메뉴 건너뛰기




Volumn 9, Issue 7, 1997, Pages 659-664

Comparison of LHRH-peptidase and plasminogen activator activity in rat testis extracts

Author keywords

Angiotensins; Gonadotrophin releasing hormone associated peptide; Plasmin; Plasminogen activator inhibitors; Prolyl endopeptidase

Indexed keywords

PEPTIDASE; UROKINASE;

EID: 0031428706     PISSN: 10313613     EISSN: None     Source Type: Journal    
DOI: 10.1071/R97062     Document Type: Article
Times cited : (5)

References (43)
  • 2
    • 0027979145 scopus 로고
    • Isolation and characterization of a dibasic selective metalloendopeptidase from rat testes that cleaves at the amino terminus of arginine residues
    • Chesneau, V., Pierotti, A. R., Barré, N., Créminon, C., Tougard, C., and Cohen, P. (1994). Isolation and characterization of a dibasic selective metalloendopeptidase from rat testes that cleaves at the amino terminus of arginine residues. J. Biol. Chem. 269, 2056-61.
    • (1994) J. Biol. Chem. , vol.269 , pp. 2056-2061
    • Chesneau, V.1    Pierotti, A.R.2    Barré, N.3    Créminon, C.4    Tougard, C.5    Cohen, P.6
  • 3
    • 0021860568 scopus 로고
    • Soluble metalloendopeptidase from rat brain: Action on enkephalin-containing peptides and other bioactive peptides
    • Chu, T. G., and Orlowski, M. (1985). Soluble metalloendopeptidase from rat brain: action on enkephalin-containing peptides and other bioactive peptides. Endocrinology 116, 1418-25.
    • (1985) Endocrinology , vol.116 , pp. 1418-1425
    • Chu, T.G.1    Orlowski, M.2
  • 4
    • 0021919091 scopus 로고
    • Formation of stable complexes between urokinase and a human urinary component
    • Cieplak, W., and Hart, D. A. (1985). Formation of stable complexes between urokinase and a human urinary component. Tromb. Haemostas. 53, 36-41.
    • (1985) Tromb. Haemostas. , vol.53 , pp. 36-41
    • Cieplak, W.1    Hart, D.A.2
  • 5
    • 0022449912 scopus 로고
    • Development of specific antisera and a radioimmunoassay procedure for the gonadotropin-releasing hormone associated peptide (GAP) of the LHRH prohormone
    • Culler, M. D., and Negro-Vilar, A. (1986). Development of specific antisera and a radioimmunoassay procedure for the gonadotropin-releasing hormone associated peptide (GAP) of the LHRH prohormone. Brain Res. Bull. 17, 219-23.
    • (1986) Brain Res. Bull. , vol.17 , pp. 219-223
    • Culler, M.D.1    Negro-Vilar, A.2
  • 7
    • 0015139369 scopus 로고
    • Concentrations of angiotensin-convcrting enzyme in tissues of the rat
    • Cushman, D. W., and Cheung, H. S. (1971). Concentrations of angiotensin-convcrting enzyme in tissues of the rat. Biochim. Biophys. Acta 250, 261-5.
    • (1971) Biochim. Biophys. Acta , vol.250 , pp. 261-265
    • Cushman, D.W.1    Cheung, H.S.2
  • 8
    • 0023200721 scopus 로고
    • Effect of an LHRH-agonist on testicular microcirculation in hypophysectomized rats
    • Damber, J. E., Bergh, A., and Widmark, A. (1987). Effect of an LHRH-agonist on testicular microcirculation in hypophysectomized rats. Int. J. Androl. 10, 785-91.
    • (1987) Int. J. Androl. , vol.10 , pp. 785-791
    • Damber, J.E.1    Bergh, A.2    Widmark, A.3
  • 10
    • 0000888012 scopus 로고
    • Proteases and antiproteases in the seminiferous tubule
    • Eds L. D. Russell and M. D. Griswold. Cache River Press: Clearwater, USA
    • Fritz, I. B., Tung, P. S., and Ailenberg, M. (1993). Proteases and antiproteases in the seminiferous tubule. In 'The Sertoli Cell'. (Eds L. D. Russell and M. D. Griswold.) pp. 217-35. (Cache River Press: Clearwater, USA.)
    • (1993) The Sertoli Cell , pp. 217-235
    • Fritz, I.B.1    Tung, P.S.2    Ailenberg, M.3
  • 11
    • 0020609834 scopus 로고
    • Plasminogen activators of the pituitary gland: Enzyme characterization and hormonal modulation
    • Granelli-Piperno, A., and Reich, E. (1983). Plasminogen activators of the pituitary gland: enzyme characterization and hormonal modulation. J. Cell Biol. 97, 1029-37.
    • (1983) J. Cell Biol. , vol.97 , pp. 1029-1037
    • Granelli-Piperno, A.1    Reich, E.2
  • 12
    • 0022461143 scopus 로고
    • Species differences in the detection of high molecular weight urinary plasminogen activators
    • Hart, D. A., Rehemtulla, A., and Babins, E. M. (1986). Species differences in the detection of high molecular weight urinary plasminogen activators. Comp. Biochem. Physiol. 84B, 287-93.
    • (1986) Comp. Biochem. Physiol. , vol.84 B , pp. 287-293
    • Hart, D.A.1    Rehemtulla, A.2    Babins, E.M.3
  • 13
    • 0025734107 scopus 로고
    • Localization of immunoreactive β-endorphin and adrenocorticotropic hormone, and pro-opiomelanocortin mRNA to testicular interstitial tissue macrophages
    • He, X. L., Hedger, M. P., Clements, J. A., and Risbridger, G. P. (1991). Localization of immunoreactive β-endorphin and adrenocorticotropic hormone, and pro-opiomelanocortin mRNA to testicular interstitial tissue macrophages. Biol. Reprod. 45, 282-9.
    • (1991) Biol. Reprod. , vol.45 , pp. 282-289
    • He, X.L.1    Hedger, M.P.2    Clements, J.A.3    Risbridger, G.P.4
  • 14
  • 15
    • 0022255421 scopus 로고
    • The isolation and measurement of luteinizing hormone-releasing hormone (LHRH) from the rat testis
    • Hedger, M. P., Robertson, D. M., Browne, C. A., and de Kretser, D. M. (1985). The isolation and measurement of luteinizing hormone-releasing hormone (LHRH) from the rat testis. Mol. Cell. Endocr. 42, 163-74.
    • (1985) Mol. Cell. Endocr. , vol.42 , pp. 163-174
    • Hedger, M.P.1    Robertson, D.M.2    Browne, C.A.3    De Kretser, D.M.4
  • 16
    • 0022458210 scopus 로고
    • Degradation of luteinizing hormone-releasing hormone (LHRH) and an LHRH agonist by the rat testis
    • Hedger, M. P., Robertson, D. M., Tepe, S. J., Browne, C. A., and de Kretser, D. M. (1986). Degradation of luteinizing hormone-releasing hormone (LHRH) and an LHRH agonist by the rat testis. Mol. Cell. Endocrinol. 46, 59-70.
    • (1986) Mol. Cell. Endocrinol. , vol.46 , pp. 59-70
    • Hedger, M.P.1    Robertson, D.M.2    Tepe, S.J.3    Browne, C.A.4    De Kretser, D.M.5
  • 17
    • 0344726001 scopus 로고
    • LHRH and 'LHRH-like' factors in the male reproductive tract
    • Eds H. Vickery and J. J. Nestor, Jr. MTP Press: Lancaster, USA
    • Hedger, M. P., Robertson, D. M., and de Kretser, D. M. (1987). LHRH and 'LHRH-like' factors in the male reproductive tract. In 'LHRH and it Analogs: Contraceptive and Therapeutic Applications'. (Eds H. Vickery and J. J. Nestor, Jr.) pp. 141-160. (MTP Press: Lancaster, USA.)
    • (1987) LHRH and It Analogs: Contraceptive and Therapeutic Applications , pp. 141-160
    • Hedger, M.P.1    Robertson, D.M.2    De Kretser, D.M.3
  • 18
    • 0022965058 scopus 로고
    • Hormonal stimulation alters the type of plasminogen activator produced by Sertoli cells
    • Hettle, J. A., Waller, E. K., and Fritz, I. B. (1986). Hormonal stimulation alters the type of plasminogen activator produced by Sertoli cells. Biol. Reprod. 34, 895-904.
    • (1986) Biol. Reprod. , vol.34 , pp. 895-904
    • Hettle, J.A.1    Waller, E.K.2    Fritz, I.B.3
  • 19
    • 0023914671 scopus 로고
    • Rat testicular peritubular cells in culture secrete an inhbitor of plasminogen activator activity
    • Hettle, J. A., Balekjian, E,. Tung, P. S., and Fritz, I. B. (1988). Rat testicular peritubular cells in culture secrete an inhbitor of plasminogen activator activity. Biol. Reprod. 38, 359-71.
    • (1988) Biol. Reprod. , vol.38 , pp. 359-371
    • Hettle, J.A.1    Balekjian, E.2    Tung, P.S.3    Fritz, I.B.4
  • 20
    • 0022723059 scopus 로고
    • Arginine vasopressin in the testis: An intragonadal peptide control system
    • Kasson, B. G., Adashi, E. Y., and Hsueh, A. J. W. (1986). Arginine vasopressin in the testis: an intragonadal peptide control system. Endocr. Rev. 7, 156-68.
    • (1986) Endocr. Rev. , vol.7 , pp. 156-168
    • Kasson, B.G.1    Adashi, E.Y.2    Hsueh, A.J.W.3
  • 21
    • 0020078563 scopus 로고
    • The cellular target for the plasminogen activator, urokinase, in human fibroblasts -66 000 dalton protein
    • Keski-Oja, J., and Vaheri, A. (1982). The cellular target for the plasminogen activator, urokinase, in human fibroblasts -66 000 dalton protein. Biochim. Biophys. Acta 720, 141-6.
    • (1982) Biochim. Biophys. Acta , vol.720 , pp. 141-146
    • Keski-Oja, J.1    Vaheri, A.2
  • 22
    • 0017085135 scopus 로고
    • Post-proline cleaving enzyme. Purification of this endopeptidase by affinity chromatography
    • Koida, M., and Walter, R. (1976). Post-proline cleaving enzyme. Purification of this endopeptidase by affinity chromatography. J. Biol. Chem. 251, 7593-9.
    • (1976) J. Biol. Chem. , vol.251 , pp. 7593-7599
    • Koida, M.1    Walter, R.2
  • 23
    • 0022341176 scopus 로고
    • Human testicular angiotensin-converting enzyme is a mixture of two molecular weight forms. Only one is similar to the seminal plasma enzyme
    • Lanzillo, J. J., Desarathy, Y., Stevens, J., Bardin, C. W., and Fanburg, B. L. (1985). Human testicular angiotensin-converting enzyme is a mixture of two molecular weight forms. Only one is similar to the seminal plasma enzyme. Biochem. Biophys. Res. Commun. 128, 457-63.
    • (1985) Biochem. Biophys. Res. Commun. , vol.128 , pp. 457-463
    • Lanzillo, J.J.1    Desarathy, Y.2    Stevens, J.3    Bardin, C.W.4    Fanburg, B.L.5
  • 24
    • 0022634405 scopus 로고
    • γ-endorphin-generating endopeptidase: Distribution in body tissues and cellular localization in rat testis
    • Lebouille, J. L., Burbach, J. P., de Kloet, E. R., and Rommerts, F. F. (1986). γ-endorphin-generating endopeptidase: distribution in body tissues and cellular localization in rat testis. Endocrinology 118, 372-6.
    • (1986) Endocrinology , vol.118 , pp. 372-376
    • Lebouille, J.L.1    Burbach, J.P.2    De Kloet, E.R.3    Rommerts, F.F.4
  • 25
    • 0028272080 scopus 로고
    • Evidence for a two-step mechanism of gonadotropin-releasing hormone metabolism by prolyl endopeptidase and metalloendopeptidase EC 3.4.24.15 in ovine hypothalamic extracts
    • Lew, R. A., Tetaz, T. J., Glucksman, M. J., Roberts, J. L., and Smith, A. I. (1994). Evidence for a two-step mechanism of gonadotropin-releasing hormone metabolism by prolyl endopeptidase and metalloendopeptidase EC 3.4.24.15 in ovine hypothalamic extracts. J. Biol. Chem. 269, 12626-32.
    • (1994) J. Biol. Chem. , vol.269 , pp. 12626-12632
    • Lew, R.A.1    Tetaz, T.J.2    Glucksman, M.J.3    Roberts, J.L.4    Smith, A.I.5
  • 26
    • 0023091329 scopus 로고
    • The ovarian renin-angiotensin system: Renin-like activity and angiotensin II/III immunoreactivity in gonadotropin-stimulated and unstimulated human follicular fluid
    • Lightman, A., Tarlatzis, B. C., Rzasa, P. J., Culler, M. D., Caride, V. J., Negro-Vilar, A. F., Lennard, D., DeCherney, A. H., and Naftolin, F. (1987). The ovarian renin-angiotensin system: renin-like activity and angiotensin II/III immunoreactivity in gonadotropin-stimulated and unstimulated human follicular fluid. Am. J. Obstet. Gynecol. 156, 808-16.
    • (1987) Am. J. Obstet. Gynecol. , vol.156 , pp. 808-816
    • Lightman, A.1    Tarlatzis, B.C.2    Rzasa, P.J.3    Culler, M.D.4    Caride, V.J.5    Negro-Vilar, A.F.6    Lennard, D.7    DeCherney, A.H.8    Naftolin, F.9
  • 27
    • 0023733678 scopus 로고
    • Porcine muscle prolyl endopeptidase and its endogenous substrates
    • Moriyama, A., Nakanishi, M., and Sasaki, M. (1988). Porcine muscle prolyl endopeptidase and its endogenous substrates. J. Biochem. 104, 112-17.
    • (1988) J. Biochem. , vol.104 , pp. 112-117
    • Moriyama, A.1    Nakanishi, M.2    Sasaki, M.3
  • 28
    • 0028102361 scopus 로고
    • Localization of urokinase- And tissue-type plasminogen activator mRNAs in rat testes
    • Penttilä, T. L., Kaipia, A., Toppari, J., Parvinen, M., and Mali, P. (1994). Localization of urokinase-and tissue-type plasminogen activator mRNAs in rat testes. Mol. Cell. Endocr. 105, 55-64.
    • (1994) Mol. Cell. Endocr. , vol.105 , pp. 55-64
    • Penttilä, T.L.1    Kaipia, A.2    Toppari, J.3    Parvinen, M.4    Mali, P.5
  • 29
    • 0025007049 scopus 로고
    • Molecular cloning and primary structure of rat testes metalloendopeptidase EC 3.4.24.15
    • Pierotti, A., Dong, K. W., Glucksman, M. J., Orlowski, M., and Roberts, J. L. (1990). Molecular cloning and primary structure of rat testes metalloendopeptidase EC 3.4.24.15. Biochemistry 29, 10323-9.
    • (1990) Biochemistry , vol.29 , pp. 10323-10329
    • Pierotti, A.1    Dong, K.W.2    Glucksman, M.J.3    Orlowski, M.4    Roberts, J.L.5
  • 30
    • 0025610577 scopus 로고
    • Serine protease and metalloprotease cascade systems involved in pericellular proteolysis
    • Quigley, J. P., Berkenpas, M. B., Aimes, R. T., and Chen, J. M. (1990). Serine protease and metalloprotease cascade systems involved in pericellular proteolysis. Cell. Differ. Dev. 32, 263-76.
    • (1990) Cell. Differ. Dev. , vol.32 , pp. 263-276
    • Quigley, J.P.1    Berkenpas, M.B.2    Aimes, R.T.3    Chen, J.M.4
  • 32
    • 0019450328 scopus 로고
    • Radial caseinolysis in agarose: A simple method for detection of plasminogen activator in the presence of inhibitory substances and serum
    • Saksela, O. (1981). Radial caseinolysis in agarose: a simple method for detection of plasminogen activator in the presence of inhibitory substances and serum. Anal. Biochem. 111, 276-82.
    • (1981) Anal. Biochem. , vol.111 , pp. 276-282
    • Saksela, O.1
  • 33
    • 0022999147 scopus 로고
    • Local synthesis of plasminogen by the seminiferous tubules of the testis
    • Saksela, O., and Vihko, K. K. (1986). Local synthesis of plasminogen by the seminiferous tubules of the testis. FEBS Lett. 204, 193-7.
    • (1986) FEBS Lett. , vol.204 , pp. 193-197
    • Saksela, O.1    Vihko, K.K.2
  • 34
    • 0023042278 scopus 로고
    • The processing of peptide precursors. 'Proline-directed arginyl cleavage' and other monobasic processing mechanisms
    • Schwartz, T. W. (1986). The processing of peptide precursors. 'Proline-directed arginyl cleavage' and other monobasic processing mechanisms. FEBS Lett. 200, 1-10.
    • (1986) FEBS Lett. , vol.200 , pp. 1-10
    • Schwartz, T.W.1
  • 35
    • 0020591940 scopus 로고
    • Direct effects of a luteinizing hormone-releasing hormone agonist on intratesticular levels of testosterone and interstitial fluid formation in intact male rats
    • Sharpe, R. M., Doogan, D. G., and Cooper, I. (1983). Direct effects of a luteinizing hormone-releasing hormone agonist on intratesticular levels of testosterone and interstitial fluid formation in intact male rats. Endocrinology 113, 1306-13.
    • (1983) Endocrinology , vol.113 , pp. 1306-1313
    • Sharpe, R.M.1    Doogan, D.G.2    Cooper, I.3
  • 36
    • 0019854529 scopus 로고
    • Sertoli-Leydig cell communication via an LHRH-like factor
    • Sharpe, R. M., Fraser, H. M., Cooper, I., and Rommerts, F. F. G. (1980). Sertoli-Leydig cell communication via an LHRH-like factor. Nature (Lond.) 290, 785-7.
    • (1980) Nature (Lond.) , vol.290 , pp. 785-787
    • Sharpe, R.M.1    Fraser, H.M.2    Cooper, I.3    Rommerts, F.F.G.4
  • 37
    • 0011118368 scopus 로고
    • 2- And COOH-terminal tripeptides from the luteinizing hormone-releasing hormone
    • 2-and COOH-terminal tripeptides from the luteinizing hormone-releasing hormone. Proc. Natl. Acad. Sci. USA 82, 1025-9.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 1025-1029
    • Skidgel, R.A.1    Erdös, E.G.2
  • 38
    • 0018901958 scopus 로고
    • Catabolism of neuropeptides by a brain proline endopeptidase
    • Taylor, W. L., and Dixon, J. E. (1980). Catabolism of neuropeptides by a brain proline endopeptidase. Biochem. Biophys. Res. Commun. 94, 9-15.
    • (1980) Biochem. Biophys. Res. Commun. , vol.94 , pp. 9-15
    • Taylor, W.L.1    Dixon, J.E.2
  • 39
    • 0026053146 scopus 로고
    • The plasminogen activator/plasmin system
    • Vassalli, J. D., Sappino, A. P., and Belin, D. (1991). The plasminogen activator/plasmin system. J. Clin. Invest. 88, 1067-72.
    • (1991) J. Clin. Invest. , vol.88 , pp. 1067-1072
    • Vassalli, J.D.1    Sappino, A.P.2    Belin, D.3
  • 41
    • 0017228039 scopus 로고
    • Partial purification and characterization of post-proline cleaving enzyme: Enzymatic inactivation of neurohypophyseal hormones by kidney preparations of various species
    • Walter, R. (1976). Partial purification and characterization of post-proline cleaving enzyme: enzymatic inactivation of neurohypophyseal hormones by kidney preparations of various species. Biochim. Biophys. Acta 422, 138-58.
    • (1976) Biochim. Biophys. Acta , vol.422 , pp. 138-158
    • Walter, R.1
  • 42
    • 0018750650 scopus 로고
    • Post-proline cleavine enzyme. Synthesis of a new fluorogenic substrate and distribution of the endopeptidase in rat tissues and body fluids of man
    • Yoshimoto, T., Ogita, K., Walter, R., Koida, M., and Tsuru, D. (1979). Post-proline cleavine enzyme. Synthesis of a new fluorogenic substrate and distribution of the endopeptidase in rat tissues and body fluids of man. Biochim. Biophys. Acta 569, 184-92.
    • (1979) Biochim. Biophys. Acta , vol.569 , pp. 184-192
    • Yoshimoto, T.1    Ogita, K.2    Walter, R.3    Koida, M.4    Tsuru, D.5
  • 43
    • 0023989389 scopus 로고
    • Prolyl endopeptidase from bovine testis: Purification, characterization and comparison with the enzymes from other tissues
    • Yoshimoto, T., Oyama, H., Koriyama, N., and Tsuru, D. (1988). Prolyl endopeptidase from bovine testis: purification, characterization and comparison with the enzymes from other tissues. Chem. Pharm. Bull. 36, 1456-62.
    • (1988) Chem. Pharm. Bull. , vol.36 , pp. 1456-1462
    • Yoshimoto, T.1    Oyama, H.2    Koriyama, N.3    Tsuru, D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.