. Eur J. Biochem. 201, 191-198.
    • (1991) Eur J. Biochem. , vol.201 , pp. 191-198
    • Baert, J.L.1    Britel, M.2    Slomianny, M.C.3    Delbart, C.4    Fournet, B.5    Sautiere, P.6    Malecha, J.7
  • 20
    • 0030608419 scopus 로고    scopus 로고
    • Structural characterization of osmoregulator peptides from the brain of the leech Theromyzon tessulatum IPEPYVWD IPEPYVWD-amide
    • Salzet, M., Vandenbulcke, F. & Verger-Bocquet, M. (1996) Structural characterization of osmoregulator peptides from the brain of the leech Theromyzon tessulatum IPEPYVWD IPEPYVWD-amide. Brain Res. Mol Brain Res. 43, 301-310.
    • (1996) Brain Res. Mol. Brain Res. , vol.43 , pp. 301-310
    • Salzet, M.1    Vandenbulcke, F.2    Verger-Bocquet, M.3
  • 21
    • 0029913857 scopus 로고    scopus 로고
    • Structural characterization of a novel neuropeptide from the central nervous system of the leech Erpobdella octoculata. The leech osmoregulator factor
    • Salzet, M., Bulet, P., Weber, W.M., Clauss, W., Verger-Bocquet, M. & Malecha, J. (1996) Structural characterization of a novel neuropeptide from the central nervous system of the leech Erpobdella octoculata. The leech osmoregulator factor. J. Biol. Chem. 271, 7237-7243.
    • (1996) J. Biol. Chem. , vol.271 , pp. 7237-7243
    • Salzet, M.1    Bulet, P.2    Weber, W.M.3    Clauss, W.4    Verger-Bocquet, M.5    Malecha, J.6
  • 23
    • 0034693344 scopus 로고    scopus 로고
    • Optimization of capillary electrophoretic separation of several inhibitors of the angiotensin-converting enzyme
    • Hillaert, S. & Van den Bossche, W. (2000) Optimization of capillary electrophoretic separation of several inhibitors of the angiotensin-converting enzyme. J. Chromatogr. A. 895, 33-42.
    • (2000) J. Chromatogr. A , vol.895 , pp. 33-42
    • Hillaert, S.1    Van Den Bossche, W.2
  • 24
    • 0034193579 scopus 로고    scopus 로고
    • An assay for angiotensin-converting enzyme using capillary zone electrophoresis
    • Zhang, R., Xu, X., Chen, T., Li, L. & Rao, P. (2000) An assay for angiotensin-converting enzyme using capillary zone electrophoresis. Anal Biochem. 280, 286-290.
    • (2000) Anal. Biochem. , vol.280 , pp. 286-290
    • Zhang, R.1    Xu, X.2    Chen, T.3    Li, L.4    Rao, P.5
  • 25
    • 0036377113 scopus 로고    scopus 로고
    • Characterization of four substrates emphasizes kinetic similarity between insect and human C-domain angiotensin-converting enzyme
    • Hens, K., Vandingenen, A., Macours, N., Baggerman, G., Karaoglanovic, A.C., Schoofs, L., De Loof, A. & Huybrechts, R. (2002) Characterization of four substrates emphasizes kinetic similarity between insect and human C-domain angiotensin-converting enzyme. Eur J. Biochem. 269, 3522-3530.
    • (2002) Eur J. Biochem. , vol.269 , pp. 3522-3530
    • Hens, K.1    Vandingenen, A.2    Macours, N.3    Baggerman, G.4    Karaoglanovic, A.C.5    Schoofs, L.6    De Loof, A.7    Huybrechts, R.8
  • 26
    • 0029928595 scopus 로고    scopus 로고
    • Metabolism of angiotensins by head membranes of the leech Theromyzon tessulatum
    • Laurent, V. & Salzet, M. (1996) Metabolism of angiotensins by head membranes of the leech Theromyzon tessulatum. FEBS Lett. 384, 123-127.
    • (1996) FEBS Lett. , vol.384 , pp. 123-127
    • Laurent, V.1    Salzet, M.2
  • 27
    • 0030576886 scopus 로고    scopus 로고
    • Metabolism of enkephalins in head membranes of the leech Theromyzon tessulatum by peptidases: Isolation of an enkephalin-degrading aminopeptidase
    • Laurent, V. & Salzet, M. (1996) Metabolism of enkephalins in head membranes of the leech Theromyzon tessulatum by peptidases: isolation of an enkephalin-degrading aminopeptidase. Regul Pept. 65, 123-131.
    • (1996) Regul. Pept. , vol.65 , pp. 123-131
    • Laurent, V.1    Salzet, M.2
  • 29
    • 0030665911 scopus 로고    scopus 로고
    • Biochemical identification and ganglionic localisation of leech angiotensin-converting enzymes
    • Vandenbulcke, F., Laurent, V., Verger-Bocquet, M., Stefano, G.B. & Salzet, M. (1997) Biochemical identification and ganglionic localisation of leech angiotensin-converting enzymes. Mol. Brain Res. 49, 229-237.
    • (1997) Mol. Brain Res. , vol.49 , pp. 229-237
    • Vandenbulcke, F.1    Laurent, V.2    Verger-Bocquet, M.3    Stefano, G.B.4    Salzet, M.5
  • 31
    • 0029767696 scopus 로고    scopus 로고
    • Biochemical properties of the angiotensin-converting-like enzyme from the leech Theromyzon tessulatum
    • Laurent, V. & Salzet, M. (1996) Biochemical properties of the angiotensin-converting-like enzyme from the leech Theromyzon tessulatum. Peptides. 17, 737-745.
    • (1996) Peptides , vol.17 , pp. 737-745
    • Laurent, V.1    Salzet, M.2
  • 32
    • 0035745536 scopus 로고    scopus 로고
    • Regulation of Na (+) transport across leech skin by peptide hormones and neurotransmitters
    • Milde, H., Weber, W.M., Salzet, M. & Clauss, W. (2001) Regulation of Na (+) transport across leech skin by peptide hormones and neurotransmitters. J. Exp Biol. 204, 1509-1517.
    • (2001) J. Exp. Biol. , vol.204 , pp. 1509-1517
    • Milde, H.1    Weber, W.M.2    Salzet, M.3    Clauss, W.4
  • 33
    • 0026513136 scopus 로고
    • Evidence for angiotensin-like molecules in the central nervous system of the leech Theromyzon tessulatum (O.F.M.). A possible diuretic effect
    • Salzet, M., Verger-Bocquet, M., Wattez, C. & Malecha, J. (1992) Evidence for angiotensin-like molecules in the central nervous system of the leech Theromyzon tessulatum (O.F.M.). A possible diuretic effect. Comp Biochem. Physiol. A. 101, 83-90.
    • (1992) Comp. Biochem. Physiol. A , vol.101 , pp. 83-90
    • Salzet, M.1    Verger-Bocquet, M.2    Wattez, C.3    Malecha, J.4
  • 34
    • 0035897099 scopus 로고    scopus 로고
    • Cloning and expression analysis of a cDNA that encodes a leech hemerythrin
    • Coutte, L., Slomianny, M.C., Malecha, J. & Baert, J.L. (2001) Cloning and expression analysis of a cDNA that encodes a leech hemerythrin. Biochim. Biophys. Acta. 1518, 282-286.
    • (2001) Biochim. Biophys. Acta , vol.1518 , pp. 282-286
    • Coutte, L.1    Slomianny, M.C.2    Malecha, J.3    Baert, J.L.4
  • 36
    • 0141993551 scopus 로고    scopus 로고
    • Angiotensin I-converting enzyme (ACE) activity of the tomato moth, Lacanobia oleracea: Changes in levels of activity during development and after copulation suggest roles during metamorphosis and reproduction
    • Ekbote, U.V., Weaver, R.J. & Isaac, R.E. (2003) Angiotensin I-converting enzyme (ACE) activity of the tomato moth, Lacanobia oleracea: changes in levels of activity during development and after copulation suggest roles during metamorphosis and reproduction. Insect Biochem. Mol Biol. 33, 989-998.
    • (2003) Insect Biochem. Mol. Biol. , vol.33 , pp. 989-998
    • Ekbote, U.V.1    Weaver, R.J.2    Isaac, R.E.3


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