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Volumn 42, Issue 3, 2003, Pages 231-237

Anterograde axonal transport of endopeptidase 24.15 in rat sciatic nerves

Author keywords

Axonal flow; Deamidase; EP24.15; Immunohistochemistry; Ligation; Sciatic nerve

Indexed keywords

AMIDASE; THIMET OLIGOPEPTIDASE;

EID: 0037290229     PISSN: 01970186     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0197-0186(02)00092-X     Document Type: Article
Times cited : (14)

References (26)
  • 1
    • 0020320365 scopus 로고
    • Functions of retrograde axonal transport
    • Bisby M.A. Functions of retrograde axonal transport. Fed. Proc. 41:1982;2307-2311.
    • (1982) Fed. Proc. , vol.41 , pp. 2307-2311
    • Bisby, M.A.1
  • 2
    • 0027416150 scopus 로고
    • High-performance liquid chromatographic determination of PZ-peptidase activity
    • Chikuma T., Tanaka W., Yamada K., Ishii Y., Tanaka A., Kato T. High-performance liquid chromatographic determination of PZ-peptidase activity. J. Chromatogr. 635:1993;81-87.
    • (1993) J. Chromatogr. , vol.635 , pp. 81-87
    • Chikuma, T.1    Tanaka, W.2    Yamada, K.3    Ishii, Y.4    Tanaka, A.5    Kato, T.6
  • 3
    • 0030049476 scopus 로고    scopus 로고
    • A fluorometric assay for measuring deamidase (lysosomal protective protein) using high-performance liquid chromatography
    • Chikuma T., Matsumoto K., Furukawa A., Nakayama N., Yajima R., Kato T., Ishii Y., Tanaka A. A fluorometric assay for measuring deamidase (lysosomal protective protein) using high-performance liquid chromatography. Anal. Biochem. 233:1996;36-41.
    • (1996) Anal. Biochem. , vol.233 , pp. 36-41
    • Chikuma, T.1    Matsumoto, K.2    Furukawa, A.3    Nakayama, N.4    Yajima, R.5    Kato, T.6    Ishii, Y.7    Tanaka, A.8
  • 4
    • 0033600514 scopus 로고    scopus 로고
    • The association of metalloendopeptidase EC 3.4.24.15 at the extracellular surface of the at T-20 cell plasma membrane
    • Crack P.J., Wu T.J., Cummins P.M., Ferro E.S., Tullai J.W., Glucksman M.J., Roberts J.L. The association of metalloendopeptidase EC 3.4.24.15 at the extracellular surface of the at T-20 cell plasma membrane. Brain Res. 835:1999;113-124.
    • (1999) Brain Res. , vol.835 , pp. 113-124
    • Crack, P.J.1    Wu, T.J.2    Cummins, P.M.3    Ferro, E.S.4    Tullai, J.W.5    Glucksman, M.J.6    Roberts, J.L.7
  • 5
    • 0026760229 scopus 로고
    • Purification of the main somatostatin-degrading proteases from rat and pig brains, their action on other neuropeptides, and their identification as endopeptidases 24.15 and 24.16
    • Dahms P., Mentlein R. Purification of the main somatostatin-degrading proteases from rat and pig brains, their action on other neuropeptides, and their identification as endopeptidases 24.15 and 24.16. Eur. J. Biochem. 208:1992;145-154.
    • (1992) Eur. J. Biochem. , vol.208 , pp. 145-154
    • Dahms, P.1    Mentlein, R.2
  • 6
    • 0031038233 scopus 로고    scopus 로고
    • Degradation of bradykinin by bovine tracheal epithelium and isolated epithelial cells
    • Dendorfer A., Vordermark D., Dominiak P. Degradation of bradykinin by bovine tracheal epithelium and isolated epithelial cells. Br. J. Pharmacol. 120:1997;121-129.
    • (1997) Br. J. Pharmacol. , vol.120 , pp. 121-129
    • Dendorfer, A.1    Vordermark, D.2    Dominiak, P.3
  • 8
    • 0035479426 scopus 로고    scopus 로고
    • Comparative fine structural distribution of endopeptidase 24.15 (EC3.4.24.15) and 24.16 (EC3.4.24.16) in rat brain
    • Fontenele-Neto J.D., Massarelli E.E., Gurgel G.P.A., Beaudet A., Ferro E.S. Comparative fine structural distribution of endopeptidase 24.15 (EC3.4.24.15) and 24.16 (EC3.4.24.16) in rat brain. J. Comp. Neurol. 438:2001;399-410.
    • (2001) J. Comp. Neurol. , vol.438 , pp. 399-410
    • Fontenele-Neto, J.D.1    Massarelli, E.E.2    Gurgel, G.P.A.3    Beaudet, A.4    Ferro, E.S.5
  • 9
    • 0026573344 scopus 로고
    • Immunocytochemical localization of endopeptidase 24.15 in rat brain
    • Healy D.P., Orlowski M. Immunocytochemical localization of endopeptidase 24.15 in rat brain. Brain Res. 571:1992;121-128.
    • (1992) Brain Res. , vol.571 , pp. 121-128
    • Healy, D.P.1    Orlowski, M.2
  • 10
    • 0025340195 scopus 로고
    • A peptidase in human platelets that deamidates tachykinins. Probable identity with the lysosomal protective protein
    • Jackman H.L., Tan F.L., Tamei H., Beurling-Harbury C., Li X.Y., Skidgel R.A., Erdos E.G. A peptidase in human platelets that deamidates tachykinins. Probable identity with the lysosomal protective protein. J. Biol. Chem. 265:1990;11265-11272.
    • (1990) J. Biol. Chem. , vol.265 , pp. 11265-11272
    • Jackman, H.L.1    Tan, F.L.2    Tamei, H.3    Beurling-Harbury, C.4    Li, X.Y.5    Skidgel, R.A.6    Erdos, E.G.7
  • 12
    • 0023149318 scopus 로고
    • The axonal transport of dipeptidyl aminopeptidase II, angiotensin-converting enzyme and other peptidases in rat sciatic nerves
    • Kato T., Ishihara H., Shimizu A., Yokosawa H., Ishii S., Komiya Y. The axonal transport of dipeptidyl aminopeptidase II, angiotensin-converting enzyme and other peptidases in rat sciatic nerves. Neurosci. Res. 4:1987;241-248.
    • (1987) Neurosci. Res. , vol.4 , pp. 241-248
    • Kato, T.1    Ishihara, H.2    Shimizu, A.3    Yokosawa, H.4    Ishii, S.5    Komiya, Y.6
  • 13
    • 0031200925 scopus 로고    scopus 로고
    • Axonal transports of Boc-Gly-Arg-Arg-MCA hydrolysing enzyme in rat sciatic nerves
    • Kato T., Yajima R., Sato N., Takahashi K., Shimizu C., Chikuma T. Axonal transports of Boc-Gly-Arg-Arg-MCA hydrolysing enzyme in rat sciatic nerves. Neurochem. Int. 32:1998;163-170.
    • (1998) Neurochem. Int. , vol.32 , pp. 163-170
    • Kato, T.1    Yajima, R.2    Sato, N.3    Takahashi, K.4    Shimizu, C.5    Chikuma, T.6
  • 15
    • 0030856790 scopus 로고    scopus 로고
    • Peptidases that degrade gonadotropin-releasing hormone: Influence on LH secretion in the ewe
    • Lew R.A., Cowley M., Clarke I.J., Smith A.I. Peptidases that degrade gonadotropin-releasing hormone: influence on LH secretion in the ewe. J. Neuroendocrinol. 9:1997;707-712.
    • (1997) J. Neuroendocrinol. , vol.9 , pp. 707-712
    • Lew, R.A.1    Cowley, M.2    Clarke, I.J.3    Smith, A.I.4
  • 17
    • 0028079465 scopus 로고
    • Endopeptidases 24.16 and 24.15 are responsible for the degradation of somatostatin, neurotensin, and other neuropeptides by cultivated rat cortical astrocytes
    • Mentlein R., Dahms P. Endopeptidases 24.16 and 24.15 are responsible for the degradation of somatostatin, neurotensin, and other neuropeptides by cultivated rat cortical astrocytes. J. Neurochem. 62:1994;27-36.
    • (1994) J. Neurochem. , vol.62 , pp. 27-36
    • Mentlein, R.1    Dahms, P.2
  • 18
    • 0035836450 scopus 로고    scopus 로고
    • Substrate specificity characterization of recombinant metallo oligo-peptidases thimet oligopeptidase and neurolysin
    • Oliveira V., Campos M., Melo R.L., Ferro E.S., Camargo A.C., Juliano M.A., Juliano L. Substrate specificity characterization of recombinant metallo oligo-peptidases thimet oligopeptidase and neurolysin. Biochemistry. 40:2001;4417-4425.
    • (2001) Biochemistry , vol.40 , pp. 4417-4425
    • Oliveira, V.1    Campos, M.2    Melo, R.L.3    Ferro, E.S.4    Camargo, A.C.5    Juliano, M.A.6    Juliano, L.7
  • 19
    • 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., Roberts J.L. Molecular cloning and primary structure of rat testes metalloendopeptidase EC 3.4.24.15. Biochemistry. 29:1990;10323-10329.
    • (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
  • 20
    • 0024405419 scopus 로고
    • A Rapid enzyme immunoassay for cholecystokinin octapeptide sulfate
    • Takeda K., Uchiumi F., Takita M., Kato T. A Rapid enzyme immunoassay for cholecystokinin octapeptide sulfate. Neurochem. Int. 15:1989;55-60.
    • (1989) Neurochem. Int. , vol.15 , pp. 55-60
    • Takeda, K.1    Uchiumi, F.2    Takita, M.3    Kato, T.4
  • 23
    • 0028094858 scopus 로고
    • A rapid anterograde axonal transport of carboxypeptidase H in rat sciatic nerves
    • Yajima R., Chikuma T., Kato T. A rapid anterograde axonal transport of carboxypeptidase H in rat sciatic nerves. J. Neurochem. 63:1994;997-1002.
    • (1994) J. Neurochem. , vol.63 , pp. 997-1002
    • Yajima, R.1    Chikuma, T.2    Kato, T.3
  • 25
    • 0033603328 scopus 로고    scopus 로고
    • Metalloendopeptidase EC 3.4.24.15 is necessary for Alzheimer's amyloid-beta peptide degradation
    • Yamin R., Malgeri E.G., Sloane J.A., McGraw W.T., Abraham C.R. Metalloendopeptidase EC 3.4.24.15 is necessary for Alzheimer's amyloid-beta peptide degradation. J. Biol. Chem. 274:1999;18777-18784.
    • (1999) J. Biol. Chem. , vol.274 , pp. 18777-18784
    • Yamin, R.1    Malgeri, E.G.2    Sloane, J.A.3    McGraw, W.T.4    Abraham, C.R.5
  • 26
    • 0031723472 scopus 로고    scopus 로고
    • Enzymatic degradation of luteinizing hormone releasing hormone (LHRH)/[D-Ala6]-LHRH in lung pneumocytes
    • Yang X., Rojanasakul Y., Wang L., Ma J.Y., Ma J.K. Enzymatic degradation of luteinizing hormone releasing hormone (LHRH)/[D-Ala6]-LHRH in lung pneumocytes. Pharm. Res. 15:1998;1480-1484.
    • (1998) Pharm. Res. , vol.15 , pp. 1480-1484
    • Yang, X.1    Rojanasakul, Y.2    Wang, L.3    Ma, J.Y.4    Ma, J.K.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.