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Volumn 125, Issue 3, 1999, Pages 641-647

Dynorphin A processing enzyme: Tissue distribution, isolation, and characterization

Author keywords

Enkephalin; Metalloprotease; Neuropeptide; Proprotein convertase

Indexed keywords

CHELATING AGENT; DYNORPHIN A; ENDORPHIN; MEMBRANE METALLOENDOPEPTIDASE; METALLOPROTEINASE; PRODYNORPHIN; THIOL; TRITON X 100;

EID: 0032934832     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a022331     Document Type: Article
Times cited : (14)

References (37)
  • 1
    • 0020008342 scopus 로고
    • Post-translational proteolysis in polypeptide hormone biosynthesis
    • Docherty, K. and Steiner, D.F. (1982) Post-translational proteolysis in polypeptide hormone biosynthesis. Annu. Rev. Physiol. 44, 625-638
    • (1982) Annu. Rev. Physiol. , vol.44 , pp. 625-638
    • Docherty, K.1    Steiner, D.F.2
  • 3
    • 0004354257 scopus 로고
    • The biosynthesis of biologically active peptides: A perspective
    • Fricker, L.D., ed., CRC Press, Boca Raton, FL
    • Steiner, D.F. (1991) The biosynthesis of biologically active peptides: A perspective in Peptide Biosynthesis and Processing (Fricker, L.D., ed.) pp. 1-16, CRC Press, Boca Raton, FL
    • (1991) Peptide Biosynthesis and Processing , pp. 1-16
    • Steiner, D.F.1
  • 4
    • 0027965348 scopus 로고
    • The family of subtilisin/kexin like pro-protein and pro-hormone convertases: Divergent or shared functions
    • Seidah, N.G., Chretien, M., and Day, R. (1994) The family of subtilisin/kexin like pro-protein and pro-hormone convertases: divergent or shared functions. Biochimie 76, 197-209
    • (1994) Biochimie , vol.76 , pp. 197-209
    • Seidah, N.G.1    Chretien, M.2    Day, R.3
  • 5
    • 0026029553 scopus 로고
    • Consensus sequence for processing of peptide precursors at monobasic sites
    • Devi, L.A. (1991) Consensus sequence for processing of peptide precursors at monobasic sites. FEBS Lett. 280, 189-194
    • (1991) FEBS Lett. , vol.280 , pp. 189-194
    • Devi, L.A.1
  • 6
    • 0345234316 scopus 로고
    • Enzymes involved in the synthesis of opioid peptides
    • Tseng, L.F., ed., Harwood Academic Press, Amsterdam
    • Fricker, L.D. and Devi, L. (1995) Enzymes involved in the synthesis of opioid peptides in Pharmacology of Opioid Peptides (Tseng, L.F., ed.) pp. 87-107, Harwood Academic Press, Amsterdam
    • (1995) Pharmacology of Opioid Peptides , pp. 87-107
    • Fricker, L.D.1    Devi, L.2
  • 7
    • 0028674393 scopus 로고
    • Pro-protein convertases of subtilisin/kexin family
    • Seidah, N.G. and Chretien, M. (1994) Pro-protein convertases of subtilisin/kexin family. Methods Enzymol. 244, 175-188
    • (1994) Methods Enzymol. , vol.244 , pp. 175-188
    • Seidah, N.G.1    Chretien, M.2
  • 8
    • 0028786585 scopus 로고
    • Purification and characterization of a dynorphin processing endoprotease
    • Berman, Y.L., Juliano, L., and Devi, L.A. (1995) Purification and characterization of a dynorphin processing endoprotease. J. Biol. Chem. 270, 23845-23850
    • (1995) J. Biol. Chem. , vol.270 , pp. 23845-23850
    • Berman, Y.L.1    Juliano, L.2    Devi, L.A.3
  • 9
    • 0027930260 scopus 로고
    • Characterization of a metalloprotease from ovine chromaffin granules which cleaves a proenkephalin fragment (BAM12P) at a single arginine residue
    • Tezapsidis, N. and Parish, D.C. (1994) Characterization of a metalloprotease from ovine chromaffin granules which cleaves a proenkephalin fragment (BAM12P) at a single arginine residue. Biochem. J. 301, 607-614
    • (1994) Biochem. J. , vol.301 , pp. 607-614
    • Tezapsidis, N.1    Parish, D.C.2
  • 10
    • 0021772781 scopus 로고
    • A putative processing enzyme from Aplysia that cleaves dynorphin A at the single arginine residue
    • Wallace, E.F., Weber, E., Barchas, J.D., and Evans, C.J. (1984) A putative processing enzyme from Aplysia that cleaves dynorphin A at the single arginine residue. Biochem. Biophys. Res. Commun. 119, 415-422
    • (1984) Biochem. Biophys. Res. Commun. , vol.119 , pp. 415-422
    • Wallace, E.F.1    Weber, E.2    Barchas, J.D.3    Evans, C.J.4
  • 11
    • 0031985151 scopus 로고    scopus 로고
    • Prodynorphin processing by proprotein convertase 2. Cleavage at single basic residues and enhanced processing in the presence of carboxypeptidase activity
    • Day, R., Lazure, C., Basak, A., Boudreault, A.P. Limperis, P., Dong, W., and Lindberg, I. (1998) Prodynorphin processing by proprotein convertase 2. Cleavage at single basic residues and enhanced processing in the presence of carboxypeptidase activity. J. Biol. Chem. 273, 829-836
    • (1998) J. Biol. Chem. , vol.273 , pp. 829-836
    • Day, R.1    Lazure, C.2    Basak, A.3    Boudreault, A.P.4    Limperis, P.5    Dong, W.6    Lindberg, I.7
  • 12
    • 0007959774 scopus 로고    scopus 로고
    • Monobasic processing specificity of dynorphin converting enzyme, furin, prohormone convertase 1 and prohormone convertase 2
    • Berman, Y., Juliano, L., Beavis, R., and Devi, L.A. (1998) Monobasic processing specificity of dynorphin converting enzyme, furin, prohormone convertase 1 and prohormone convertase 2. Soc. Neurosci. Abs. 23, 2317
    • (1998) Soc. Neurosci. Abs. , vol.23 , pp. 2317
    • Berman, Y.1    Juliano, L.2    Beavis, R.3    Devi, L.A.4
  • 13
    • 0021026058 scopus 로고
    • Regional distribution of dynorphin and neo-endorphin peptides in rat brain, spinal cord, and pituitary
    • Cone, R.I., Weber, E., Barchas, J.D., and Goldstein, A. (1983) Regional distribution of dynorphin and neo-endorphin peptides in rat brain, spinal cord, and pituitary. J. Neurosci. 3, 2146-2153
    • (1983) J. Neurosci. , vol.3 , pp. 2146-2153
    • Cone, R.I.1    Weber, E.2    Barchas, J.D.3    Goldstein, A.4
  • 14
    • 0023404762 scopus 로고
    • Distribution pattern of metorphamide compared with other opioid peptides from proenkephalin and prodynorphin in the bovine brain
    • Sonders, M. and Weber, E. (1987) Distribution pattern of metorphamide compared with other opioid peptides from proenkephalin and prodynorphin in the bovine brain. J. Neurochem. 49, 671-680
    • (1987) J. Neurochem. , vol.49 , pp. 671-680
    • Sonders, M.1    Weber, E.2
  • 15
    • 0026015656 scopus 로고
    • Subcellular localization, partial purification, and characterization of a dynorphin processing endopeptidase from bovine pituitary
    • Devi, L., Gupta, P., and Fricker, L.D. (1991) Subcellular localization, partial purification, and characterization of a dynorphin processing endopeptidase from bovine pituitary. J. Neurochem. 56, 320-329
    • (1991) J. Neurochem. , vol.56 , pp. 320-329
    • Devi, L.1    Gupta, P.2    Fricker, L.D.3
  • 16
    • 0019961953 scopus 로고
    • Predominance of the amino-terminal octapeptide fragment of dynorphin in rat brain regions
    • Weber, E., Evans, C.J., and Barchas, J.D. (1982) Predominance of the amino-terminal octapeptide fragment of dynorphin in rat brain regions. Nature 299, 77-79
    • (1982) Nature , vol.299 , pp. 77-79
    • Weber, E.1    Evans, C.J.2    Barchas, J.D.3
  • 17
    • 0004877840 scopus 로고
    • Studies on the redox state in polyacrylamide gels
    • Dirksen, M.L. and Chrambach, A. (1972) Studies on the redox state in polyacrylamide gels. Separation Sci. 7, 747-772
    • (1972) Separation Sci. , vol.7 , pp. 747-772
    • Dirksen, M.L.1    Chrambach, A.2
  • 18
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 19
    • 0020824984 scopus 로고
    • A soluble metalloendopeptidase from rat brain; purification of the enzyme and determination of specificity with synthetic and natural peptides
    • Orlowski, M., Michaud, C., and Chu, T.G. (1983) A soluble metalloendopeptidase from rat brain; purification of the enzyme and determination of specificity with synthetic and natural peptides. Eur. J. Biochem. 135, 81-88
    • (1983) Eur. J. Biochem. , vol.135 , pp. 81-88
    • Orlowski, M.1    Michaud, C.2    Chu, T.G.3
  • 20
    • 0028897489 scopus 로고
    • Characterization of a mitochondrial metallopeptidase reveals neurolysin as a homologue of thimet oligopeptidase
    • Serizawa, A., Dandom, P.M., and Barrett, A.J. (1995) Characterization of a mitochondrial metallopeptidase reveals neurolysin as a homologue of thimet oligopeptidase. J. Biol. Chem. 270, 2092-2098
    • (1995) J. Biol. Chem. , vol.270 , pp. 2092-2098
    • Serizawa, A.1    Dandom, P.M.2    Barrett, A.J.3
  • 21
    • 0021007899 scopus 로고
    • Purification of endopeptidase-24.11 ('enkephalinase') from pig brain by immunoadsorbent chromatography
    • Relton, J.M., Gee, N.S., Matsas, R., Turner, A.J., and Kenny, A.J. (1983) Purification of endopeptidase-24.11 ('enkephalinase') from pig brain by immunoadsorbent chromatography. Biochem. J. 215, 519-523
    • (1983) Biochem. J. , vol.215 , pp. 519-523
    • Relton, J.M.1    Gee, N.S.2    Matsas, R.3    Turner, A.J.4    Kenny, A.J.5
  • 22
    • 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., Pierottin, A.R., Barre, N., Creminon, 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, 2056-2061
    • (1994) J. Biol. Chem. , vol.269 , pp. 2056-2061
    • Chesneau, V.1    Pierottin, A.R.2    Barre, N.3    Creminon, C.4    Tougard, C.5    Cohen, P.6
  • 25
    • 0026785317 scopus 로고
    • Characterization of dynorphin A-converting enzyme in human spinal cord
    • Silberring, J., Castello, M.E., and Nyberg, F. (1992) Characterization of dynorphin A-converting enzyme in human spinal cord. J. Biol. Chem. 267, 21324-21328
    • (1992) J. Biol. Chem. , vol.267 , pp. 21324-21328
    • Silberring, J.1    Castello, M.E.2    Nyberg, F.3
  • 26
    • 0026697367 scopus 로고
    • Characterization of a cholecystokinin 8-generating endoprotease purified from rat brain synaptosomes
    • Viereck, J.C. and Beinfeld, M.C. (1992) Characterization of a cholecystokinin 8-generating endoprotease purified from rat brain synaptosomes. J. Biol. Chem. 267, 19475-19482
    • (1992) J. Biol. Chem. , vol.267 , pp. 19475-19482
    • Viereck, J.C.1    Beinfeld, M.C.2
  • 27
    • 0025997564 scopus 로고
    • Identification of a somatostatin 14-generating propeptide converting enzyme as a member of the kex2/furin/PC family
    • Mackin, R.B., Noe, B.D., and Spiess, J. (1991) Identification of a somatostatin 14-generating propeptide converting enzyme as a member of the kex2/furin/PC family. Endocrinology 129, 2263-2265
    • (1991) Endocrinology , vol.129 , pp. 2263-2265
    • Mackin, R.B.1    Noe, B.D.2    Spiess, J.3
  • 28
    • 0023935001 scopus 로고
    • Atrial granules contain an amino-terminal processing enzyme of atrial natriuretic factor
    • Wypij, D.M. and Harris, R.B. (1988) Atrial granules contain an amino-terminal processing enzyme of atrial natriuretic factor. J. Biol. Chem. 263, 7079-7086
    • (1988) J. Biol. Chem. , vol.263 , pp. 7079-7086
    • Wypij, D.M.1    Harris, R.B.2
  • 29
    • 0026750606 scopus 로고
    • Prohormone thiol protease and enkephalin precursor processing: Cleavage at dibasic and monobasic sites
    • Krieger, T.J. and Hook, V.Y.H. (1992) Prohormone thiol protease and enkephalin precursor processing: cleavage at dibasic and monobasic sites. J. Neurochem. 59, 26-31
    • (1992) J. Neurochem. , vol.59 , pp. 26-31
    • Krieger, T.J.1    Hook, V.Y.H.2
  • 30
    • 0026742960 scopus 로고
    • Purification and characterization of furin, a Kex2-like processing endoprotease, produced in Chinese hamster ovary cells
    • Hatsuzawa, K., Nagahama, M., Takahashi, S., Takada, K., Murakami, K., and Barr, P.J. (1992) Purification and characterization of furin, a Kex2-like processing endoprotease, produced in Chinese hamster ovary cells. J. Biol. Chem. 267, 16094-16099
    • (1992) J. Biol. Chem. , vol.267 , pp. 16094-16099
    • Hatsuzawa, K.1    Nagahama, M.2    Takahashi, S.3    Takada, K.4    Murakami, K.5    Barr, P.J.6
  • 31
    • 0027268151 scopus 로고
    • Enzymic characterization of murine and human prohormone convertase-1 (mPC1 and hPC1) expressed in mammalian GH4C1 cells
    • Jean, F., Basak, A., Rondeau, N., Benjannet, S., Hendy, G., and Seidah, N.G. (1993) Enzymic characterization of murine and human prohormone convertase-1 (mPC1 and hPC1) expressed in mammalian GH4C1 cells. Biochem. J. 292, 891-900
    • (1993) Biochem. J. , vol.292 , pp. 891-900
    • Jean, F.1    Basak, A.2    Rondeau, N.3    Benjannet, S.4    Hendy, G.5    Seidah, N.G.6
  • 32
    • 0027460523 scopus 로고
    • Purification and characterization of the prohormone convertase PC1
    • Zhou, Y. and Lindberg, I. (1993) Purification and characterization of the prohormone convertase PC1. J. Biol. Chem. 268, 5615-5623
    • (1993) J. Biol. Chem. , vol.268 , pp. 5615-5623
    • Zhou, Y.1    Lindberg, I.2
  • 33
    • 0002799850 scopus 로고
    • Angiotensin I converting enzyme and its role in neuropeptide metabolism
    • Turner, A.J., ed., Eliss Horwood, Chichester, England
    • Skidgel, R.A., Defendini, R., and Erdos, E.G. (1987) Angiotensin I converting enzyme and its role in neuropeptide metabolism in Neuropeptides and Their Peptidases (Turner, A.J., ed.) pp. 165-182, Eliss Horwood, Chichester, England
    • (1987) Neuropeptides and Their Peptidases , pp. 165-182
    • Skidgel, R.A.1    Defendini, R.2    Erdos, E.G.3
  • 35
    • 0342726574 scopus 로고    scopus 로고
    • Structure-activity relationship studies on the novel neuropeptide orphanin FQ
    • Reinscheild, R.K., Ardati, A., Monsma, F.J., and Civelli, O. (1996) Structure-activity relationship studies on the novel neuropeptide orphanin FQ. J. Biol. Chem. 271, 14163-14168
    • (1996) J. Biol. Chem. , vol.271 , pp. 14163-14168
    • Reinscheild, R.K.1    Ardati, A.2    Monsma, F.J.3    Civelli, O.4
  • 36
    • 0017102431 scopus 로고
    • Angiotensin-converting enzyme and the regulation of vasoactive peptides
    • Soffer, R.L. (1976) Angiotensin-converting enzyme and the regulation of vasoactive peptides. Annu. Rev. Biochem. 45, 73-94
    • (1976) Annu. Rev. Biochem. , vol.45 , pp. 73-94
    • Soffer, R.L.1
  • 37
    • 0015139369 scopus 로고
    • Concentrations of angiotensin-converting enzyme in tissues of the rat
    • Cushman, D.W. and Cheung, H.S. (1971) Concentrations of angiotensin-converting enzyme in tissues of the rat. Biophys. Biophys. Biochim. Acta 250, 261-265
    • (1971) Biophys. Biophys. Biochim. Acta , vol.250 , pp. 261-265
    • Cushman, D.W.1    Cheung, H.S.2


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