Carboxypeptidase M: Multiple alliances and unknown partners

Clinica Chimica Acta

Volumn 399, Issue 1-2, 2009, Pages 24-39

  Deiteren, Kathleen ^a   Hendriks, Dirk ^a   Scharpé, Simon ^a   Lambeir, Anne Marie ^a  

^a UNIVERSITY OF ANTWERP   (Belgium)

Author keywords

Cancer; Carboxypeptidase; Inflammation; Membrane protein; Mesenchymal cells; Peptides

Indexed keywords

CARBOXYPEPTIDASE; CARBOXYPEPTIDASE M; CELL SURFACE PROTEIN; PROTEINASE; UNCLASSIFIED DRUG;

CARBOXY TERMINAL SEQUENCE; CELL SURFACE; CELL TYPE; CELLULAR DISTRIBUTION; CRYSTAL STRUCTURE; ENZYME MECHANISM; HUMAN; INFLAMMATION; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FAMILY; PROTEIN PROTEIN INTERACTION; REVIEW;

AMINO ACID SEQUENCE; ANIMALS; CELL MEMBRANE; HUMANS; METALLOENDOPEPTIDASES; MOLECULAR SEQUENCE DATA; PROTEASE INHIBITORS; PROTEIN BINDING; SUBSTRATE SPECIFICITY;

EID: 57049098571     PISSN: 00098981     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cca.2008.10.003     Document Type: Review

References (240)

1. Rawlings N.D., Morton F.R., and Barrett A.J. MEROPS: the peptidase database. Nucleic Acids Res 34 (2006) D270-D272
2. Kalinina E., Biswas R., Berezniuk I., Hermoso A., Aviles F.X., and Fricker L.D. A novel subfamily of mouse cytosolic carboxypeptidases. FASEB J 21 (2007) 836-850
3. Rodriguez de la Vega M., Sevilla R.G., Hermoso A., et al. Nna1-like proteins are active metallocarboxypeptidases of a new and diverse M14 subfamily. FASEB J 21 (2007) 851-865
4. Reznik S.E., and Fricker L.D. Carboxypeptidases from A to z: implications in embryonic development and Wnt binding. Cell Mol Life Sci 58 (2001) 1790-1804
5. Lei Y.H., Xin X.N., Morgan D., Pintar J.E., and Fricker L.D. Identification of mouse CPX-1, a novel member of the metallocarboxypeptidase gene family with highest similarity to CPX-2. DNA Cell Biol 18 (1999) 175-185
6. Xin X.N., Day R., Dong W.J., Lei Y.H., and Fricker L.D. Identification of mouse CPX-2, a novel member of the metallocarboxypeptidase gene family: cDNA cloning, mRNA distribution, and protein expression and characterization. DNA Cell Biol 17 (1998) 897-909
7. Fricker L.D., and Leiter E.H. Peptides, enzymes and obesity: new insights from a 'dead' enzyme. Trends in Biochem Sci 24 (1999) 390-393
8. He G.P., Muise A., Li A.W., and Ro H.S. A eukaryotic transcriptional repressor with carboxypeptidase activity. Nature 378 (1995) 92-96
9. Vendrell J., Querol E., and Avilés F.X. Metallocarboxypeptidases and their protein inhibitors. Structure, function and biomedical properties. Biochim Biophys Acta 1477 (2000) 284-298
10. Handbook of proteolytic enzymes (1998), Academic Press, London
11. Osterman A.L., Grishin N.V., Smulevitch S.V., et al. Primary structure of carboxypeptidase-T: delineation of functionally relevant features in Zn carboxypeptidase family. J Protein Chem 11 (1992) 561-570
12. Marx P.F., Brondijk T.H., Plug T., et al. Crystal structures of TAFI elucidate the inactivation mechanism of activated TAFI: a novel mechanism for enzyme autoregulation. Blood. 112 (2008) 2803-2809
13. Nantermet P.G., Barrow J.C., Lindsley S.R., et al. Imidazole acetic acid TAFI inhibitors: SAR studies centered around the basic P'1 group. Bioorg Med Chem Lett 14 (2004) 2141-2145
14. Polla M.O., Tottie L., Nordén C., et al. Design and synthesis of potent, orally active, inhibitors of carboxypeptidase U (TAFIa). Bioorg Med Chem 12 (2004) 1151-1175
15. Adler M., Buckman B., Bryant J., et al. Structures of potent selective peptide mimetics bound to carboxypeptidase B. Acta Crystallogr D 64 (2008) 149-157
16. Bunnage M.E., Blagg J., Steele J., et al. Discovery of potent and selective inhibitors of activated thrombin-activatable fibrinolysis inhibitor for the treatment of thrombosis. J Med Chem 50 (2007) 6095-6103
17. Deiteren K., Surpateanu G., Gilany K., et al. The role of the S1 binding site of carboxypeptidase M in substrate specificity and turn-over. BBA-Proteins Proteom 1774 (2007) 267-277
18. Willemse J.L., Polla M., Olsson T., and Hendriks D.F. Comparative substrate specificity study of carboxypeptidase U (TAFIa) and carboxypeptidase N: development of highly selective CPU substrates as useful tools for assay development. Clin Chim Acta 387 (2008) 158-160
19. Chen H., Jawahar S., Qian Y.M., et al. Missense polymorphism in the human carboxypeptidase E gene alters enzymatic activity. Hum Mutat 18 (2001) 120-131
20. Novikova E.G., Eng F.J., Yan L., Qian Y.M., and Fricker L.D. Characterization of the enzymatic properties of the first and second domains of metallocarboxypeptidase D. J Biol Chem 274 (1999) 28887-28892
21. Shimamori Y., Kumagai Y., Watanabe Y., and Fujimoto Y. Human placental carboxypeptidase M is anchored by a glycosyl-phosphatidylinositol moiety. Biochem Int 20 (1990) 607-613
22. Deddish P.A., Skidgel R.A., Kriho V.B., Li X.Y., Becker R.P., and Erdös E.G. Carboxypeptidase M in Madin-Darby canine kidney cells. Evidence that carboxypeptidase M has a phosphatidylinositol glycan anchor. J Biol Chem 265 (1990) 15083-15089
23. Skidgel R.A., McGwire G.B., and Li X.Y. Membrane anchoring and release of carboxypeptidase M: implications for extracellular hydrolysis of peptide hormones. Immunopharmacology 32 (1996) 48-52
24. Harris R.J. Processing of C-terminal lysine and arginine residues of proteins isolated from mammalian cell culture. J Chromatogr A 705 (1995) 129-134
25. Matthiessen H.P., Willemse J., Weber A., et al. Ethanol dependence of alpha(1)-antitrypsin C-terminal Lys truncation mediated by basic carboxypeptidases. Transfusion 48 (2008) 314-320
26. Skidgel R.A., Johnson A.R., and Erdös E.G. Hydrolysis of opioid hexapeptides by carboxypeptidase-N. Presence of carboxypeptidase in cell-membranes. Biochem Pharmacol 33 (1984) 3471-3478
27. Emmrich F., and Andreesen R. Monoclonal antibodies against differentiation antigens on human macrophages. Immunol Lett 9 (1985) 321-324
28. Skidgel R.A., Deddish P.A., and Davis R.M. Isolation and characterization of a basic carboxypeptidase from human seminal plasma. Arch Biochem Biophys 267 (1988) 660-667
29. Tan F., Chan S.J., Steiner D.F., Schilling J.W., and Skidgel R.A. 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
30. Skidgel R.A., Davis R.M., and Tan F. Human carboxypeptidase M. Purification and characterization of a membrane-bound carboxypeptidase that cleaves peptide hormones. J Biol Chem 264 (1989) 2236-2241
31. Rehli M., Krause S.W., Kreutz M., and Andreesen R. Carboxypeptidase M is identical to the MAX.1 antigen and its expression is associated with monocyte to macrophage differentiation. J Biol Chem 270 (1995) 15644-15649
32. Kas K., Schoenmakers E.F., and Van de Ven W.J. Physical map location of the human carboxypeptidase M gene (CPM) distal to D12S375 and proximal to D12S8 at chromosome 12q15. Genomics 30 (1995) 403-405
33. Pessoa L.G., da Silva I.D., Baptista H.A., et al. Molecular structure and alternative splicing of the human carboxypeptidase M gene. Biol Chem 383 (2002) 263-269
34. Li J., Rehli M., Timblin B., Tan F., Krause S.W., and Skidgel R.A. Structure of the human carboxypeptidase M gene. Identification of a proximal GC-rich promoter and a unique distal promoter that consists of repetitive elements. Gene 284 (2002) 189-202
35. Tan F., Deddish P.A., and Skidgel R.A. Human carboxypeptidase M. Methods Enzymol 248 (1995) 663-675
36. Yoshioka S., Fujiwara H., Yamada S., et al. Membrane-bound carboxypeptidase-M is expressed on human ovarian follicles and corpora lutea of menstrual cycle and early pregnancy. Mol Hum Reprod 4 (1998) 709-717
37. Skidgel R.A., Davis R.M., and Erdös E.G. Purification of a human urinary carboxypeptidase (kininase) distinct from carboxypeptidase-A, carboxypeptidase-B, or carboxypeptidase-N. Anal Biochem 140 (1984) 520-531
38. Li N., Mak A., Richards D.P., et al. Monocyte lipid rafts contain proteins implicated in vesicular trafficking and phagosome formation. Proteomics 3 (2003) 536-548
39. McGwire G.B., Becker R.P., and Skidgel R.A. Carboxypeptidase M, a glycosylphosphatidylinositol-anchored protein, is localized on both the apical and basolateral domains of polarized Madin-Darby canine kidney cells. J Biol Chem 274 (1999) 31632-31640
40. Li X.Y., and Skidgel R.A. Release of glycosylphosphatidylinositol-anchored carboxypeptidase M by phosphatidylinositol-specific phospholipase C upregulates enzyme synthesis. Biochem Biophys Res Commun 258 (1999) 204-210
41. Andreesen R., Gadd S., Costabel U., et al. Human macrophage maturation and heterogeneity: restricted expression of late differentiation antigens in situ. Cell Tissue Res 253 (1988) 271-279
42. Krause S.W., Rehli M., and Andreesen R. Carboxypeptidase M as a marker of macrophage maturation. Immunol Rev 161 (1998) 119-127
43. Tan F., Balsitis S., Black J.K., et al. Effect of mutation of two critical glutamic acid residues on the activity and stability of human carboxypeptidase M and characterization of its signal for glycosylphosphatidylinositol anchoring. Biochem J 370 (2003) 567-578
44. Craveiro R.B., Ramalho J.D., Chagas J.R., et al. High expression of human carboxypeptidase M in Pichia pastoris. Purification and partial characterization. Braz J Med Biol Res 39 (2006) 211-217
45. Elortza F., Nühse T.S., Foster L.J., Stensballe A., Peck S.C., and Jensen O.N. Proteomic analysis of glycosylphosphatidylinositol-anchored membrane proteins. Mol Cell Proteomics 2 (2003) 1261-1270
46. Grzybek M., Kozubek A., Dubielecka P., and Sikorski A.F. Rafts-the current picture. Folia Histochem Cytobiol 43 (2005) 3-10
47. Li N., Shaw A.R.E., Zhang N., Mak A., and Li L. Lipid raft proteomics: analysis of in-solution digest of sodium dodecyl sulphate-solubilized lipid raft proteins by liquid chromatography-matrix-assisted laser desorption/ionization tandem mass spectrometry. Proteomics 4 (2004) 3156-3166
48. Zhang X.M., Tan F.L., Zhang Y.K., and Skidgel R.A. Carboxypeptidase M and kinin B1 receptors interact to facilitate efficient B1 signaling from B2 agonists. J Biol Chem 283 (2008) 7994-8004
49. Dhanvantari S., and Loh Y.P. Lipid raft association of carboxypeptidase E is necessary for its function as a regulated secretory pathway sorting receptor. J Biol Chem 275 (2000) 29887-29893
50. Hamai K., Ikeda R., Sumi H., and Mihara H. Carboxypeptidase activity in human urine from healthy subjects and renal disease patients. Clin Chim Acta 188 (1990) 233-242
51. McGwire G.B., and Skidgel R.A. Extracellular conversion of epidermal growth factor (EGF) to des-Arg53-EGF by carboxypeptidase M. J Biol Chem 270 (1995) 17154-17158
52. Dragovic T., Schraufnagel D.E., Becker R.P., Sekosan M., Votta-Velis E.G., and Erdös E.G. Carboxypeptidase M activity is increased in bronchoalveolar lavage in human lung disease. Am J Respir Crit Care Med 152 (1995) 760-764
53. Skidgel R.A. Structure and function of mammalian zinc carboxypeptidases. In: Hooper N.M. (Ed). Zinc metalloproteases in health and disease (1996), Taylor & Francis Ltd., London 241-283
54. Skidgel R.A. Assays for arginine/lysine carboxypeptidases: carboxypeptidase H (E; enkephalin convertase), M, and N. In: Rawlings N.D., Barrett A.J., and Woessner J.F. (Eds). Methods in neurosciences (1991), Academic Press, Toronto 373-385
55. Schatteman K.A., Goossens F.J., Scharpé S.S., Neels H.M., and Hendriks D.F. Assay of procarboxypeptidase U, a novel determinant of the fibrinolytic cascade, in human plasma. Clin Chem 45 (1999) 807-813
56. Willemse J., Leurs J., Verkerk R., and Hendriks D. Development of a fast kinetic method for the determination of carboxypeptidase U (TAFIa) using C-terminal arginine containing peptides as substrate. Anal Biochem 340 (2005) 106-112
57. Mao S.S., Colussi D., Bailey C.M., et al. Electrochemiluminescence assay for basic carboxypeptidases: inhibition of basic carboxypeptidases and activation of thrombin-activatable fibrinolysis inhibitor. Anal Biochem 319 (2003) 159-170
58. Mentlein R., and Roos T. Proteases involved in the metabolism of angiotensin II, bradykinin, calcitonin gene-related peptide (CGRP), and neuropeptide Y by vascular smooth muscle cells. Peptides 17 (1996) 709-720
59. Michel B., Igíc R., Leray V., Deddish P.A., and Erdös E.G. Removal of Arg141 from the alpha chain of human hemoglobin by carboxypeptidases N and M. Circ Res 78 (1996) 635-642
60. Dragovic T., Igíc R., Erdös E.G., and Rabito S.F. Metabolism of bradykinin by peptidases in the lung. Am Rev Respir Dis 147 (1993) 1491-1496
61. Nagae A., Abe M., Becker R.P., Deddish P.A., Skidgel R.A., and Erdös E.G. High concentration of carboxypeptidase M in lungs: presence of the enzyme in alveolar type I cells. Am J Respir Cell Mol Biol 9 (1993) 221-229
62. Desmazes N., Lockhart A., Lacroix H., and Dusser D.J. Carboxypeptidase M-like enzyme modulates the noncholinergic bronchoconstrictor response in guinea pig. Am J Respir Cell Mol Biol 7 (1992) 477-484
63. Nagae A., Deddish P.A., Becker R.P., et al. Carboxypeptidase M in brain and peripheral nerves. J Neurochem 59 (1992) 2201-2212
64. Chodimella V., Skidgel R.A., Krowiak E.J., and Murlas C.G. Lung peptidases, including carboxypeptidase, modulate airway reactivity to intravenous bradykinin. Am Rev Respir Dis 144 (1991) 869-874
65. Sangsree S., Brovkovych V., Minshall R.D., and Skidgel R.A. Kininase I-type carboxypeptidases enhance nitric oxide production in endothelial cells by generating bradykinin B1 receptor agonists. Am J Physiol Heart Circ Physiol 284 (2003) H1959-H1968
66. Arolas J.L., Popowicz G.M., Lorenzo J., et al. The three-dimensional structures of tick carboxypeptidase inhibitor in complex with A/B carboxypeptidases reveal a novel double-headed binding mode. J Mol Biol 350 (2005) 489-498
67. Reverter D., Fernández-Catalán C., Baumgartner R., et al. Structure of a novel leech carboxypeptidase inhibitor determined free in solution and in complex with human carboxypeptidase A2. Nat Struct Biol 7 (2000) 322-328
68. Aloy P., Companys V., Vendrell J., et al. The crystal structure of the inhibitor-complexed carboxypeptidase D domain II and the modeling of regulatory carboxypeptidases. J Biol Chem 276 (2001) 16177-16184
69. Reverter D., Maskos K., Tan F., Skidgel R.A., and Bode W. Crystal structure of human carboxypeptidase M, a membrane-bound enzyme that regulates peptide hormone activity. J Mol Biol 338 (2004) 257-269
70. Keil C., Maskos K., Than M., et al. Crystal structure of the human carboxypeptidase N (kininase I) catalytic domain. J Mol Biol 366 (2007) 504-516
71. Gomis-Rüth F.X., Companys V., Qian Y., et al. Crystal structure of avian carboxypeptidase D domain II: a prototype for the regulatory metallocarboxypeptidase subfamily. EMBO J 18 (1999) 5817-5826
72. Moeller C., Swindell E.C., Kispert A., and Eichele G. Carboxypeptidase Z (CPZ) modulates Wnt signaling and regulates the development of skeletal elements in the chicken. Development. 130 (2003) 5103-5111
73. Bayés A., Fernández D., Solà M., et al. Caught after the act: a human A-type metallocarboxypeptidase in a product complex with a cleaved hexapeptide. Biochemistry 46 (2007) 6921-6930
74. Vallee B.L., and Auld D.S. Kinetics of carboxypeptidase A. The pH dependence of tripeptide hydrolysis catalyzed by zinc, cobalt and manganese enzymes. Biochemistry 9 (1970) 4352-4359
75. Skidgel R.A. Basic carboxypeptidases: regulators of peptide hormone activity. Trends Pharmacol Sci 9 (1988) 299-304
76. Rehli M., Krause S.W., and Andreesen R. The membrane-bound ectopeptidase CPM as a marker of macrophage maturation in vitro and in vivo. Adv Exp Med Biol 477 (2000) 205-216
77. Zhou A., Webb G., Zhu X.R., and Steiner D.F. Proteolytic processing in the secretory pathway. J Biol Chem 274 (1999) 20745-20748
78. Day R., Lazure C., Basak A., et al. Prodynorphin processing by proprotein convertase 2. Cleavage at single basic residues and enhanced processing in the presence of carboxypeptidase activity. J Biol Chem 273 (1998) 829-836
79. Skotland T., Hustvedt S.O., Oulie I., et al. NC100668, a new tracer for imaging of venous thromboembolism: disposition and metabolism in rats. Drug Metab Dispos 34 (2006) 111-120
80. de Saint-Vis B., Cupillard L., Pandrau-Garcia D., et al. Distribution of carboxypeptidase M on lymphoid and myeloid cells parallels the other zinc-dependent proteases CD10 and CD13. Blood 86 (1995) 1098-1105
81. Baird J.W., Ryan K.M., Hayes I., et al. Differentiating embryonal stem cells are a rich source of haemopoietic gene products and suggest erythroid preconditioning of primitive haemopoietic stem cells. J Biol Chem 276 (2001) 9189-9198
82. Marquez-Curtis L., Jalili A., Deiteren K., Shirvaikar N., Lambeir A.M., and Janowska-Wieczorek A. Carboxypeptidase M expressed by human bone marrow cells cleaves the C-terminal lysine of stromal cell-derived factor-1 alpha: another player in hematopoietic stem/progenitor cell mobilization?. Stem Cells 26 (2008) 1211-1220
83. Dewar A.L., Domaschenz R.M., Doherty K.V., Hughes T.P., and Lyons A.B. Imatinib inhibits the in vitro development of the monocyte/macrophage lineage from normal human bone marrow progenitors. Leukemia 17 (2003) 1713-1721
84. Blumenthal A., Lauber J., Hoffmann R., et al. Common and unique gene expression signatures of human macrophages in response to four strains of Mycobacterium avium that differ in their growth and persistence characteristics. Infect Immun 73 (2005) 3330-3341
85. Ammon C., Kreutz M., Rehli M., Krause S.W., and Andreesen R. Platelets induce monocyte differentiation in serum-free coculture. J Leukocyte Biol 63 (1998) 469-476
86. Scheuerer B., Ernst M., Dürrbaum-Landmann I., et al. The CXC-chemokine platelet factor 4 promotes monocyte survival and induces monocyte differentiation into macrophages. Blood 95 (2000) 1158-1166
87. Kreutz M., Fritsche J., Ackermann U., Krause S.W., and Andreesen R. Retinoic acid inhibits monocyte to macrophage survival and differentiation. Blood 91 (1998) 4796-4802
88. Krause S.W., Zaiss M., Kreutz M., and Andreesen R. Activation of lymphocytes inhibits human monocyte to macrophage differentiation. Immunobiology 203 (2001) 709-724
89. Andreesen R., Brugger W., Scheibenbogen C., et al. Surface phenotype analysis of human monocyte to macrophage maturation. J Leucocyte Biol 47 (1990) 490-497
90. Ammon C., Meyer S.P., Schwarzfischer L., Krause S.W., Andreesen R., and Kreutz M. Comparative analysis of integrin expression on monocyte-derived macrophages and monocyte-derived dendritic cells. Immunology 100 (2000) 364-369
91. Grassi F., Dezutter-Dambuyant C., McIlroy D., et al. Monocyte-derived dendritic cells have a phenotype comparable to that of dermal dendritic cells and display ultrastructural granules distinct from Birbeck granules. J Leukocyte Biol 64 (1998) 484-493
92. Kahlert H., Grage-Griebenow E., Stüwe H.T., Cromwell O., and Fiebig H. T cell reactivity with allergoids: influence of the type of APC. J Immunol 165 (2000) 1807-1815
93. Galibert L., Burdin N., de Saint-Vis B., et al. CD40 and B cell antigen receptor dual triggering of resting B lymphocytes turns on a partial germinal center phenotype. J Exp Med 183 (1996) 77-85
94. Liu T.M., Martina M., Hutmacher D.W., Hui J.H.P., Lee E.H., and Lim B. Identification of common pathways mediating differentiation of bone marrow- and adipose tissue-derived human mesenchymal stem cells into three mesenchymal lineages. Stem Cells 25 (2007) 750-760
95. Salasznyk R.M., Klees R.F., Westcott A.M., Vandenberg S., Bennett K., and Plopper G.E. Focusing of gene expression as the basis of stem cell differentiation. Stem Cells Dev 14 (2005) 608-620
96. Jeong J.A., Ko K.M., Park H.S., et al. Membrane proteomic analysis of human mesenchymal stromal cells during adipogenesis. Proteomics 7 (2007) 4181-4191
97. Bennett K.P., Bergeron C., Acar E., et al. Proteomics reveals multiple routes to the osteogenic phenotype in mesenchymal stem cells. Bmc Genomics 8 (2007) 380
98. Bujalska I.J., Quinkler M., Tomlinson J.W., Montague T., Smith D.M., and Stewart P.M. Expression profiling of 11 beta-hydroxysteroid dehydrogenase type-1 and glucocorticoid-target genes in subcutaneous and omental human preadipocytes. J Mol Endocrinol 37 (2006) 327-340
99. Summers K.L., O'Donnell J.L., Hoy M.S., et al. Monocyte-macrophage antigen expression on chondrocytes. J Rheumatol 22 (1995) 1326-1334
100. Howell S., Caswell A.M., Kenny A.J., and Turner A.J. Membrane peptidases on human osteoblast-like cells in culture: hydrolysis of calcitonin and hormonal regulation of endopeptidase-24.11. Biochem J 290 (1993) 159-164
101. Christodoulou I., Buttery L.D.K., Saravanapavan P., Tai G.P., Hench L.L., and Polak J.M. Dose- and time-dependent effect of bioactive gel-glass ionic-dissolution products on human fetal osteoblast-specific gene expression. J Biomed Mater Res B Appl Biomater 74B (2005) 529-537
102. Filippov V., Filippova M., and Duerksen-Hughes P.J. The early response to DNA damage can lead to activation of alternative splicing activity resulting in CD44 splice pattern changes. Cancer Res 67 (2007) 7621-7630
103. Monroe D.G., Getz B.J., Johnsen S.A., Riggs B.L., Khosla S., and Spelsberg T.C. Estrogen receptor isoform-specific regulation of endogenous gene expression in human osteoblastic cell lines expressing either ER alpha or ER beta. J Cell Biochem 90 (2003) 315-326
104. Monroe D.G., Secreto F.J., Subramaniam M., Getz B.J., Khosla S., and Spelsberg T.C. Estrogen receptor alpha and beta heterodimers exert unique effects on estrogen- and tamoxifen-dependent gene expression in human U2OS osteosarcoma cells. Mol Endocrinol 19 (2005) 1555-1568
105. Palmieri F.E., Bausback H.H., Churchill L., and Ward P.E. Kinin and enkephalin conversion by an endothelial, plasma-membrane carboxypeptidase. Biochem Pharmacol 35 (1986) 2749-2756
106. Johnson A.R., Skidgel R.A., Gafford J.T., and Erdös E.G. Enzymes in placental microvilli-angiotensin-I converting enzyme, angiotensinase-A, carboxypeptidase, and neutral endopeptidase (enkephalinase). Peptides 5 (1984) 789-796
107. Dassen H., Punyadeera C., Kamps R., et al. Progesterone regulation of implantation-related genes: new insights into the role of oestrogen. Cell Mol Life Sci 64 (2007) 1009-1032
108. Abdelmagid S.A., and Too C.K. Prolactin and estrogen up-regulate carboxypeptidase-d to promote nitric oxide production and survival of mcf-7 breast cancer cells. Endocrinology 149 (2008) 4821-4828
109. Fujiwara H., Imai K., Inoue T., Maeda M., and Fujii S. Membrane-bound cell surface peptidases in reproductive organs. Endocr J 46 (1999) 11-25
110. Batista F., Vaiman D., Dausset J., Fellous M., and Veitia R.A. Potential targets of FOXL2, a transcription factor involved in craniofacial and follicular development, identified by transcriptomics. Proc Natl Acad Sci U S A 104 (2007) 3330-3335
111. Nishioka Y., Higuchi T., Sato Y., et al. Human migrating extravillous trophoblasts express a cell surface peptidase, carboxypeptidase-M. Mol Hum Reprod 9 (2003) 799-806
112. Fujiwara H., Higuchi T., Sato Y., et al. Regulation of human extravillous trophoblast function by membrane-bound peptidases. BBA-Proteins Proteom 1751 (2005) 26-32
113. Schremmer-Danninger E., Nägler D.K., Miska K., et al. Kinin receptors in stimulated and characterized decidua tissue-derived cells. Int Immunopharmacol 7 (2007) 103-112
114. Popovici R.M., Betzler N.K., Krause M.S., et al. Gene expression profiling of human endometrial-trophoblast interaction in a coculture model. Endocrinology 147 (2006) 5662-5675
115. Ramirez M.I., Millien G., Hinds A., Cao Y.X., Seldin D.C., and Williams M.C. T1 alpha, a lung type I cell differentiation gene, is required for normal lung cell proliferation and alveolus formation at birth. Dev Biol 256 (2003) 61-72
116. Williams M.C. Alveolar type I cells: molecular phenotype and development. Annu Rev Physiol 65 (2003) 669-695
117. Howell S., Kenny A.J., and Turner A.J. A survey of membrane peptidases in two human colonic cell lines, Caco-2 and HT-29. Biochem J 284 (1992) 595-601
118. Hooper N.M., and Turner A.J. Ectoenzymes of the kidney microvillar membrane. Aminopeptidase P is anchored by a glycosyl-phosphatidylinositol moiety. FEBS Lett 229 (1988) 340-344
119. Gerritsma J.S.J., van Kooten C., Gerritsen A.F., Mommaas A.M., van Es L.A., and Daha M.R. Production of inflammatory mediators and cytokine responsiveness of an SV40-transformed human proximal tubular epithelial cell line. Exp Nephrol 6 (1998) 208-216
120. Bourne A., Barnes K., Taylor B.A., Turner A.J., and Kenny A.J. Membrane peptidases in the pig choroid plexus and on other cell surfaces in contact with the cerebrospinal fluid. Biochem J 259 (1989) 69-80
121. Jókay I., Soós G., Répássy G., and Dezsö B. Apoptosis in the human inner ear. Detection by in situ end-labeling of fragmented DNA and correlation with other markers. Hearing Res 117 (1998) 131-139
122. Nierhoff D., Levoci L., Schulte S., Goeser T., Rogler L.E., and Shafritz D.A. New cell surface markers for murine fetal hepatic stem cells identified through high density complementary DNA microarrays. Hepatology 46 (2007) 535-547
123. Fujiwara N., Ikeda M., Hirabayashi S., et al. Monoclonal antibody 7F9 recognizes rat protein homologous to human carboxypeptidase-M in developing and adult rat lung. Respirology 12 (2007) 54-62
124. Forbes B., Wilson C.G., and Gumbleton M. Temporal dependence of ectopeptidase expression in alveolar epithelial cell culture: implications for study of peptide absorption. Int J Pharm 180 (1999) 225-234
125. Nagy B., Soós G., Nagy K., and Dezsö B. Natural course of isolated pulmonary Langerhans' cell histiocytosis in a toddler. 3-year follow-up. Respiration 75 (2008) 215-220
126. Kovács J., Varga A., Bessenyei M., and Gomba S. Renal cell cancer associated with sarcoid-like reaction. Pathol Oncol Res 10 (2004) 169-171
127. Boldrick J.C., Alizadeh A.A., Diehn M., et al. Stereotyped and specific gene expression programs in human innate immune responses to bacteria. Proc Natl Acad Sci U S A 99 (2002) 972-977
128. Ramsborg C.G., Windgassen D., Fallon J.K., Paredes C.J., and Papoutsakis E.T. Molecular insights into the pleiotropic effects of plasma on ex vivo-expanded T cells using DNA-microarray analysis. Exp Hematol 32 (2004) 970-990
129. Andreesen R., Brugger W., Thomssen C., Rehm A., Speck B., and Lohr G.W. Defective monocyte-to-macrophage maturation in patients with aplastic anemia. Blood 74 (1989) 2150-2156
130. Andreesen R., Brugger W., Kunze R., Stille W., and von Briesen H. Defective monocyte to macrophage maturation in human-immunodeficiency-virus infection. Res Virol 141 (1990) 217-224
131. Eisert V., Kreutz M., Becker K., et al. Analysis of cellular factors influencing the replication of human immunodeficiency virus type I in human macrophages derived from blood of different healthy donors. Virology 286 (2001) 31-44
132. Chertova E., Chertov O., Coren L.V., et al. Proteomic and biochemical analysis of purified human immunodeficiency virus type 1 produced from infected monocyte-derived macrophages. J Virol 80 (2006) 9039-9052
133. Kálmán J., Kitajka K., Pákáski M., et al. Gene expression profile analysis of lymphocytes from Alzheimer's patients. Psychiat Genet 15 (2005) 1-6
134. Blanchard C., Mingler M.K., Vicario M., et al. IL-13 involvement in eosinophilic esophagitis: transcriptome analysis and reversibility with glucocorticoids. J Allergy Clin Immunol 120 (2007) 1291-1300
135. Zhu H., Tang Y., Ivanciu L., et al. Temporal dynamics of gene expression in the lung in a baboon model of E. coli sepsis. BMC Genomics 8 (2007) 58
136. Nowak K., Kamler M., Bock M., et al. Bronchial artery revascularization affects graft recovery after lung transplantation. Am J Respir Crit Care Med 165 (2002) 216-220
137. Kuebler J.F., Schremmer-Danninger E., Bhoola K.D., Roscher A.A., Messmer K., and Hoffmann T.F. Kinin-B1 receptors in ischaemia-induced pancreatitis: functional importance and cellular localisation. Biol Chem 384 (2003) 1311-1319
138. Lendeckel U., Arndt M., Wrenger S., et al. Expression and activity of ectopeptidases in fibrillating human atria. J Mol Cell Cardiol 33 (2001) 1273-1281
139. Hall J.L., Grindle S., Han X.Q., et al. Genomic profiling of the human heart before and after mechanical support with a ventricular assist device reveals alterations in vascular signaling networks. Physiol Genomics 17 (2004) 283-291
140. Kim M., Lee S., Yang S.K., Song K., and Lee I. Differential expression in histologically normal crypts of ulcerative colitis suggests primary crypt disorder. Oncol Rep 16 (2006) 663-670
141. Gurcel L., Icovache I., and van der Goot F.G. Aerolysin and related Aeromonas toxins. In: Alouf J.E., and Popoff M.R. (Eds). The source book of bacterial protein toxins (2006), Elsevier Academic Press, Amsterdam 606-620
142. Gonzalez M.R., Bischofberger M., Pernot L., van der Goot F.G., and Frêche B. Bacterial pore-forming toxins: the (w)hole story?. Cell Mol Life Sci 65 (2008) 493-507
143. Geny B., and Popoff M.R. Bacterial protein toxins and lipids: role in toxin targeting and activity. Biol Cell 98 (2006) 633-651
144. Hahn Y., Bera T.K., Gehlhaus K., Kirsch I.R., Pastan I.H., and Lee B. Finding fusion genes resulting from chromosome rearrangement by analyzing the expressed sequence databases. Proc Natl Acad Sci U S A 101 (2004) 13257-13261
145. Ramaswamy S., Ross K.N., Lander E.S., and Golub T.R. A molecular signature of metastasis in primary solid tumors. Nat Genet 33 (2003) 49-54
146. Albini A., Mirisola V., and Pfeffer U. Metastasis signatures: genes regulating tumor-microenvironment interactions predict metastatic behavior. Cancer Metastasis Rev 27 (2008) 75-83
147. Overall C.M., Tam E.M., Kappelhoff R., et al. Protease degradomics: mass spectrometry discovery of protease substrates and the CLIP-CHIP, a dedicated DNA microarray of all human proteases and inhibitors. Biol Chem 385 (2004) 493-504
148. Schwartz D.R., Kardia S.L.R., Shedden K.A., et al. Gene expression in ovarian cancer reflects both morphology and biological behavior, distinguishing clear cell from other poor-prognosis ovarian carcinomas. Cancer Res 62 (2002) 4722-4729
149. Tsuda H., Ito Y.M., Ohashi Y., et al. Identification of overexpression and amplification of ABCF2 in clear cell ovarian adenocarcinomas by cDNA microarray analyses. Clin Cancer Res 11 (2005) 6880-6888
150. Haider A.S., Peters S.B., Kaporis H., et al. Genomic analysis defines a cancer-specific gene expression signature for human squamous cell carcinoma and distinguishes malignant hyperproliferation from benign hyperplasia. J Invest Dermatol 126 (2006) 869-881
151. Francis P., Namløs H.M., Müller C., et al. Diagnostic and prognostic gene expression signatures in 177 soft tissue sarcomas: hypoxia-induced transcription profile signifies metastatic potential. BMC Genomics 8 (2007) 73
152. Deddish P.A., Dragovic T., Erdös E.G., and Weber G. High concentration of neutral endopeptidase (enkephalinase E.C. 3.4.24.11) in a malignant tumor: rat hepatoma 3924A. Biochem Biophys Res Commun 169 (1990) 81-86
153. Hockley S.L., Arlt V.M., Brewer D., Giddings I., and Phillips D.H. Time- and concentration-dependent changes in gene expression induced by benzo(a)pyrene in two human cell lines, MCF-7 and HepG2. BMC Genomics 7 (2006) 260
154. Johnson S.K., Dennis R.A., Barone G.W., Lamps L.W., and Haun R.S. Differential expression of insulin-like growth factor binding protein-5 in pancreatic adenocarcinomas: identification using DNA microarray. Mol Carcinog 45 (2006) 814-827
155. Schwarze S.R., Deprimo S.E., Grabert L.M., Fu V.X., Brooks J.D., and Jarrard D.F. Novel pathways associated with bypassing cellular senescence in human prostate epithelial cells. J Biol Chem 277 (2002) 14877-14883
156. Kannan K., Amariglio N., Rechavi G., et al. DNA microarrays identification of primary and secondary target genes regulated by p53. Oncogene 20 (2001) 2225-2234
157. Cohen A.J., Skidgel R.A., Gilman L.B., et al. Carboxypeptidase M. Variable expression in normal human lung and inactivation in lung cancer. Chest 111 (1997) 149S
158. Rizzatti E.G., Falcão R.P., Panepucci R.A., et al. Gene expression profiling of mantle cell lymphoma cells reveals aberrant expression of genes from the PI3K-AKT, WNT and TGF beta signalling pathways. Br J Haematol 130 (2005) 516-526
159. Lewis C.E., and Pollard J.W. Distinct role of macrophages in different tumor microenvironments. Cancer Res 66 (2006) 605-612
160. Gottfried E., Faust S., Fritsche J., et al. Identification of genes expressed in tumor-associated macrophages. Immunobiology 207 (2003) 351-359
161. Konur A., Kreutz M., Knüchel R., Krause S.W., and Andreesen R. Three-dimensional co-culture of human monocytes and macrophages with tumor cells: Analysis of macrophage differentiation and activation. Int J Cancer 66 (1996) 645-652
162. Thomas J.G., Olson J.M., Tapscott S.J., and Zhao L.P. An efficient and robust statistical modeling approach to discover differentially expressed genes using genomic expression profiles. Genome Res 11 (2001) 1227-1236
163. Van Hemert S., Hoekman A.J.W., Smits M.A., and Rebel J.M.J. Gene expression responses to a Salmonella infection in the chicken intestine differ between lines. Vet Immunol Immunopathol 114 (2006) 247-258
164. Van Hemert S., Hoekman A.J.W., Smits M.A., and Rebel J.M.J. Immunological and gene expression responses to a Salmonella infection in the chicken intestine. Vet Res 38 (2007) 51-63
165. Tsakiris I., Soós G., Nemes Z., et al. The presence of carboxypeptidase-M in tumour cells signifies epidermal growth factor receptor expression in lung adenocarcinomas: the coexistence predicts a poor prognosis regardless of EGFR levels. J Cancer Res Clin Oncol 134 (2007) 439-451
166. Thuerigen O., Schneeweiss A., Toedt G., et al. Gene expression signature predicting pathologic complete response with gemcitabine, epirubicin, and docetaxel in primary breast cancer. J Clin Oncol 24 (2006) 1839-1845
167. 2+ on kinetic parameters of substrate hydrolysis. Biochem J 285 (1992) 613-618
168. Hadkar V., and Skidgel R.A. Carboxypeptidase D is up-regulated in RAW 264.7 macrophages and stimulates nitric oxide synthesis by cells in arginine-free medium. Mol Pharmacol 59 (2001) 1324-1332
169. Hadkar V., Sangsree S., Vogel S.M., Brovkovych V., and Skidgel R.A. Carboxypeptidase-mediated enhancement of nitric oxide production in rat lungs and microvascular endothelial cells. Am J Physiol Lung Cell Mol Physiol 287 (2004) L35-L45
170. Leatherbarrow R.J. GraFit version 5 (2001), Erithacus Software Ltd, Horley, UK
171. Erdös E.G., and Sloane E.M. An enzyme in human blood plasma that inactivates bradykinin and kallidins. Biochem Pharmacol. 11 (1962) 585-592
172. Erdös E.G., and Yang H.Y.T. Bradykinin, kallidin and kallikrein. In: Erdös E.G. (Ed). Handbook of experimental pharmacology (1970), Heidelberg, Springer 427-487
173. Regoli D., and Barabé J. Pharmacology of bradykinin and related kinins. Pharmacol Rev 32 (1980) 1-46
174. Babiuk C., Marceau F., St-Pierre S., and Regoli D. Kininases and vascular responses to kinins. Eur J Pharmacol 78 (1982) 167-174
175. Oppermann M., and Götze O. Characterization of physiological breakdown products of the complement fragment Ba. Mol Immunol 31 (1994) 307-314
176. Davrinche C., Charlionet R., Rivat C., Helal A.N., and Lefranc G. Insulin induced activation of factor B in whole serum-description of structural modifications in the Ba fragment. Eur J Immunol 14 (1984) 957-961
177. Hellwage J., Jokiranta T.S., Friese M.A., et al. Complement C3b/C3d and cell surface polyanions are recognized by overlapping binding sites on the most carboxyl-terminal domain of complement factor H. J Immunol 169 (2002) 6935-6944
178. Jokiranta T.S., Cheng Z.Z., Seeberger H., et al. Binding of complement factor H to endothelial cells is mediated by the carboxy-terminal glycosaminoglycan binding site. Am J Pathol 167 (2005) 1173-1181
179. Bokisch V., and Müller-Eberhard H. Anaphylatoxin inactivator of human plasma: its isolation and characterization as a carboxypeptidase. J Clin Invest 49 (1970) 2427-2436
180. Skidgel R.A., Kawahara M., and Hugli T.E. Functional significance of the subunits of carboxypeptidase N (kininase I). Adv Exp Med Biol 198 (1986) 375-380
181. Hugli T.E., Gerard C., Kawahara M., et al. Isolation of three separate anaphylatoxins from complement activated human serum. Mol Cell Biochem 41 (1981) 59-66
182. Klos A., Bank S., Gietz C., et al. C3a receptor on dibutyryl-cAMP-differentiated U937 cells and human neutrophils: the human C3a receptor characterized by functional responses and I-125 C3a binding. Biochemistry 31 (1992) 11274-11282
183. Caporale L.H., Tippett P.S., Erickson B.W., and Hugli T.E. The active site of C3a anaphylatoxin. J Biol Chem 255 (1980) 10758-10763
184. Zwirner J., Werfel T., Wilken H.C., Theile E., and Götze O. Anaphylatoxin C3a but not C3a(desArg) is a chemotaxin for the mouse macrophage cell line J774. Eur J Immunol 28 (1998) 1570-1577
185. Wilken H.C., Götze O., Werfel T., and Zwirner J. C3a(desArg) does not bind to and signal through the human C3a receptor. Immunol Lett 67 (1999) 141-145
186. Daffern P.J., Pfeifer P.H., Ember J.A., and Hugli T.E. C3a is a chemotaxin for human eosinophils but not for neutrophils. I. C3a stimulation of neutrophils is secondary to eosinophil activation. J Exp Med 181 (1995) 2119-2127
187. Meuer S., Ecker U., Hadding U., and Bitter-Suermann D. Platelet-serotonin release by C3a and C5a-two independent pathways of activation. J Immunol 126 (1981) 1506-1509
188. Elsner J., Oppermann M., Czech W., and Kapp A. C3a activates the respiratory burst in human polymorphonuclear neutrophilic leukocytes via pertussis toxin-sensitive G-proteins. Blood 83 (1994) 3324-3331
189. Zwirner J., Götze O., Moser A., et al. Blood- and skin-derived monocytes/macrophages respond to C3a but not to C3a(desArg) with a transient release of calcium via a pertussis toxin-sensitive signal transduction pathway. Eur J Immunol 27 (1997) 3541
190. Kreuzpaintner G., Damerau B., Zimmermann B., Plummer T.H., and Brade V. Inactivation of C3a by a monocarboxypeptidase present in culture supernatants of stimulated guinea pig peritoneal macrophages. J Immunol 136 (1986) 3384-3389
191. Kalant D., Cain S.A., Maslowska M., Sniderman A.D., Cianflone K., and Monk P.N. The chemoattractant receptor-like protein C5L2 binds the C3a des-Arg(77)/acylation-stimulating protein. J Biol Chem 278 (2003) 11123-11129
192. Fischer W.H., Jagels M.A., and Hugli T.E. Regulation of IL-6 synthesis in human peripheral blood mononuclear cells by C3a and C3a(desArg). J Immunol 162 (1999) 453-459
193. Jinsmaa Y., Takahashi M., Takahashi M., and Yoshikawa M. Anti-analgesic and anti-amnesic effect of complement C3a. Life Sci 67 (2000) 2137-2143
194. Charriaut C., Senik A., Kolb J.P., Barel M., and Frade R. Inhibition of in vitro natural killer activity by the third component of complement: role for the C3a fragment. Proc Nat Acad Sci U S A 79 (1982) 6003-6007
195. Haeffner-Cavaillon N., Cavaillon J.M., Laude M., and Kazatchkine M.D. C3a(C3a-des-arg) induces production and release of interleukin-1 by cultured human monocytes. J Immunol 139 (1987) 794-799
196. Fischer W.H., and Hugli T.E. Regulation of B cell functions by C3a and C3a(desArg)-suppression of TNF-alpha, IL-6, and the polyclonal immune response. J Immunol 159 (1997) 4279-4286
197. Mousli M., Hugli T.E., Landry Y., and Bronner C. A mechanism of action for anaphylatoxin C3a stimulation of mast cells. J Immunol 148 (1992) 2456-2461
198. Baldo A., Sniderman A.D., St-Luce S., et al. The adipsin-acylation stimulating protein system and regulation of intracellular triglyceride synthesis. J Clin Invest 92 (1993) 1543-1547
199. Tsuruta T., Yamamoto T., Matsubara S., et al. Novel function of C4a anaphylatoxin - Release from monocytes of protein which inhibits monocyte chemotaxis. Am J Pathol 142 (1993) 1848-1857
200. Fernandez H.N., and Hugli T.E. Primary structural analysis of polypeptide portion of human C5a anaphylatoxin: polypeptide sequence determination and assignment of oligosaccharide attachment site in C5a. J Biol Chem 253 (1978) 6955-6964
201. Gerard C., and Hugli T.E. Identification of classical anaphylatoxin as the des-Arg form of the C5a molecule-evidence of a modulator role for the oligosaccharide unit in human des-Arg74-C5a. Proc Nat Acad Sci U S A 78 (1981) 1833-1837
202. Hennecke M., Otto A., Baensch M., et al. A detailed analysis of the C5a anaphylatoxin effector domain: selection of C5a phage libraries on differentiated U937 cells. Eur J Biochem 252 (1998) 36-44
203. Chavkin C., and Goldstein A. Specific receptor for the opioid peptide dynorphin-structure-activity relationships. Proc Natl Acad Sci U S A 78 (1981) 6543-6547
204. Snyder K.R., Story S.C., Heidt M.E., Murray T.F., DeLander G.E., and Aldrich J.V. Effect of modification of the basic residues of dynorphin A(1-13) amide on kappa opioid receptor selectivity and opioid activity. J Med Chem 35 (1992) 4330-4333
205. Magnan J., Paterson S.J., and Kosterlitz H.W. The interaction of [Met5] enkephalin and [Leu5] enkephalin sequences, extended at the C-terminus, with the mu-, delta- and kappa-binding sites in the guinea pig brain. Life Sci 31 (1982) 1359-1361
206. Zhao M., Wang C., Liu J.G., Zhou K.X., and Peng S.Q. The composition and sequence specificity of Pro-Ala-Lys-OH for the thrombolytic activities of P6A and related oligopeptides. Bioorgan Med Chem 12 (2004) 2275-2286
207. Belew M., Gerdin B., Larsson L.E., et al. Structure-activity studies on synthetic analogs to vasoactive peptides derived from human fibrinogen. Biochim Biophys Acta 632 (1980) 87-94
208. Ebert R.F., and Bell W.R. Assay of human fibrinopeptides by high-performance liquid chromatography. Anal Biochem 148 (1985) 70-78
209. Oshima T., Currie M.G., Geller D.M., and Needleman P. An atrial peptide is a potent renal vasodilator substance. Circ Res 54 (1984) 612-616
210. Murtaugh T.J., Wright L.S., and Siegel F.L. Posttranslational modification of calmodulin in rat brain and pituitary. J Neurochem 47 (1986) 164-172
211. Perryman M.B., Knell J.D., and Roberts R. Carboxypeptidase-catalyzed hydrolysis of C-terminal lysine: mechanism for in vivo production of multiple forms of creatine kinase in plasma. Clin Chem 30 (1984) 662-664
212. Hendriks D., Soons J., Scharpé S., Wevers R., van Sande M., and Holmquist B. Identification of the carboxypeptidase responsible for the post-synthetic modification of creatine kinase in human serum. Clin Chim Acta 172 (1988) 253-260
213. George S., Ishikawa Y., Perryman M.B., and Roberts R. Purification and characterization of naturally occurring and in vitro induced multiple forms of MM creatine kinase. J Biol Chem 259 (1984) 2667-2674
214. Schlattner U., Gehring F., Vernoux N., et al. C-terminal lysines determine phospholipid interaction of sarcomeric mitochondrial creatine kinase. J Biol Chem 279 (2004) 24334-24342
215. Recny M.A., Scoble H.A., and Kim Y. Structural characterization of natural human urinary and recombinant DNA-derived erythropoietin-identification of des-arginine 166 erythropoietin. J Biol Chem 262 (1987) 17156-17163
216. Lappin T.R., Winter P.C., Elder G.E., McHale C.M., Hodges V.H., and Bridges J.M. Structure-function relationships of the erythropoietin molecule. Ann N Y Acad Sci 718 (1994) 191-202
217. Rao R.K., Koldovský O., Korc M., Pollack P.F., Wright S., and Davis T.P. Processing and transfer of epidermal growth factor in developing rat jejunum and ileum. Peptides 11 (1990) 1093-1102
218. Schaudies R.P., and Johnson J.P. Increased soluble EGF after ischemia is accompanied by a decrease in membrane-associated precursors. Am J Physiol 264 (1993) F523-F531
219. Renfrew C.A., and Hubbard A.L. Sequential processing of epidermal growth factor in early and late endosomes of rat liver. J Biol Chem 266 (1991) 4348-4356
220. Schaudies R.P., and Savage C.R. Intracellular modification of I-125 labeled epidermal growth factor by normal human foreskin fibroblasts. Endocrinology 118 (1986) 875-882
221. Hollenberg M.D., and Gregory H. Epidermal growth factor-urogastrone: biological activity and receptor binding of derivatives. Mol Pharmacol 17 (1980) 314-320
222. Calnan D.P., Fagbemi A., Berlanga-Acosta J., et al. Potency and stability of C terminal truncated human epidermal growth factor. Gut 47 (2000) 622-627
223. Davis D.A., Singer K.E., De La Luz Sierra M.D., et al. Identification of carboxypeptidase N as an enzyme responsible for C-terminal cleavage of stromal cell-derived factor-1 alpha in the circulation. Blood 105 (2005) 4561-4568
224. De La Luz Sierra M.D., Yang F.Q., Narazaki M., et al. Differential processing of stromal-derived factor-1 alpha and stromal-derived factor-1 beta explains functional diversity. Blood 103 (2004) 2452-2459
225. Fasan G., Grandgeorge M., Vigneron C., and Dellacherie E. Preparation of unaltered hemoglobin from human placentas for possible use in blood substitutes. J Biochem Biophys Methods 23 (1991) 53-66
226. Joshi A.A., and McDonald M.J. Role of alpha and beta carboxyl-terminal residues in the kinetics of human oxyhemoglobin dimer assembly. J Biol Chem 269 (1994) 8549-8553
227. Myles T., Nishimura T., Yun T.H., et al. Thrombin activatable fibrinolysis inhibitor, a potential regulator of vascular inflammation. J Biol Chem 278 (2003) 51059-51067
228. Green P.M., Ludbrook S.B., Miller D.D., Horgan C.M.T., and Barry S.T. Structural elements of the osteopontin SVVYGLR motif important for the interaction with alpha(4) integrins. FEBS Lett 503 (2001) 75-79
229. Senger D.R., and Perruzzi C.A. Cell migration promoted by a potent GRGDS-containing thrombin-cleavage fragment of osteopontin. Biochim Biophys Acta 1314 (1996) 13-24
230. Senger D.R., Perruzzi C.A., Papadopoulos-Sergiou A., and Van de Water L. Adhesive properties of osteopontin: regulation by a naturally occurring thrombin cleavage in close proximity to the GRGDS cell binding domain. Mol Biol Cell 5 (1994) 565-574
231. Reijerkerk A., Mosnier L.O., Kranenburg O., et al. Amyloid endostatin induces endothelial cell detachment by stimulation of the plasminogen activation system. Mol Cancer Res 1 (2003) 561-568
232. Hale J.E., Williamson M.K., and Price P.A. Carboxyl-terminal proteolytic processing of matrix Gla protein. J Biol Chem 266 (1991) 21145-21149
233. MacLeod T.J., Kwon M., Filipenko N.R., and Waisman D.M. Phospholipid-associated annexin A2-S100A10 heterotetramer and its subunits-characterization of the interaction with tissue plasminogen activator, plasminogen, and plasmin. J Biol Chem 278 (2003) 25577-25584
234. Kwon M.J., MacLeod T.J., Zhang Y., and Waisman D.M. S100A10, annexin A2, and annexin A2 heterotetramer as candidate plasminogen receptors. Front Biosci 10 (2005) 300-325
235. Kassam G., Le B.H., Choi K.S., et al. The p11 subunit of the annexin II tetramer plays a key role in the stimulation of t-PA-dependent plasminogen activation. Biochemistry 37 (1998) 16958-16966
236. Fogg D.K., Bridges D.E., Cheung K.K.T., et al. The p11 subunit of annexin II heterotetramer is regulated by basic carboxypeptidase. Biochemistry 41 (2002) 4953-4961
237. Wevers R.A., Boegheim J.P., Hommes O.R., et al. A study on post-synthetic modifications in alfa-alfa enolase (EC-4.2.1.11) brought about by a human serum protein. Clin Chim Acta 139 (1984) 127-135
238. Miles L.A., Dahlberg C.M., Plescia J., Felez J., Kato K., and Plow E.F. Role of cell surface lysines in plasminogen binding to cells: identification of alpha-enolase as a candidate plasminogen receptor. Biochemistry 30 (1991) 1682-1691
239. Hawley S.B., Tamura T., and Miles L.A. Purification, cloning, and characterization of a profibrinolytic plasminogen-binding protein, TIP49a. J Biol Chem 276 (2001) 179-186
240. Jackman H.L., Tan F., Schraufnagel D., et al. Plasma membrane-bound and lysosomal peptidases in human alveolar macrophages. Am J Respir Cell Mol Biol 13 (1995) 196-204