Hexapeptide fragment of carcinoembryonic antigen which acts as an agonist of heterogeneous ribonucleoprotein M

Journal of Peptide Science

Volumn 18, Issue 4, 2012, Pages 252-260

  Palermo, Nicholas Y ^a   Thomas, Peter ^a   Murphy, Richard F ^a   Lovas, Sándor ^a  

^a CREIGHTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

Carcinoembryonic antigen; HnRNP M; Minimal sequence; Molecular docking; Molecular dynamics; Replica exchange

Indexed keywords

CARCINOEMBRYONIC ANTIGEN; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN M; HEXAPEPTIDE; INTERLEUKIN 6;

ARTICLE; BIOLOGICAL ACTIVITY; CIRCULAR DICHROISM; COMPUTER MODEL; ELECTRONIC CIRCULAR DICHROISM; ENZYME LINKED IMMUNOSORBENT ASSAY; HUMAN; HUMAN CELL; MOLECULAR DOCKING; MOLECULAR DYNAMICS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN STRUCTURE; VIBRATIONAL CIRCULAR DICHROISM;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; CARCINOEMBRYONIC ANTIGEN; CELL LINE; HETEROGENEOUS-NUCLEAR RIBONUCLEOPROTEIN GROUP M; HUMANS; HYDROGEN BONDING; INTERLEUKIN-6; MOLECULAR DYNAMICS SIMULATION; PEPTIDE FRAGMENTS; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SURFACE PROPERTIES; THERMODYNAMICS;

EID: 84858863285     PISSN: 10752617     EISSN: 10991387     Source Type: Journal    
DOI: 10.1002/psc.2393     Document Type: Article

References (44)

1. Gold P, Freedman SO. Specific carcinoembryonic antigens of the human digestive system. J. Exp. Med. 1965; 122: 467-481.
2. Hammerstrom S. The carcinoembryonic antigen (CEA) family: structures, suggested functions and expression in normal and malignant tissues. Semin. Cancer Biol. 1999; 9: 67-81.
3. Thomas P, Toth CA, Saini KS, Jessup JM, Steele GD. The structure, metabolism and function of the carcinoembryonic antigen gene family. Biochim. Biophys. Acta 1990; 1032: 177-189.
4. Thomas P, Zamcheck N. Role of the liver in clearance and excretion of circulating carcinoembryonic antigen (CEA). Dig. Dis. Sci. 1983; 28: 216-224.
5. Wagner HE, Toth CA, Steele GD, Thomas P. Metastatic potential of human colon cancer cell lines: relationship to cellular differentiation and carcinoembryonic antigen production. Clin. Exp. Metastasis 1992; 10: 25-31.
6. Tibbetts LM, Doremus CM, Tzanakakis GN, Vezeridis MP. Liver metastases with 10 human colon carcinoma cell lines in nude mice and association with carcinoembryonic antigen production. Cancer 1993; 71: 315-321.
7. Hostetter RB, Augustus LB, Mankarious R, Chi K, Fan D, Toth CA, Thomas P, Jessup JM. Carcinoembryonic antigen as a selective enhancer of colorectal cancer metastasis. J. Natl. Cancer Inst. 1990; 82: 380-385.
8. Thomas P, Gangopadhyay A, Steele G, Andrews C, Nakazato H, Oikawa S, Jessup JM. The effect of transfection of the CEA gene on the metastatic behavior of the human colorectal cancer cell line MIP-101. Cancer Lett. 1995; 92: 59-66.
9. Hashino J, Fukada Y, Oikawa S, Nakazato H, Nakanishi T. Metastatic potential of human colorectal carcinoma SW1222 cells transfected with cDNA encoding carcinoembryonic antigen. Clin. Exp. Metastasis 1994; 12: 324-328.
10. Jessup JM, Petrick AT, Toth CA, Ford R, Meterissian S, O'Hara CJ, Steele G, Thomas P Carcinoembryonic antigen: enhancement of liver colonisation through retention of human colorectal carcinoma cells. Br. J. Cancer 1993; 67: 464-470.
11. Gangopadhyay A, Lazure DA, Thomas P. Adhesion of colorectal carcinoma cells to the endothelium is mediated by cytokines from CEA stimulated Kupffer cells. Clin. Exp. Metastasis 1998; 16: 703-712.
12. Langley RR, Fidler IJT. Tumor cell-organ microenvironment interactions in the pathogenesis of cancer metastasis. Endocrine Revs. 2007; 28: 297-321.
13. Gangopadhyay A, Bajenova O, Kelly TM, Thomas P. Carcinoembryonic antigen induces cytokine expression in Kupffer cells: implications for hepatic metastasis from colorectal cancer. Cancer Res. 1996; 56: 4805-4810.
14. Toth CA, Thomas P, Broitman SA, Zamcheck N. Receptor-mediated endocytosis of carcinoembryonic antigen by rat liver Kupffer cells. Cancer Res. 1985; 45: 392-397.
15. Edmiston K, Gangopadhyay A, Shoji Y, Nachman A, Thomas P, Jessup JM. In vivo induction of murine cytokine production by carcinoembryonic antigen. Cancer Res. 1997; 57: 4432-4436.
16. Bajenova OV, Zimmer R, Stolper E, Salisbury-Rowswell J, Nanji A, Thomas P. Heterogeneous RNA-binding protein M4 is a receptor for carcinoembryonic antigen in Kupffer cells. J. Biol. Chem. 2001; 276: 31067-31073.
17. Kim JH, Hahm B, Kim YK, Choi M, Jang SK. Protein-protein interaction among hnRNPs shuttling between nucleus and cytoplasm. J. Mol. Biol. 2000; 298: 395-405.
18. Dreyfuss G, Kim VN, Kataoka N. Messenger-RNA-binding proteins and the messages they carry. Nat. Rev. Mol. Cell Biol. 2002; 3: 195-205.
19. Bajenova O, Stolper E, Gapon S, Sundina N, Zimmer R, Thomas P. Surface expression of heterogeneous nuclear RNA binding protein M4 on Kupffer cell relates to its function as a carcinoembryonic antigen receptor. Exp. Cell Res. 2003; 291: 228-241.
20. Gangopadhyay A, Thomas P. Processing of carcinoembryonic antigen by Kupffer cells: recognition of a penta-peptide sequence. Arch. Biochem. Biophys. 1996; 334: 151-157.
21. Bates PA, Luo J, Sternberg JE. A predicted three-dimensional structure for the carcinoembryonic antigen (CEA). FEBS Lett. 1992; 301: 207-214.
22. Zimmer R, Thomas P. Mutations in the carcinoembryonic antigen gene in colorectal cancer patients: implications on liver metastasis. Cancer Res. 2001; 61: 2822-2826.
23. Palermo NY, Csontos J, Murphy RF, Lovas S. Role of aromatic residues in stabilizing the secondary and tertiary structure of avian pancreatic polypeptide. Int. J. Quant. Chem. 2008; 108: 814-819.
24. Hatfield MPD, Palermo NY, Csontos J, Murphy RF, Lovas S. Quantum chemical quantification of weakly polar interaction energies in the TC5b miniprotein. J. Phys. Chem. B 2008; 112: 3503-3508.
25. Korotkova N, Yang Y, Le Trong I, Cota E, Demeler B, Marchant J, Thomas WE, Stenkamp RE, Moseley SL, Matthews S. Binding of Dr adhesins of Escherichia coli to carcinoembryonic antigen triggers receptor dissociation. Mol. Microbiol. 2008; 67: 420-434.
26. Boehm MK, Perkins SJ. Structural models for carcinoembryonic antigen and its complex with the single-chain Fv antibody molecule MFE23. FEBS Lett. 2000; 475: 11-16
27. Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE. The protein data bank. Nucleic Acids Res. 2000; 28: 235-242.
28. Szendrei GI, Fabian H, Mantsch HH, Lovas S, Nyeki O, Schon I, Otvos L, Jr. Aspartate-bond isomerization affects the major conformations of synthetic peptides. Eur. J. Biochem. 1994; 226: 917-924.
29. van der Spoel D, Lindahl E, Hess B, Groenhof G, Mark AE, Berendsen HJC. GROMACS: fast, flexible, and free. J. Comput. Chem. 2005; 26: 1701-1718.
30. Sugita Y, Okamoto Y. Replica-exchange molecular dynamics method for protein folding. Chem. Phys. Lett. 1999; 314: 141-151.
31. Patriksson A, van der Spoel D. A temperature predictor for parallel tempering simulations. Phys. Chem. Chem. Phys. 2008; 10: 2073-2077.
32. Jorgensen WL, Chandrasekhar J, Madura JD, Impey RW, Klein ML. Comparison of simple potential functions for simulating liquid water. J. Chem. Phys. 1983; 79: 926-935.
33. Kaminski GA, Friesner RA, Tirado-Rives J, Jorgensen WL. Evaluation and reparametrization of the OPLS-AA force field for proteins via comparison with accurate quantum chemical calculations on peptides. J. Phys. Chem. B 2001; 105: 6474-6487.
34. Daura X, Gademann K, Jaun B, Seebach D, van Gunsteren WF, Mark AE. Peptide folding: when simulation meets experiment. Angew. Chem. Int. Ed Engl. 1999; 38: 236-240.
35. Glide, Version 4.5. Schrödinger, LLC: New York, NY, 2007.
36. Kabsch W, Sander C. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 1983; 22: 2577-2637.
37. de Groot BL, Amadei A, van Aalten DMF, Berendsen HJC. Towards an exhaustive sampling of the configurational spaces of the two forms of the peptide hormone guanylin. J. Biomol. Struct. Dynam. 1996; 13: 741-751.
38. Wassenaar TA, Quax WJ, Mark AE. The conformation of the extracellular binding domain of Death Receptor 5 in the presence and absence of the activating ligand TRAIL: a molecular dynamics study. Proteins 2008; 70: 333-343.
39. Eisenhaber F, Lijnzaad P, Argos, P, Sander C, Scharf M. The double cubic lattice method: efficient approaches to numerical integration of surface area and volume and to dot surface contouring of molecular assemblies. J. Comput. Chem. 1995; 16: 273-284.
40. Rucker AL, Creamer TP. Polyproline II helical structure in protein unfolded states: lysine peptides revisited. Protein Sci. 2002; 11: 980-985.
41. Dukor RK, Keiderling TA. Reassessment of the random coil conformation: vibrational CD study of proline oligopeptides and related polypeptides. Biopolymers 1991; 31: 1747-1761.
42. Jung C. Insight into protein structure and protein-ligand recognition by Fourier transform infrared spectroscopy. J. Mol. Recognit. 2000; 13: 325-351.
43. Dukor RK, Keiderling TA. Mutarotation studies of poly-L-proline using FTIR, electronic and vibrational circular dichroism. Biospectroscopy 1996; 2: 83-100.
44. London N, Movshovitz-Attias D, Schueler-Furman O. The structural basis of peptide-protein binding strategies. Structure 2010; 18: 188-199.