메뉴 건너뛰기




Volumn 237, Issue 2, 1996, Pages 414-423

Cloning and characterisation of angiotensin-converting enzyme from the dipteran species, Haematobia irritans exigua, and its expression in the maturing male reproductive system

Author keywords

Angiotensin converting enzyme; Diptera neuropeptide; Haematobia irritans; Male reproductive system

Indexed keywords

DIPEPTIDYL CARBOXYPEPTIDASE;

EID: 0029866962     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1996.0414k.x     Document Type: Article
Times cited : (58)

References (51)
  • 1
    • 0017584729 scopus 로고
    • Design of potent competitive inhibitors of angiotensin-converting enzyme. Carboxyalkanoyl and mercaptoalkanoyl amino acids
    • Cushman, D. W., Cheung, H. S., Sabo, E. F. & Ondetti, M. A. (1977) Design of potent competitive inhibitors of angiotensin-converting enzyme. Carboxyalkanoyl and mercaptoalkanoyl amino acids, Biochemistry 16, 5484-5491.
    • (1977) Biochemistry , vol.16 , pp. 5484-5491
    • Cushman, D.W.1    Cheung, H.S.2    Sabo, E.F.3    Ondetti, M.A.4
  • 2
    • 0018583165 scopus 로고
    • Development of specific inhibitors of angiotensin I converting enzyme (kininase II)
    • Cushman, D. W., Cheung, H. S., Sabo, E. F., Rubin, B. & Ondetti, M. A. (1979) Development of specific inhibitors of angiotensin I converting enzyme (kininase II), Fed. Proc. 38, 2778-2782.
    • (1979) Fed. Proc. , vol.38 , pp. 2778-2782
    • Cushman, D.W.1    Cheung, H.S.2    Sabo, E.F.3    Rubin, B.4    Ondetti, M.A.5
  • 3
    • 0024347759 scopus 로고
    • Angiotensin-converting enzyme: New concepts concerning its biological role
    • Ehlers, M. R. W. & Riordan, J. F. (1989) Angiotensin-converting enzyme: new concepts concerning its biological role. Biochemistry 28, 5311-5318.
    • (1989) Biochemistry , vol.28 , pp. 5311-5318
    • Ehlers, M.R.W.1    Riordan, J.F.2
  • 4
    • 0017102431 scopus 로고
    • Biochemical properties of angiotensin-converting enzyme
    • Soffer, R. L. (1976) Biochemical properties of angiotensin-converting enzyme, Annu. Rev. Biochem. 45, 73-94.
    • (1976) Annu. Rev. Biochem. , vol.45 , pp. 73-94
    • Soffer, R.L.1
  • 5
    • 0021175531 scopus 로고
    • Hydrolysis of substance P and neurotensin by converting enzyme and neutral endopeptidase
    • Skidgel, R. A., Engelbrecht, S., Johnson, A. R. & Erdös, E. G. (1984) Hydrolysis of substance P and neurotensin by converting enzyme and neutral endopeptidase, Peptides (Elmsford) 5, 769-776.
    • (1984) Peptides (Elmsford) , vol.5 , pp. 769-776
    • Skidgel, R.A.1    Engelbrecht, S.2    Johnson, A.R.3    Erdös, E.G.4
  • 6
    • 0011118368 scopus 로고
    • 2- and COOH-terminal tripeptides from luteinizing hormone-releasing factor
    • 2- and COOH-terminal tripeptides from luteinizing hormone-releasing factor, Proc. Natl Acad. Sci. USA 82, 1025-1029.
    • (1985) Proc. Natl Acad. Sci. USA , vol.82 , pp. 1025-1029
    • Skidgel, R.A.1    Erdös, E.G.2
  • 8
    • 0024433127 scopus 로고
    • Novel activity of angiotensin-converting enzyme. Hydrolysis of cholecystokinin and gastrin analogues with release of the amidated C-terminal dipeptide
    • Dubreuil, P., Fulcrand, P., Rodriguez, M., Fulcrand, H., Laur, J. & Martinez, J. (1989) Novel activity of angiotensin-converting enzyme. Hydrolysis of cholecystokinin and gastrin analogues with release of the amidated C-terminal dipeptide, Biochem. J. 262, 125-130.
    • (1989) Biochem. J. , vol.262 , pp. 125-130
    • Dubreuil, P.1    Fulcrand, P.2    Rodriguez, M.3    Fulcrand, H.4    Laur, J.5    Martinez, J.6
  • 9
    • 0017359335 scopus 로고
    • Serum angiotensin I-converting enzyme: Isolation and relationship to the pulmonary enzyme
    • Das., M., Hartley, J. L. & Soffer, R. L. (1977) Serum angiotensin I-converting enzyme: isolation and relationship to the pulmonary enzyme. J. Biol. Chem. 252, 1316-1319.
    • (1977) J. Biol. Chem. , vol.252 , pp. 1316-1319
    • Das, M.1    Hartley, J.L.2    Soffer, R.L.3
  • 10
    • 0020074132 scopus 로고
    • Correlation between angiotensin-converting enzyme activity and histologic patterns in benign prostatic hypertropy tissue
    • Yokoyama, M., Takada, Y., Iwata, H., Ochi, K., Takeuchi, M., Hiwada, K. & Kokubu, T. (1982) Correlation between angiotensin-converting enzyme activity and histologic patterns in benign prostatic hypertropy tissue, J. Urol. 127, 368-370.
    • (1982) J. Urol. , vol.127 , pp. 368-370
    • Yokoyama, M.1    Takada, Y.2    Iwata, H.3    Ochi, K.4    Takeuchi, M.5    Hiwada, K.6    Kokubu, T.7
  • 11
    • 0022005455 scopus 로고
    • Angiotensin-converting enzyme in the testis and epididymus: Differential development and pituitary regulation of isozymes
    • Strittmatter, S. M., Theile, E. A., De Souza, E. B. & Snyder, S. H. (1985) Angiotensin-converting enzyme in the testis and epididymus: differential development and pituitary regulation of isozymes, Endocrinology 117, 1374-1379.
    • (1985) Endocrinology , vol.117 , pp. 1374-1379
    • Strittmatter, S.M.1    Theile, E.A.2    De Souza, E.B.3    Snyder, S.H.4
  • 12
    • 0026517233 scopus 로고
    • The unique N-terminal sequence of testis angiotensin-converting enzyme is heavily O-glycosylated and unessential for activity or stability
    • Ehlers, M. R. W., Chen, Y. N.-P. & Riordan, J. F. (1992) The unique N-terminal sequence of testis angiotensin-converting enzyme is heavily O-glycosylated and unessential for activity or stability, Biochem. Biophys. Res. Commun. 183, 199-205.
    • (1992) Biochem. Biophys. Res. Commun. , vol.183 , pp. 199-205
    • Ehlers, M.R.W.1    Chen, Y.N.-P.2    Riordan, J.F.3
  • 13
    • 0024425354 scopus 로고
    • Structure of testicular angiotensin-converting enzyme: A segmental mosaic enzyme
    • Kumar, R. S., Kusari, J., Roy, S. N., Soffer, R. L. & Sen, G. C. (1989) Structure of testicular angiotensin-converting enzyme: a segmental mosaic enzyme, J. Biol. Chem. 264, 16754-16758.
    • (1989) J. Biol. Chem. , vol.264 , pp. 16754-16758
    • Kumar, R.S.1    Kusari, J.2    Roy, S.N.3    Soffer, R.L.4    Sen, G.C.5
  • 14
    • 0024473131 scopus 로고
    • The testicular transcript of the angiotensin I-converting enzyme encodes for the ancestral, nonduplicated form of the enzyme
    • Lattion, A.-L., Soubrier, F., Allegrini, J., Hubert, C., Corvol, P. & Alhenc-Gelas, F. (1989) The testicular transcript of the angiotensin I-converting enzyme encodes for the ancestral, nonduplicated form of the enzyme, FEBS Lett. 252, 99-104.
    • (1989) FEBS Lett. , vol.252 , pp. 99-104
    • Lattion, A.-L.1    Soubrier, F.2    Allegrini, J.3    Hubert, C.4    Corvol, P.5    Alhenc-Gelas, F.6
  • 15
    • 0025284828 scopus 로고
    • Transcription of testicular angiotensin-converting enzyme (ACE) is initiated within the 12th intron of the somatic ACE gene
    • Howard, T. D., Shai, S. Y., Langford, K. G., Martin, B. M. & Bernstein, K. E. (1990) Transcription of testicular angiotensin-converting enzyme (ACE) is initiated within the 12th intron of the somatic ACE gene, Mol. Cell. Biol. 10, 4294-4302.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 4294-4302
    • Howard, T.D.1    Shai, S.Y.2    Langford, K.G.3    Martin, B.M.4    Bernstein, K.E.5
  • 16
    • 0022996473 scopus 로고
    • Leucosulfakinin, a sulfated insect neuropeptide with homology to gastrin and cholecystokinin
    • Nachman, R. J., Holman, G. M., Haddon, W. F. & Ling, N. (1986) Leucosulfakinin, a sulfated insect neuropeptide with homology to gastrin and cholecystokinin, Science 234, 71-73.
    • (1986) Science , vol.234 , pp. 71-73
    • Nachman, R.J.1    Holman, G.M.2    Haddon, W.F.3    Ling, N.4
  • 17
    • 0023050513 scopus 로고
    • Leucosulfakinin-II, a blocked sulfated insect neuropeptide with homology to cholecystokinin and gastrin
    • Nachman, R. J., Holman, G. M., Cook, B. J., Haddon, W. F. & Ling, N. (1986) Leucosulfakinin-II, a blocked sulfated insect neuropeptide with homology to cholecystokinin and gastrin, Biochem. Biophys. Res. Commun. 140, 357-364.
    • (1986) Biochem. Biophys. Res. Commun. , vol.140 , pp. 357-364
    • Nachman, R.J.1    Holman, G.M.2    Cook, B.J.3    Haddon, W.F.4    Ling, N.5
  • 18
    • 0024342196 scopus 로고
    • Isolation and structure of two gastrin/CCK-like neuropeptides from the American cockroach homologous to the leucosulfakinins
    • Veenstra, J. A. (1989) Isolation and structure of two gastrin/CCK-like neuropeptides from the American cockroach homologous to the leucosulfakinins, Neuropeptides 14, 145-149.
    • (1989) Neuropeptides , vol.14 , pp. 145-149
    • Veenstra, J.A.1
  • 19
    • 0024710311 scopus 로고
    • Primary structure of four allatostatins: Neuropeptide inhibitors of juvenile hormone synthesis
    • Woodhead, A. P., Stay, B., Siedel, S. L., Khan, M. A. & Tobe, S. S. (1989) Primary structure of four allatostatins: neuropeptide inhibitors of juvenile hormone synthesis, Proc. Natl Acad. Sci. USA 86, 5997-6001.
    • (1989) Proc. Natl Acad. Sci. USA , vol.86 , pp. 5997-6001
    • Woodhead, A.P.1    Stay, B.2    Siedel, S.L.3    Khan, M.A.4    Tobe, S.S.5
  • 20
    • 0028274686 scopus 로고
    • Identification and properties of a peptidyl dipeptidase in the housefly, Musca domestica, that resembles mammalian angiotensin-converting enzyme
    • Lamango, N. S. & Isaac, R. E. (1994) Identification and properties of a peptidyl dipeptidase in the housefly, Musca domestica, that resembles mammalian angiotensin-converting enzyme, Biochem. J. 299, 651-657.
    • (1994) Biochem. J. , vol.299 , pp. 651-657
    • Lamango, N.S.1    Isaac, R.E.2
  • 21
    • 0028172007 scopus 로고
    • A protective concealed antigen from Boophilus microplus: Isolation, localisation and possible function
    • Riding, G. A., Jarmey, J., McKenna, R. V., Pearson, R., Cobon, G. S. & Willadsen, P. (1994) A protective concealed antigen from Boophilus microplus: isolation, localisation and possible function, J. Immunol. 153, 5158-5166.
    • (1994) J. Immunol. , vol.153 , pp. 5158-5166
    • Riding, G.A.1    Jarmey, J.2    McKenna, R.V.3    Pearson, R.4    Cobon, G.S.5    Willadsen, P.6
  • 22
    • 9244253811 scopus 로고    scopus 로고
    • Cobon, G., Willadsen, P., Kemp, D., Tellam, R., inventors; Biotech Australia Pty Ltd., CSIRO assignees. Tick antigen. PCT/AU94/00463. 1994
    • Cobon, G., Willadsen, P., Kemp, D., Tellam, R., inventors; Biotech Australia Pty Ltd., CSIRO assignees. Tick antigen. PCT/AU94/00463. 1994.
  • 24
    • 0028978407 scopus 로고
    • Race: A Drosophila homologue of the angiotensin converting enzyme
    • Tatei, K., Cai, H., Ip, Y. T. & Levine, M. (1995) Race: a Drosophila homologue of the angiotensin converting enzyme, Mech. Dev. 51, 157-168.
    • (1995) Mech. Dev. , vol.51 , pp. 157-168
    • Tatei, K.1    Cai, H.2    Ip, Y.T.3    Levine, M.4
  • 25
    • 0017697995 scopus 로고
    • A simple radioassay for angiotensin-converting enzyme
    • Ryan, J. W., Chung, A., Ammons, C. & Carlton, M. L. (1977) A simple radioassay for angiotensin-converting enzyme, Biochem. J. 167, 501-504.
    • (1977) Biochem. J. , vol.167 , pp. 501-504
    • Ryan, J.W.1    Chung, A.2    Ammons, C.3    Carlton, M.L.4
  • 26
    • 0029379628 scopus 로고
    • Carboxydipeptidase from Boophilus microplus: A 'concealed' antigen with similarity to angiotensin converting enzyme
    • Jarmey, J. N., Riding, G. A., Pearson, R., McKenna, R. V. & Willadsen, P. (1995) Carboxydipeptidase from Boophilus microplus: a 'concealed' antigen with similarity to angiotensin converting enzyme, Insect Biochem. Mol. Biol. 25, 969-974.
    • (1995) Insect Biochem. Mol. Biol. , vol.25 , pp. 969-974
    • Jarmey, J.N.1    Riding, G.A.2    Pearson, R.3    McKenna, R.V.4    Willadsen, P.5
  • 29
    • 0027320313 scopus 로고
    • A family of serine protease genes expressed in adult buffalo fly (Haematobia irritans exigua)
    • Elvin, C. M., Whan, V. & Riddles, P. W. (1993) A family of serine protease genes expressed in adult buffalo fly (Haematobia irritans exigua), Mol. & Gen. Genet. 240, 132-139.
    • (1993) Mol. & Gen. Genet. , vol.240 , pp. 132-139
    • Elvin, C.M.1    Whan, V.2    Riddles, P.W.3
  • 30
    • 0028534766 scopus 로고
    • Excretory/secretory chymotrypsin from Lucilia cuprina: Purification, enzymatic specificity and amino acid sequence from mRNA
    • Casu, R. E., Pearson, R. D., Jarmey, J. M., Cadogan, L. C., Riding, G. A. & Tellam, R. L. (1994) Excretory/secretory chymotrypsin from Lucilia cuprina: purification, enzymatic specificity and amino acid sequence from mRNA, Insect Mol. Biol. 3, 201-211.
    • (1994) Insect Mol. Biol. , vol.3 , pp. 201-211
    • Casu, R.E.1    Pearson, R.D.2    Jarmey, J.M.3    Cadogan, L.C.4    Riding, G.A.5    Tellam, R.L.6
  • 31
    • 0020678693 scopus 로고
    • Activation of angiotensin converting enzyme by monovalent anions
    • Bünning, P. & Riordan, J. F. (1983) Activation of angiotensin converting enzyme by monovalent anions, Biochemistry 22, 110-116.
    • (1983) Biochemistry , vol.22 , pp. 110-116
    • Bünning, P.1    Riordan, J.F.2
  • 32
    • 0023878613 scopus 로고
    • Improvement and simplification of low background silver staining of proteins by using sodium dithionite
    • Rabilloud, T., Carpentier, G. & Tarroux, P. (1988) Improvement and simplification of low background silver staining of proteins by using sodium dithionite, Electrophoresis 9, 288-291.
    • (1988) Electrophoresis , vol.9 , pp. 288-291
    • Rabilloud, T.1    Carpentier, G.2    Tarroux, P.3
  • 34
    • 0024979085 scopus 로고
    • Enhancement of immunoblot staining using a mixed chromogenic substrate
    • Young, P. R. (1989) Enhancement of immunoblot staining using a mixed chromogenic substrate, J. Immunol. Methods 121, 295-296.
    • (1989) J. Immunol. Methods , vol.121 , pp. 295-296
    • Young, P.R.1
  • 35
    • 0019887744 scopus 로고
    • Phase separation of integral membrane proteins in Triton X-114 solution
    • Bordier, C. (1981) Phase separation of integral membrane proteins in Triton X-114 solution, J. Biol. Chem. 256, 1604-1607.
    • (1981) J. Biol. Chem. , vol.256 , pp. 1604-1607
    • Bordier, C.1
  • 36
    • 0017293687 scopus 로고
    • Kinetic properties of pulmonary angiotensin-converting enzyme. Hydrolysis of hippurylglycylglycine
    • Dorer, F. E., Kahn, J. R., Lentz, K. E., Levine, M. & Skeggs, L. T. (1976) Kinetic properties of pulmonary angiotensin-converting enzyme. Hydrolysis of hippurylglycylglycine, Biochim. Biophys. Acta 429, 220-228.
    • (1976) Biochim. Biophys. Acta , vol.429 , pp. 220-228
    • Dorer, F.E.1    Kahn, J.R.2    Lentz, K.E.3    Levine, M.4    Skeggs, L.T.5
  • 38
    • 0027970068 scopus 로고
    • Identification of two active site residues in human angiotensin I-converting enzyme
    • Williams, T. A., Corvol, P. A & Soubrier, F. (1994) Identification of two active site residues in human angiotensin I-converting enzyme, J. Biol. Chem. 269, 29430-29434.
    • (1994) J. Biol. Chem. , vol.269 , pp. 29430-29434
    • Williams, T.A.1    Corvol, P.A.2    Soubrier, F.3
  • 39
    • 0027312101 scopus 로고
    • Molecular biology of the angiotensin I converting enzyme. I. Biochemistry and structure of the gene
    • Soubrier, F., Hubert, C., Testut, P., Nadaud, S., Alhenc-Gelas, F. & Corvol, P. (1993) Molecular biology of the angiotensin I converting enzyme. I. Biochemistry and structure of the gene, J. Hypertens. 11, 471-476.
    • (1993) J. Hypertens. , vol.11 , pp. 471-476
    • Soubrier, F.1    Hubert, C.2    Testut, P.3    Nadaud, S.4    Alhenc-Gelas, F.5    Corvol, P.6
  • 40
    • 0026052382 scopus 로고
    • Peptide inhibitors and the active site(s) of angiotensin converting enzyme
    • Riordan, J. F., Chen, Y.-N. P., Kleemann, S. G. & Banning, P. (1991) Peptide inhibitors and the active site(s) of angiotensin converting enzyme, Biomed. Biochim. Acta 50, 809-814.
    • (1991) Biomed. Biochim. Acta , vol.50 , pp. 809-814
    • Riordan, J.F.1    Chen, Y.-N.P.2    Kleemann, S.G.3    Banning, P.4
  • 42
    • 0018886259 scopus 로고
    • Inhibitors of angiotensin-converting enzyme for treatment of hypertension
    • Cushman, D. W. & Ondetti, M. A. (1980) Inhibitors of angiotensin-converting enzyme for treatment of hypertension, Biochem. Pharmacol. 29, 1871-1877.
    • (1980) Biochem. Pharmacol. , vol.29 , pp. 1871-1877
    • Cushman, D.W.1    Ondetti, M.A.2
  • 43
    • 0022378632 scopus 로고
    • Substance P and substance K as possible endogenous substrates of angiotensin converting enzyme in the brain
    • Thiele, E. A., Strittmatter, S. M. & Snyder, S. H. (1985) Substance P and substance K as possible endogenous substrates of angiotensin converting enzyme in the brain, Biochem. Biophys. Res. Commun. 128, 317-324.
    • (1985) Biochem. Biophys. Res. Commun. , vol.128 , pp. 317-324
    • Thiele, E.A.1    Strittmatter, S.M.2    Snyder, S.H.3
  • 44
    • 0021329606 scopus 로고
    • Carboxyl-terminal tripeptidyl hydrolysis of substance P by purified rabbit lung angiotensin-converting enzyme and the potentiation of substance P activity in vivo by captopril and MK-422
    • Cascieri, M. A., Bull, H. G., Mumford, R. A., Patchett, A. A., Thomberry, N. A. & Liang, T. (1984) Carboxyl-terminal tripeptidyl hydrolysis of substance P by purified rabbit lung angiotensin-converting enzyme and the potentiation of substance P activity in vivo by captopril and MK-422, Mol. Pharmacol. 25, 287-293.
    • (1984) Mol. Pharmacol. , vol.25 , pp. 287-293
    • Cascieri, M.A.1    Bull, H.G.2    Mumford, R.A.3    Patchett, A.A.4    Thomberry, N.A.5    Liang, T.6
  • 45
    • 0021043072 scopus 로고
    • A new feature of angiotensin-converting enzyme in the brain: Hydrolysis of substance P, Biochem
    • Yokosawa, H., Endo, S., Ogura, Y. & Ishii, S.-I. (1983) A new feature of angiotensin-converting enzyme in the brain: hydrolysis of substance P, Biochem. Biophys. Res. Commun. 116, 735-742.
    • (1983) Biophys. Res. Commun. , vol.116 , pp. 735-742
    • Yokosawa, H.1    Endo, S.2    Ogura, Y.3    Ishii, S.-I.4
  • 46
    • 0017578611 scopus 로고
    • Design of specific inhibitors of angiotensin-converting enzyme: New class of orally active hypertensive agents
    • Ondetti, M. A., Rubin, B. & Cushman, D. W. (1977) Design of specific inhibitors of angiotensin-converting enzyme: new class of orally active hypertensive agents. Science 196, 441-444.
    • (1977) Science , vol.196 , pp. 441-444
    • Ondetti, M.A.1    Rubin, B.2    Cushman, D.W.3
  • 47
    • 0015139369 scopus 로고
    • Concentrations of angiotensin-converting enzyme in tissues of the rat, Biochim
    • Cushman, D. W. & Cheung, H. S. (1971) Concentrations of angiotensin-converting enzyme in tissues of the rat, Biochim. Biophys. Acta 250, 261-265.
    • (1971) Biophys. Acta , vol.250 , pp. 261-265
    • Cushman, D.W.1    Cheung, H.S.2
  • 48
    • 0016297590 scopus 로고
    • Influence of diapause and diet on the development of gonads and accessory reproductive glands of the black blowfly, Phormia regina (Meigen)
    • Stoffolano, J. G. (1974) Influence of diapause and diet on the development of gonads and accessory reproductive glands of the black blowfly, Phormia regina (Meigen), Can. J. Zool. 52, 981-988.
    • (1974) Can. J. Zool. , vol.52 , pp. 981-988
    • Stoffolano, J.G.1
  • 49
    • 0007751735 scopus 로고
    • Male sexual maturation of the tsetse flies Glossina morisitans Westwood and G. austeni Newstead (Dipt., Glossinidae) in relation to blood feeding
    • Foster, W. A. (1976) Male sexual maturation of the tsetse flies Glossina morisitans Westwood and G. austeni Newstead (Dipt., Glossinidae) in relation to blood feeding, Bull. Entomol. Res. 66, 389-399.
    • (1976) Bull. Entomol. Res. , vol.66 , pp. 389-399
    • Foster, W.A.1
  • 50
    • 0018271367 scopus 로고
    • Mating behaviour of Stomoxys calcitrans: Effects of a blood meal on the mating drive of males and its necessity as a prerequisite for proper insemination of females
    • Anderson J. R. (1978) Mating behaviour of Stomoxys calcitrans: effects of a blood meal on the mating drive of males and its necessity as a prerequisite for proper insemination of females, J. Econ. Entomol. 71, 379-386.
    • (1978) J. Econ. Entomol. , vol.71 , pp. 379-386
    • Anderson, J.R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.