The membrane-bound basic carboxypeptidase from hog intestinal mucosa

Biochimica et Biophysica Acta - Biomembranes

Volumn 1421, Issue 2, 1999, Pages 234-248

  Ore, Florence Dalle ^a   Ajandouz, El Hassan ^a   Giardina, Thierry ^a   Puigserver, Antoine ^a  

^a AIX MARSEILLE UNIVERSITY   (France)

Author keywords

Carboxypeptidase; Hog intestine; Membrane bound protein; Metalloprotein

Indexed keywords

CARBOXYPEPTIDASE; CARBOXYPEPTIDASE D;

AMINO ACID COMPOSITION; ANIMAL TISSUE; ARTICLE; CELL STRAIN; CONTROLLED STUDY; ENZYME ACTIVITY; IMMUNOBLOTTING; INTESTINE MUCOSA; MEMBRANE BINDING; NONHUMAN; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; SWINE;

AMINO ACIDS; ANIMALS; CARBOXYPEPTIDASES; CELL MEMBRANE; DETERGENTS; ENDOPEPTIDASES; ENZYME ACTIVATION; GASTRIC MUCOSA; HYDROGEN-ION CONCENTRATION; INTESTINAL MUCOSA; INTRACELLULAR MEMBRANES; PHOSPHOLIPASE C; SOLUBILITY; SUBCELLULAR FRACTIONS; SWINE; TRYPSIN;

EID: 0345425636     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0005-2736(99)00122-4     Document Type: Article

References (65)

1. R.A. Skidgel, Basic carboxypeptidases: regulators of peptide hormone activity, Trends Pharmacol. Sci. 9 (1988) 299-304.
2. T.H. Plummer, M.Y. Hurwitz, Human plasma carboxypeptidase N. Isolation and characterization, J. Biol. Chem. 253 (1978) 3907-3912.
3. Y. Levin, R.A. Skidgel, E.G. Erdös, Isolation and characterization of the subunits of human plasma carboxypeptidase N (kininase I), Proc. Natl. Acad. Sci. USA 79 (1982) 4618-4622.
4. R. Huey, C.M. Bloor, M.S. Kawahara, T.E. Hugli, Potentiation of the anaphylatoxins in vivo using an inhibitor of serum carboxypeptidase N (SCPN). I. Lethality and pathologic effects on pulmonary tissue, Am. J. Pathol. 112 (1983) 48-60.
5. D.L. Eaton, B.E. Malloy, S.P. Tsai, W. Henzel, D. Drayna, Isolation, molecular cloning, and partial characterization of a novel carboxypeptidase B from human plasma, J. Biol. Chem. 266 (1991) 21833-21838.
6. A.K. Tan, D.L. Eaton, Activation and characterization of procarboxypeptidase B from human plasma, Biochemistry 34 (1995) 5811-5816.
7. L. Bajzar, R. Manuel, M.E. Nesheim, Purification and characterization of TAFI, a thrombin-activable fibrinolysis inhibitor, J. Biol. Chem. 270 (1995) 14477-14484.
8. L. Bajzar, J. Morser, M.E. Nesheim, TAFI, or plasma procarboxypeptidase B, couples the coagulation and fibrinolytic cascades through the thrombin-thrombomodulin complex, J. Biol. Chem. 271 (1996) 16603-16608.
9. L.D. Fricker, S.H. Snyder, Enkephalin convertase: purification and characterization of a specific enkephalin-synthesizing carboxypeptidase localized to adrenal chromaffin granules, Proc. Natl. Acad. Sci. USA 79 (1982) 3886-3890.
10. L.D. Fricker, S. Supattapone, S.H. Snyder, Enkephalin convertase: a specific enkephalin synthesizing carboxypeptidase in adrenal chromaffin granules, brain, and pituitary gland, Life Sci. 31 (1982) 1841-1844.
11. L.D. Fricker, S.H. Snyder, Purification and characterization of enkephalin convertase, an enkephalin-synthesizing carboxypeptidase, J. Biol. Chem. 258 (1983) 10950-10955.
12. V.Y.H. Hook, Y.P. Loh, Carboxypeptidase B-like converting enzyme activity in secretory granules of rat pituitary, Proc. Natl. Acad. Sci. USA 81 (1984) 2776-2780.
13. H.W. Davidson, J.C. Hutton, The insulin-secretory-granule carboxypeptidase H. Purification and demonstration of involvement in proinsulin processing, Biochem. J. 245 (1987) 575-582.
14. S. Supattapone, L.D. Fricker, S.H. Snyder, Purification and characterization of a membrane-bound enkephalin-forming carboxypeptidase, 'enkephalin convertase', J. Neurochem. 42 (1984) 1017-1023.
15. L.D. Fricker, B. Das, R.H. Angeletti, Identification of the pH-dependent membrane anchor of carboxypeptidase E (EC 3.4.17.10), J. Biol. Chem. 265 (1990) 2476-2482.
16. 31P nuclear magnetic resonance spectroscopy, J. Biol. Chem. 254 (1979) 1170-1177.
17. J.C. Hutton, The internal pH and membrane potential of the insulin-secretory granule, Biochem. J. 204 (1982) 171-178.
18. L.D. Fricker, Carboxypeptidase E, Annu. Rev. Physiol. 50 (1988) 309-321.
19. L. Song, L.D. Fricker, Purification and characterization of carboxypeptidase D, a novel carboxypeptidase E-like enzyme, from bovine pituitary, J. Biol. Chem. 270 (1995) 25007-25013.
20. L. Song, L.D. Fricker, Tissue distribution and characterization of soluble and membrane-bound forms of metallocarboxypeptidase D, J. Biol. Chem. 271 (1996) 28884-28889.
21. R.A. Skidgel, R.M. Davis, F. Tan, M. Human carboxypeptidase, Purification and characterization of a membrane-bound carboxypeptidase that cleaves peptide hormones, J. Biol. Chem. 264 (1989) 2236-2241.
22. F. Tan, S.J. Chan, D.F. Steiner, J.W. Schilling, R.A. Skidgel, Molecular cloning and sequencing of the cDNA for human membrane-bound carboxypeptidase M. Comparison with carboxypeptidases A, B, H, and N, J. Biol. Chem. 264 (1989) 13165-13170.
23. Y. Shimamori, Y. Kumagai, Y. Watanabe, Y. Fujimoto, Human placental carboxypeptidase M is anchored by a glycosyl-phosphatidylinositol moiety, Biochem. Int. 20 (1990) 607-613.
24. L. Song, L.D. Fricker, Cloning and expression of human carboxypeptidase Z, a novel metallocarboxypeptidase, J. Biol. Chem. 272 (1997) 10543-10550.
25. G.-P. He, A. Muise, A.W. Li, H.-S. Ro, A eukaryotic transcriptional repressor with carboxypeptidase activity, Nature 378 (1995) 92-96.
26. 3H]guanidinoethylmercaptosuccinic acid, Endocrinology 121 (1987) 116-126.
27. 2+ activation and inhibitor binding of carboxypeptidase M at low pH. Similarity to carboxypeptidase H (enkephalin convertase), Biochem. J. 261 (1989) 289-291.
28. R.A. Skidgel, R.A. Anders, P.A. Deddish, E.G. Erdös, Carboxypeptidase (CP) M and H in small intestine, FASEB J. 5 (1991) A1578.
29. A. Koheil, G. Forstner, Isoelectric focusing of carboxypeptidase N, Biochim. Biophys. Acta 524 (1978) 156-161.
30. R.A. Skidgel, E.G. Erdös, Carboxypeptidase N (arginine carboxypeptidase), in: H.U. Bergmeyer (Ed.), Methods of Enzymatic Analysis, Verlag Chemie, Weinheim, 1984, pp. 34-43.
31. D. Louvard, S. Maroux, J. Baratti, P. Desnuelle, S. Mutaftschiev, On the preparation and some properties of closed membrane vesicles from hog duodenal and jejunal brush border, Biochim. Biophys. Acta 291 (1973) 747-763.
32. H. Murer, E. Amman, J. Biber, U. Hopfer, The surface membrane of the small intestinal epithelial cell. I. Localization of adenyl cyclase, Biochim. Biophys. Acta 433 (1976) 509-519.
33. M.L. Clark, H.C. Lanz, J.R. Senior, Enzymatic distinction of rat intestinal cell brush border and endoplasmic reticular membranes, Biochim. Biophys. Acta 183 (1969) 233-235.
34. G.L. Sottocasa, B. Kuylenstierna, L. Ernster, A. Bergstrand, An electron-transport system associated with the outer membrane of liver mitochondria. A biochemical and morphological study, J. Cell Biol. 32 (1967) 415-438.
35. S.J. Cooperstein, A. Lazarow, A microspectrophotometric method for the determination of cytochrome oxidase, J. Biol. Chem. 189 (1951) 665-670.
36. A.J. Barrett, Fluorimetric assays for cathepsin B and cathepsin H with methylcoumarylamide substrates, Biochem. J. 187 (1980) 909-912.
37. D. Gabrijelcic, B. Svetic, D. Spaic, J. Skrk, M. Budihna, I. Dolenc, T. Popovic, V. Cotic, V. Turk, Cathepsins B, H, and L in human breast carcinoma, Eur. J. Clin. Chem. Clin. Biochem. 30 (1992) 69-74.
38. M.M. Bradford, A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding, Anal. Biochem. 72 (1976) 248-254.
39. J. Schmitz, H. Preiser, D. Maestracci, B.K. Ghosh, J.J. Cerda, R.K. Crane, Purification of the human intestinal brush border membrane, Biochim. Biophys. Acta 323 (1973) 98-112.
40. J. Maury, C. Nicoletti, L. Guzzo-Chambraud, S. Maroux, The filamentous brush border glycocalyx, a mucin-like marker of enterocyte hyper-polarization, Eur. J. Biochem. 228 (1995) 323-331.
41. U.K. Laemmli, Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature 227 (1970) 680-685.
42. O. Gabriel, Analytical disc gel electrophoresis, Methods Enzymol. 22 (1971) 565-578.
43. R.M. Zacharius, T.E. Zell, J.H. Morrison, J.J. Woodlock, Glycoprotein staining following electrophoresis on acrylamide gels, Anal. Biochem. 30 (1969) 148-152.
44. P. Matsudaira, Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes, J. Biol. Chem. 262 (1987) 10035-10038.
45. B.A. Bidlingmeyer, S.A. Cohen, T.L. Tarvin, Rapid analysis of amino acids using pre-column derivatization, J. Chromatogr. 336 (1984) 93-104.
46. R.M. Hewik, M.W. Hunkapiller, L.E. Hood, W.J. Dreyer, A gas-liquid solid phase peptide and protein sequanator, J. Biol. Chem. 256 (1981) 7990-7997.
47. W.N. Burnette, 'Western blotting': electrophoretic transfer of proteins from dodecyl sulfate-polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A, Anal. Biochem. 112 (1981) 195-203.
48. E. Coudrier, H. Reggio, D. Louvard, Characterization of an integral membrane glycoprotein associated with the microfilaments of pig intestinal microvilli, EMBO J. 2 (1983) 469-475.
49. J.-P. Gorvel, A. Rigal, J. Sarles, S. Maroux, Aminopeptidase N- and human blood group A-antigenicity along the digestive tract and associated glands in the rabbit, Cell Tissue Res. 239 (1985) 241-248.
50. P.A. Deddish, R.A. Skidgel, V.B. Kriho, X.-Y. Li, R.P. Becker, E.G. Erdös, Carboxypeptidase M in Madin-Darby canine kidney cells. Evidence that Carboxypeptidase M has a phosphatidylinositol glycan anchor, J. Biol. Chem. 265 (1990) 15083-15089.
51. A.J. Barrett, H. Kirschke, Cathepsin B, cathepsin H, and cathepsin L, Methods Enzymol. 80 (1981) 535-561.
52. N.M. Hooper, A.J. Turner, Ectoenzymes of the kidney microvillar membrane. Differential solubilization by detergents can predict a glycosyl-phosphatidylinositol membrane anchor, Biochem. J. 250 (1988) 865-869.
53. N.M. Hooper, A.J. Turner, Ectoenzymes of the kidney microvillar membrane. Aminopeptidase P is anchored by a glycosyl-phosphatidylinositol moiety, FEBS Lett. 229 (1988) 340-344.
54. F. Tan, M. Rehli, S.W. Krause, R.A. Skidgel, Sequence of human Carboxypeptidase D reveals it to be a member of the regulatory Carboxypeptidase family with three tandem active site domains, Biochem. J. 327 (1997) 81-87.
55. H. Koga, H. Yamada, Y. Nishimura, K. Kato, T. Imoto, Multiple proteolytic action of rat liver cathepsin B: specificities and pH-dependencies of the endo- and exopeptidase activities, J. Biochem. 110 (1991) 179-188.
56. G.M. Ekström, B.R. Weström, Cathepsin B and D activities in intestinal mucosa during postnatal development in pigs. Relation to intestinal uptake and transmission of macromolecules, Biol. Neonate 59 (1991) 314-321.
57. M. Furuhashi, A. Nakahara, H. Fukutomi, E. Kominami, D. Grube, Y. Uchiyama, Immunocytochemical localization of cathepsins B, H, and L in the rat gastro-duodenal mucosa, Histochemistry 95 (1991) 231-239.
58. G.B. McGwire, F. Tan, B. Michel, M. Rehli, R.A. Skidgel, Identification of a membrane-bound Carboxypeptidase as the mammalian homolog of duck gp180, a hepatitis B virus-binding protein, Life Sci. 60 (1997) 715-724.
59. K. Kuroki, F. Eng, T. Ishikawa, C. Turck, F. Harada, D. Ganem, gp180, a host cell glycoprotein that binds duck hepatitis B virus particles, is encoded by a member of the carboxypeptidase gene family, J. Biol. Chem. 270 (1995) 15022-15028.
60. fat mice, Cell 88 (1997) 73-83.
61. fat mice associated with a Carboxypeptidase E mutation, Proc. Natl. Acad. Sci. USA 94 (1997) 5314-5319.
62. K.D. Bhoola, C.D. Figueroa, K. Worthy, Bioregulation of kinins: kallikreins, kininogens, and kininases, Pharmacol. Rev. 44 (1992) 1-80.
63. O. Varlamov, L.D. Fricker, Intracellular trafficking of metallocarboxypeptidase D in AtT-20 cells: localization to the trans-Golgi network and recycling from the cell surface, J. Cell Sci. 111 (1998) 877-885.
64. B. Delmas, J. Gelfi, R. L'Haridon, L.K. Vogel, H. Sjöström, O. Noren, H. Laude, Aminopeptidase N is a major receptor for the enteropathogenic coronavirus TGEV, Nature 357 (1992) 417-420.
65. C.L. Yeager, R.A. Ashmun, R.K. Williams, C.B. Cardellichio, L.H. Shapin, A.T. Look, K.V. Holmes, Human aminopeptidase N is a receptor for human coronavirus 229E, Nature 357 (1992) 420-422.