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Volumn 261, Issue 2, 1999, Pages 421-429

N-benzoyl-L-tyrosyl-p-aminobenzoic acid hydrolase β (human meprinβ): A 13-amino-acid sequence is required for proteolytic processing and subsequent secretion

Author keywords

Astacin family; Human meprin; Intracellular transport; N benzoyl L tyrosyl p aminobenzoic acid hydrolase; Proteolytic processing

Indexed keywords

BREFELDIN A; MEPRIN; PEPTIDE FRAGMENT;

EID: 0013043261     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1999.00268.x     Document Type: Article
Times cited : (15)

References (52)
  • 1
    • 0023677695 scopus 로고
    • Biosynthesis of N-benzoyl-L-tyrosyl-p-aminobenzoic acid hydrolase: Disulfide-linked dimers are formed at the site of synthesis in the rough endoplasmic reticulum
    • 1. Sterchi, E.E., Naim, H.Y. & Lentze, M.J. (1988) Biosynthesis of N-benzoyl-L-tyrosyl-p-aminobenzoic acid hydrolase: disulfide-linked dimers are formed at the site of synthesis in the rough endoplasmic reticulum. Arch. Biochem. Biophys. 265, 119-127.
    • (1988) Arch. Biochem. Biophys. , vol.265 , pp. 119-127
    • Sterchi, E.E.1    Naim, H.Y.2    Lentze, M.J.3
  • 2
    • 0023688437 scopus 로고
    • N-benzoyl-L-tyrosyl-p-aminobenzoic acid hydrolase: A metalloendopeptidase of the human intestinal microvillus membrane which degrades biologically active peptides
    • 2. Sterchi, E.E., Naim, H.Y., Lentze, M.J., Hauri, H.P. & Fransen, J.A. (1988) N-benzoyl-L-tyrosyl-p-aminobenzoic acid hydrolase: a metalloendopeptidase of the human intestinal microvillus membrane which degrades biologically active peptides. Arch. Biochem. Biophys. 265, 105-118.
    • (1988) Arch. Biochem. Biophys. , vol.265 , pp. 105-118
    • Sterchi, E.E.1    Naim, H.Y.2    Lentze, M.J.3    Hauri, H.P.4    Fransen, J.A.5
  • 3
    • 0020032479 scopus 로고
    • Non-pancreatic hydrolysis of N-benzoyl-L-tyrosyl-p-aminobenzoic acid (PABA-peptide) in the human small intestine
    • 3. Sterchi, E.E., Green, J.R. & Lentze, M.J. (1982) Non-pancreatic hydrolysis of N-benzoyl-L-tyrosyl-p-aminobenzoic acid (PABA-peptide) in the human small intestine. Clin. Sci. 62, 557-560.
    • (1982) Clin. Sci. , vol.62 , pp. 557-560
    • Sterchi, E.E.1    Green, J.R.2    Lentze, M.J.3
  • 4
    • 0020619468 scopus 로고
    • Nonpancreatic hydrolysis of N-benzoyl-L-tyrosyl-p-aminobenzoic acid (PABA peptide) in the rat small intestine
    • 4. Sterchi, E.E., Green, J.R. & Lentze, M.J. (1983) Nonpancreatic hydrolysis of N-benzoyl-L-tyrosyl-p-aminobenzoic acid (PABA peptide) in the rat small intestine. J. Pediatr Gastroenterol. Nutr. 2, 539-547.
    • (1983) J. Pediatr Gastroenterol. Nutr. , vol.2 , pp. 539-547
    • Sterchi, E.E.1    Green, J.R.2    Lentze, M.J.3
  • 5
    • 0023131106 scopus 로고
    • Characterization of meprin, a membrane-bound metalloendopeptidase from mouse kidney
    • 5. Butler, P.E., McKay, M.J. & Bond, J.S. (1987) Characterization of meprin, a membrane-bound metalloendopeptidase from mouse kidney. Biochem. J. 241, 229-235.
    • (1987) Biochem. J. , vol.241 , pp. 229-235
    • Butler, P.E.1    McKay, M.J.2    Bond, J.S.3
  • 6
    • 0027934376 scopus 로고
    • An old enzyme with a new function: Purification and characterization of a distinct matrix-degrading metalloproteinase in rat kidney cortex and its identification as meprin
    • 6. Kaushal, G.P., Walker, P.D. & Shah, S.V. (1994) An old enzyme with a new function: purification and characterization of a distinct matrix-degrading metalloproteinase in rat kidney cortex and its identification as meprin. J. Cell Biol. 126, 1319-1327.
    • (1994) J. Cell Biol. , vol.126 , pp. 1319-1327
    • Kaushal, G.P.1    Walker, P.D.2    Shah, S.V.3
  • 7
    • 0023655460 scopus 로고
    • Proteins of the kidney microvillar membrane. Purification and properties of the phosphoramidon-insensitive endopeptidase ('endopeptidase-2') from rat kidney
    • 7. Kenny, A.J. & Ingram, J. (1987) Proteins of the kidney microvillar membrane. Purification and properties of the phosphoramidon-insensitive endopeptidase ('endopeptidase-2') from rat kidney. Biochem. J. 245, 515-524.
    • (1987) Biochem. J. , vol.245 , pp. 515-524
    • Kenny, A.J.1    Ingram, J.2
  • 8
    • 0023153985 scopus 로고
    • Metabolism of neuropeptides. Hydrolysis of the angiotensins, bradykinin, substance P and oxytocin by pig kidney microvillar membranes
    • 8. Stephenson, S.L. & Kenny, A.J. (1987) Metabolism of neuropeptides. Hydrolysis of the angiotensins, bradykinin, substance P and oxytocin by pig kidney microvillar membranes. Biochem. J. 241, 237-247.
    • (1987) Biochem. J. , vol.241 , pp. 237-247
    • Stephenson, S.L.1    Kenny, A.J.2
  • 9
    • 0025572436 scopus 로고
    • Phe5 (4-nitro)-bradykinin: A chromogenic substrate for assay and kinetics of the metalloendopeptidase meprin
    • 9. Wolz, R.L. & Bond, J.S. (1990) Phe5 (4-nitro)-bradykinin: a chromogenic substrate for assay and kinetics of the metalloendopeptidase meprin. Anal Biochem. 191, 314-320.
    • (1990) Anal Biochem. , vol.191 , pp. 314-320
    • Wolz, R.L.1    Bond, J.S.2
  • 10
    • 0026077289 scopus 로고
    • Mapping the active site of meprin-A with peptide substrates and inhibitors
    • 10. Wolz, R.L., Harris, R.B. & Bond, J.S. (1991) Mapping the active site of meprin-A with peptide substrates and inhibitors. Biochemistry 30, 8488-8493.
    • (1991) Biochemistry , vol.30 , pp. 8488-8493
    • Wolz, R.L.1    Harris, R.B.2    Bond, J.S.3
  • 11
    • 0028352165 scopus 로고
    • A kinetic comparison of the homologous proteases astacin and meprin A
    • 11. Wolz, R.L. (1994) A kinetic comparison of the homologous proteases astacin and meprin A. Arch. Biochem. Biophys. 310, 144-151.
    • (1994) Arch. Biochem. Biophys. , vol.310 , pp. 144-151
    • Wolz, R.L.1
  • 12
    • 0027941838 scopus 로고
    • Families of zinc metalloproteases
    • 12. Hooper, N.M. (1994) Families of zinc metalloproteases. FEBS Lett. 354, 1-6.
    • (1994) FEBS Lett. , vol.354 , pp. 1-6
    • Hooper, N.M.1
  • 13
    • 0028969678 scopus 로고
    • The metzincins - Topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a superfamily of zinc-peptidases
    • 13. Stocker, W., Grams, F., Baumann, U., Reinemer, P., Gomis-Ruth, F.X., McKay, D.B. & Bode, W. (1995) The metzincins - topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a superfamily of zinc-peptidases. Protein Sci. 4, 823-840.
    • (1995) Protein Sci. , vol.4 , pp. 823-840
    • Stocker, W.1    Grams, F.2    Baumann, U.3    Reinemer, P.4    Gomis-Ruth, F.X.5    McKay, D.B.6    Bode, W.7
  • 14
    • 0029016839 scopus 로고
    • The astacin family of metalloendopeptidases
    • 14. Bond, J.S. & Beynon, R.J. (1995) The astacin family of metalloendopeptidases. Protein Sci. 4, 1247-1261.
    • (1995) Protein Sci. , vol.4 , pp. 1247-1261
    • Bond, J.S.1    Beynon, R.J.2
  • 16
    • 0026697681 scopus 로고
    • Isolation of cDNAs for LCE and HCE, two constituent proteases of the hatching enzyme of Oryzias latipes, and concurrent expression of their mRNAs during development
    • 16. Yasumasu, S., Yamada, K., Akasaka, K., Mitsunaga, K., Iuchi, I., Shimada, H. & Yamagami, K. (1992) Isolation of cDNAs for LCE and HCE, two constituent proteases of the hatching enzyme of Oryzias latipes, and concurrent expression of their mRNAs during development. Dev. Biol. 153, 250-258.
    • (1992) Dev. Biol. , vol.153 , pp. 250-258
    • Yasumasu, S.1    Yamada, K.2    Akasaka, K.3    Mitsunaga, K.4    Iuchi, I.5    Shimada, H.6    Yamagami, K.7
  • 18
    • 0025096627 scopus 로고
    • Molecular approach to dorsoanterior development in Xenopus laevis
    • 18. Sato, S.M. & Sargent, T.D. (1990) Molecular approach to dorsoanterior development in Xenopus laevis. Dev. Biol. 137, 135-141.
    • (1990) Dev. Biol. , vol.137 , pp. 135-141
    • Sato, S.M.1    Sargent, T.D.2
  • 19
    • 0025986820 scopus 로고
    • The Drosophila dorsal-ventral patterning gene tolloid is related to human bone morphogenetic protein 1
    • 19. Shimell, M.J., Ferguson, E.L., Childs, S.R. & O'Connor, M.B. (1991) The Drosophila dorsal-ventral patterning gene tolloid is related to human bone morphogenetic protein 1. Cell 67, 469-481.
    • (1991) Cell , vol.67 , pp. 469-481
    • Shimell, M.J.1    Ferguson, E.L.2    Childs, S.R.3    O'Connor, M.B.4
  • 20
    • 0026536983 scopus 로고
    • Spatial and temporal expression pattern during sea urchin embryogenesis of a gene coding for a protease homologous to the human protein BMP-1 and to the product of the Drosophila dorsal-ventral patterning gene tolloid
    • 20. Lepage, T., Ghiglione, C. & Gache, C. (1992) Spatial and temporal expression pattern during sea urchin embryogenesis of a gene coding for a protease homologous to the human protein BMP-1 and to the product of the Drosophila dorsal-ventral patterning gene tolloid. Development 114, 147-163.
    • (1992) Development , vol.114 , pp. 147-163
    • Lepage, T.1    Ghiglione, C.2    Gache, C.3
  • 21
    • 0026603920 scopus 로고
    • Early mRNAs, spatially restricted along the animal-vegetal axis of sea urchin embryos, include one encoding a protein related to tolloid BMP-1
    • 21. Reynolds, S.D., Angerer, L.M., Palis, J., Nasir, A. & Angerer, R.C. (1992) Early mRNAs, spatially restricted along the animal-vegetal axis of sea urchin embryos, include one encoding a protein related to tolloid BMP-1. Development 114, 769-786.
    • (1992) Development , vol.114 , pp. 769-786
    • Reynolds, S.D.1    Angerer, L.M.2    Palis, J.3    Nasir, A.4    Angerer, R.C.5
  • 22
    • 0028990388 scopus 로고
    • A 25.7 × 10(3) M(r) hydra metalloproteinase (HMP1), a member of the astacin family, localizes to the extracellular matrix of Hydra vulgaris in a head-specific manner and has a developmental function
    • 22. Yan, L., Pollock, G.H., Nagase, H. & Sarras, M.P.J. (1995) A 25.7 × 10(3) M(r) hydra metalloproteinase (HMP1), a member of the astacin family, localizes to the extracellular matrix of Hydra vulgaris in a head-specific manner and has a developmental function. Development 121, 1591-1602.
    • (1995) Development , vol.121 , pp. 1591-1602
    • Yan, L.1    Pollock, G.H.2    Nagase, H.3    Sarras, M.P.J.4
  • 23
    • 27244461848 scopus 로고
    • A new member to the astacin family of metalloendopeptidases: A novel 1,25-dihydroxyvitamin D-3-stimulated mRNA from chorioallantoic membrane of quail
    • 23. Elaroussi, M.A. & DeLuca, H.F. (1994) A new member to the astacin family of metalloendopeptidases: a novel 1,25-dihydroxyvitamin D-3-stimulated mRNA from chorioallantoic membrane of quail. Biochim. Biophys. Acta 1217, 1-8.
    • (1994) Biochim. Biophys. Acta , vol.1217 , pp. 1-8
    • Elaroussi, M.A.1    Deluca, H.F.2
  • 24
    • 0027193209 scopus 로고
    • An adhesive domain detected in functionally diverse receptors
    • 24. Beckmann, G. & Bork, P. (1993) An adhesive domain detected in functionally diverse receptors. Trends Biochem. Sci. 18, 40-41.
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 40-41
    • Beckmann, G.1    Bork, P.2
  • 25
    • 0030200109 scopus 로고    scopus 로고
    • TRAF proteins and meprins share a conserved domain
    • 25. Uren, A.G. & Vaux, D.L. (1996) TRAF proteins and meprins share a conserved domain. Trends Biochem. Sci. 21, 244-245.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 244-245
    • Uren, A.G.1    Vaux, D.L.2
  • 26
    • 0030789739 scopus 로고    scopus 로고
    • Polarised expression of human intestinal N-benzoyl-L-tyrosyl-p-aminobenzoic acid hydrolase (human meprin) alpha and beta subunits in Madin-Darby canine kidney cells
    • 26. Eldering, J.A., Grunberg, J., Hahn, D., Croes, H.J., Fransen, J.A. & Sterchi, E.E. (1997) Polarised expression of human intestinal N-benzoyl-L-tyrosyl-p-aminobenzoic acid hydrolase (human meprin) alpha and beta subunits in Madin-Darby canine kidney cells. Eur. J. Biochem. 247, 920-932.
    • (1997) Eur. J. Biochem. , vol.247 , pp. 920-932
    • Eldering, J.A.1    Grunberg, J.2    Hahn, D.3    Croes, H.J.4    Fransen, J.A.5    Sterchi, E.E.6
  • 27
    • 0027360581 scopus 로고
    • Cloning of the PABA peptide hydrolase alpha subunit (PPH alpha) from human small intestine and its expression in COS-1 cells
    • 27. Dumermuth, E., Eldering, J.A., Grunberg, J., Jiang, W. & Sterchi, E.E. (1993) Cloning of the PABA peptide hydrolase alpha subunit (PPH alpha) from human small intestine and its expression in COS-1 cells. FEBS Lett. 335, 367-375.
    • (1993) FEBS Lett. , vol.335 , pp. 367-375
    • Dumermuth, E.1    Eldering, J.A.2    Grunberg, J.3    Jiang, W.4    Sterchi, E.E.5
  • 28
    • 0027361420 scopus 로고
    • Expression of the alpha subunit of PABA peptide hydrolase (EC3.4.24.18) in MDCK cells. Synthesis and secretion of an enzymatically inactive homodimer
    • 28. Grunberg, J., Dumermuth, E., Eldering, J.A. & Sterchi, E.E. (1993) Expression of the alpha subunit of PABA peptide hydrolase (EC3.4.24.18) in MDCK cells. Synthesis and secretion of an enzymatically inactive homodimer. FEBS Lett. 335, 376-379.
    • (1993) FEBS Lett. , vol.335 , pp. 376-379
    • Grunberg, J.1    Dumermuth, E.2    Eldering, J.A.3    Sterchi, E.E.4
  • 29
    • 0027504487 scopus 로고
    • Rat endopeptidase-24.18 alpha subunit is secreted into the culture medium as a zymogen when expressed by COS-1 cells
    • 29. Corbeil, D., Milhiet, P.E., Simon, V., Ingram, J., Kenny, A.J., Boileau, G. & Crine, P. (1993) Rat endopeptidase-24.18 alpha subunit is secreted into the culture medium as a zymogen when expressed by COS-1 cells. FEBS Lett. 335, 361-366.
    • (1993) FEBS Lett. , vol.335 , pp. 361-366
    • Corbeil, D.1    Milhiet, P.E.2    Simon, V.3    Ingram, J.4    Kenny, A.J.5    Boileau, G.6    Crine, P.7
  • 31
    • 0023470609 scopus 로고
    • Distribution of meprin in kidneys from mice with high-and low-meprin activity
    • 31. Craig, S.S., Reckelhoff, J.F. & Bond, J.S. (1987) Distribution of meprin in kidneys from mice with high-and low-meprin activity. Am. J. Physiol. 253, C535-C540.
    • (1987) Am. J. Physiol. , vol.253
    • Craig, S.S.1    Reckelhoff, J.F.2    Bond, J.S.3
  • 32
    • 0028237463 scopus 로고
    • Membrane association and oligomeric organization of the alpha and beta subunits of mouse meprin A
    • 32. Marchand, P., Tang, J. & Bond, J.S. (1994) Membrane association and oligomeric organization of the alpha and beta subunits of mouse meprin A. J. Biol. Chem. 269, 15388-15393.
    • (1994) J. Biol. Chem. , vol.269 , pp. 15388-15393
    • Marchand, P.1    Tang, J.2    Bond, J.S.3
  • 33
    • 0001082248 scopus 로고    scopus 로고
    • Secretion of human meprin from intestinal epithelial cells depends on differential expression of the α and β subunits
    • 33. Lottaz, D., Hahn, D., Müller, S., Müller, Ch. & Sterchi, E.E. (1999) Secretion of human meprin from intestinal epithelial cells depends on differential expression of the α and β subunits. Eur J Biochem. 259, 496-504.
    • (1999) Eur J Biochem. , vol.259 , pp. 496-504
    • Lottaz, D.1    Hahn, D.2    Müller, S.3    Müller, Ch.4    Sterchi, E.E.5
  • 35
    • 0001823786 scopus 로고
    • Recombinant PCR
    • (Innis, M.A., Gelfand, D.H., Sninsky, J.J. & White, T.J., eds), Academic Press, San Diego, CA
    • 35. Higuchi, R. (1990) Recombinant PCR. A Guide to Methods and Applications (Innis, M.A., Gelfand, D.H., Sninsky, J.J. & White, T.J., eds), pp. 177-183. Academic Press, San Diego, CA.
    • (1990) A Guide to Methods and Applications , pp. 177-183
    • Higuchi, R.1
  • 36
    • 0023073231 scopus 로고
    • Preparation of cDNA and the generation of cDNA libraries: Overview
    • 36. Kimmel, A.R. & Berger, S.L. (1987) Preparation of cDNA and the generation of cDNA libraries: overview. Meth Enzymol. 152, 307-316.
    • (1987) Meth Enzymol. , vol.152 , pp. 307-316
    • Kimmel, A.R.1    Berger, S.L.2
  • 37
    • 0026451052 scopus 로고
    • Maturation of human lactase-phlorizin hydrolase. Proteolytic cleavage of precursor occurs after passage through the Golgi complex
    • 37. Lottaz, D., Oberholzer, T., Bahler, P., Semenza, G. & Sterchi, E.E. (1992) Maturation of human lactase-phlorizin hydrolase. Proteolytic cleavage of precursor occurs after passage through the Golgi complex. FEBS Lett. 313, 270-276.
    • (1992) FEBS Lett. , vol.313 , pp. 270-276
    • Lottaz, D.1    Oberholzer, T.2    Bahler, P.3    Semenza, G.4    Sterchi, E.E.5
  • 38
    • 0030839259 scopus 로고    scopus 로고
    • C-cytosolic and transmembrane domains of the N-benzoyl-L-tyrosyl-p-aminobenzoic acid hydrolase alpha subunit (human meprin alpha) are essential for its retention in the endoplasmic rcticulum and C-terminal processing
    • 38. Hahn, D., Lottaz, D. & Sterchi, E.E. (1997) C-cytosolic and transmembrane domains of the N-benzoyl-L-tyrosyl-p-aminobenzoic acid hydrolase alpha subunit (human meprin alpha) are essential for its retention in the endoplasmic rcticulum and C-terminal processing. Eur J. Biochem. 247, 933-941.
    • (1997) Eur J. Biochem. , vol.247 , pp. 933-941
    • Hahn, D.1    Lottaz, D.2    Sterchi, E.E.3
  • 39
    • 0023008846 scopus 로고
    • Novel blockade by brefeldin A of intracellular transport of secretory proteins in cultured rat hepatocytes
    • 39. Misumi, Y., Miki, K., Takatsuki, A., Tamura, G. & Ikehara, Y. (1986) Novel blockade by brefeldin A of intracellular transport of secretory proteins in cultured rat hepatocytes. J. Biol Chem. 261, 11398-11403.
    • (1986) J. Biol Chem. , vol.261 , pp. 11398-11403
    • Misumi, Y.1    Miki, K.2    Takatsuki, A.3    Tamura, G.4    Ikehara, Y.5
  • 40
    • 0025103773 scopus 로고
    • Compartmentation of the Golgi complex: Brefeldin-A distinguishes trans-Golgi cisternae from the trans-Golgi network
    • 40. Chege, N.W. & Pfeffer, S.R. (1990) Compartmentation of the Golgi complex: brefeldin-A distinguishes trans-Golgi cisternae from the trans-Golgi network. J. Cell Biol. 111, 893-899.
    • (1990) J. Cell Biol. , vol.111 , pp. 893-899
    • Chege, N.W.1    Pfeffer, S.R.2
  • 41
    • 0024308993 scopus 로고
    • Brefeldin A redistributes resident and itinerant Golgi proteins to the endoplasmic reticulum
    • 41. Doms, R.W., Russ, G. & Yewdell, J.W. (1989) Brefeldin A redistributes resident and itinerant Golgi proteins to the endoplasmic reticulum. J. Cell Biol. 109, 61-72.
    • (1989) J. Cell Biol. , vol.109 , pp. 61-72
    • Doms, R.W.1    Russ, G.2    Yewdell, J.W.3
  • 42
    • 0024237306 scopus 로고
    • Brefeldin A causes disassembly of the Golgi complex and accumulation of secretory proteins in the endoplasmic reticulum
    • 42. Fujiwara, T., Oda, K., Yokota, S., Takatsuki, A. & Ikehara, Y. (1988) Brefeldin A causes disassembly of the Golgi complex and accumulation of secretory proteins in the endoplasmic reticulum. J. Biol. Chem. 263, 18545-18552.
    • (1988) J. Biol. Chem. , vol.263 , pp. 18545-18552
    • Fujiwara, T.1    Oda, K.2    Yokota, S.3    Takatsuki, A.4    Ikehara, Y.5
  • 43
    • 0025232841 scopus 로고
    • Microtubule-dependent retrograde transport of proteins into the ER in the presence of brefeldin A suggests an ER recycling pathway
    • 43. Lippincott-Schwartz, J., Donaldson, J.G., Schweizer, A., Berger, E.G., Hauri, H.P., Yuan, L.C. & Klausner, R.D. (1990) Microtubule-dependent retrograde transport of proteins into the ER in the presence of brefeldin A suggests an ER recycling pathway. Cell 60, 821 -836.
    • (1990) Cell , vol.60 , pp. 821-836
    • Lippincott-Schwartz, J.1    Donaldson, J.G.2    Schweizer, A.3    Berger, E.G.4    Hauri, H.P.5    Yuan, L.C.6    Klausner, R.D.7
  • 44
    • 0025916877 scopus 로고
    • Arg-X-Lys/Arg-Arg motif as a signal for precursor cleavage catalyzed by furin within the constitutive secretory pathway
    • 44. Hosaka, M., Nagahama, M., Kim, W.S., Watanabe, T., Hatsuzawa, K., Ikemizu, J., Murakami, K. & Nakayama, K. (1991) Arg-X-Lys/Arg-Arg motif as a signal for precursor cleavage catalyzed by furin within the constitutive secretory pathway. J. Biol. Chem. 266, 12127-12130.
    • (1991) J. Biol. Chem. , vol.266 , pp. 12127-12130
    • Hosaka, M.1    Nagahama, M.2    Kim, W.S.3    Watanabe, T.4    Hatsuzawa, K.5    Ikemizu, J.6    Murakami, K.7    Nakayama, K.8
  • 45
    • 0028980285 scopus 로고
    • Proteolytic processing of the alpha-subunit of rat endopeptidase-24.18 by furin
    • 45. Milhiet, P.E., Chevallier, S., Corbeil, D., Seidah, N.G., Crine, P. & Boileau, G. (1995) Proteolytic processing of the alpha-subunit of rat endopeptidase-24.18 by furin. Biochem. J. 309, 683-688.
    • (1995) Biochem. J. , vol.309 , pp. 683-688
    • Milhiet, P.E.1    Chevallier, S.2    Corbeil, D.3    Seidah, N.G.4    Crine, P.5    Boileau, G.6
  • 46
    • 0031818050 scopus 로고    scopus 로고
    • Maturation of secreted meprin alpha during biosynthesis: Role of the furin site and identification of the COOH-terminal amino acids of the mouse kidney metalloprotease subunit
    • 46. Tang, J. & Bond, J.S. (1998) Maturation of secreted meprin alpha during biosynthesis: role of the furin site and identification of the COOH-terminal amino acids of the mouse kidney metalloprotease subunit. Arch. Biochem. Biophys. 349, 192-200.
    • (1998) Arch. Biochem. Biophys. , vol.349 , pp. 192-200
    • Tang, J.1    Bond, J.S.2
  • 47
    • 0028923308 scopus 로고
    • COOH-terminal proteolytic processing of secreted and membrane forms of the alpha subunit of the metalloprotease meprin A. Requirement of the I domain for processing in the endoplasmic reticulum
    • 47. Marchand, P., Tang, J., Johnson, G.D. & Bond, J.S. (1995) COOH-terminal proteolytic processing of secreted and membrane forms of the alpha subunit of the metalloprotease meprin A. Requirement of the I domain for processing in the endoplasmic reticulum. J. Biol. Chem. 270, 5449-5456.
    • (1995) J. Biol. Chem. , vol.270 , pp. 5449-5456
    • Marchand, P.1    Tang, J.2    Johnson, G.D.3    Bond, J.S.4
  • 48
    • 0027236997 scopus 로고
    • Membrane-anchored growth factors
    • 48. Massague, J. & Pandiella, A. (1993) Membrane-anchored growth factors. Annu. Rev. Biochem. 62, 515-541.
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 515-541
    • Massague, J.1    Pandiella, A.2
  • 51
    • 0033104363 scopus 로고    scopus 로고
    • Non-polarized secretion of human meprin a in colorectal cancer generates an increased proteolytic potential in the stroma
    • in press
    • 51. Lottaz, D., Maurer, C.A., Hahn, D., Büchler, M.W. & Sterchi, E.E. (1999) Non-polarized secretion of human meprin a in colorectal cancer generates an increased proteolytic potential in the stroma. Cancer Research, in press
    • (1999) Cancer Research
    • Lottaz, D.1    Maurer, C.A.2    Hahn, D.3    Büchler, M.W.4    Sterchi, E.E.5
  • 52
    • 0014757386 scopus 로고
    • A general method applicable to the search for similarities in the amino acid sequence of two proteins
    • 52. Needleman, S.B. & Wunsch, C.D. (1970) A general method applicable to the search for similarities in the amino acid sequence of two proteins. J. Mol. Biol. 48, 443-453.
    • (1970) J. Mol. Biol. , vol.48 , pp. 443-453
    • Needleman, S.B.1    Wunsch, C.D.2


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