The interaction of angiocidin with tissue transglutaminase

Experimental and Molecular Pathology

Volumn 88, Issue 1, 2010, Pages 15-25

  L'Heureux, Darryl Z ^a   Rothman, Vicki L ^a   Tuszynski, George P ^a  

^a TEMPLE UNIVERSITY   (United States)

Author keywords

Angiocidin; Angiogenesis; Endothelial cells; Tissue transglutaminase; Tumor progression

Indexed keywords

ANGIOCIDIN; ANGIOGENESIS INHIBITOR; FIBRONECTIN; MONOMER; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE; UNCLASSIFIED DRUG;

ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; ANTIANGIOGENIC ACTIVITY; ARTICLE; CANCER CELL; CELL MIGRATION; CELLULAR DISTRIBUTION; CONCENTRATION RESPONSE; CONTROLLED STUDY; ENDOTHELIUM CELL; EXTRACELLULAR MATRIX; HUMAN; HUMAN CELL; LEWIS CARCINOMA; MOUSE; NONHUMAN; PROTEIN CROSS LINKING; PROTEIN PROTEIN INTERACTION; TUMOR GROWTH; TUMOR REGRESSION;

ANIMALS; BREAST NEOPLASMS; CARRIER PROTEINS; CELL ADHESION; CELL LINE; CELL MOVEMENT; CHILD; ENDOTHELIAL CELLS; EXTRACELLULAR MATRIX; FIBRONECTINS; GENE DELETION; GTP-BINDING PROTEINS; GUINEA PIGS; HUMANS; NEOVASCULARIZATION, PATHOLOGIC; PROTEIN BINDING; RECOMBINANT PROTEINS; TRANSGLUTAMINASES;

EID: 74749083436     PISSN: 00144800     EISSN: 10960945     Source Type: Journal    
DOI: 10.1016/j.yexmp.2009.11.001     Document Type: Article

References (43)

1. Aeschlimann D., and Paulsson M. Cross-linking of laminin-nidogen complexes by tissue transglutaminase. A novel mechanism for basement membrane stabilization. J. Biol. Chem. 266 (1991) 15308-15317
2. Akerman M.E., et al. Angiostatic peptides use plasma fibronectin to home to angiogenic vasculature. Proc. Natl. Acad Sci. U. S. A. 102 (2005) 2040-2045
3. Akimov S.S., et al. Tissue transglutaminase is an integrin-binding adhesion coreceptor for fibronectin. J. Cell Biol 148 (2000) 825-838
4. Arnoletti J.P., et al. Computer-assisted image analysis of tumor sections for a new thrombospondin receptor. Am. J. Surg. 168 (1994) 433-436
5. Bale M.D., and Mosher D.F. Thrombospondin is a substrate for blood coagulation factor XIIIa. Biochemistry 25 (1986) 5667-5673
6. Barsigian C., et al. Tissue (type II) transglutaminase covalently incorporates itself, fibrinogen, or fibronectin into high molecular weight complexes on the extracellular surface of isolated hepatocytes. Use of 2-[(2-oxopropyl)thio] imidazolium derivatives as cellular transglutaminase inactivators. J. Biol. Chem. 266 (1991) 22501-22509
7. Belkin A.M., et al. Matrix-dependent proteolysis of surface transglutaminase by membrane-type metalloproteinase regulates cancer cell adhesion and locomotion. J. Biol. Chem. 276 (2001) 18415-18422
8. Brown M.C., et al. Angiostatic activity of obtustatin as alpha1beta1 integrin inhibitor in experimental melanoma growth. Int. J. Cancer 123 (2008) 2195-2203
9. Deveraux Q., et al. Molecular cloning and expression of a 26 S protease subunit enriched in dileucine repeats. J. Biol. Chem 270 (1995) 23726-23729
10. Dimitrov S., et al. The endothelial apoptotic activity of angiocidin is dependent on its polyubiquitin binding activity. Br. J. Cancer 93 (2005) 662-669
11. Esposito C., et al. Tissue transglutaminase and celiac disease. Prog. Exp. Tumor Res. 38 (2005) 158-173
12. Fok J.Y., et al. Implications of tissue transglutaminase expression in malignant melanoma. Mol. Cancer Ther. 5 (2006) 1493-1503
13. Folkman J. Role of angiogenesis in tumor growth and metastasis. Semin. Oncol. 29 (2002) 15-18
14. Folkman J. Angiogenesis. Annu. Rev. Med. 57 (2006) 1-18
15. Gaurnier-Hausser A., et al. The novel angiogenic inhibitor, angiocidin, induces differentiation of monocytes to macrophages. Cancer Res. 68 (2008) 5905-5914
16. Gaurnier-Hausser A., and Tuszynski G.P. The immunomodulatory role of angiocidin, a novel angiogenesis inhibitor. Curr. Pharm. Des. 15 (2009) 1937-1948
17. Johansson E., et al. Identification of an active site in the antisecretory factor protein. Biochim. Biophys. Acta. 1362 (1997) 177-182
18. Johansson E., et al. Molecular cloning and expression of a pituitary gland protein modulating intestinal fluid secretion. J. Biol. Chem. 270 (1995) 20615-20620
19. Lee J., et al. Transglutaminase 2 induces nuclear factor-kappaB activation via a novel pathway in BV-2 microglia. J. Biol. Chem. 279 (2004) 53725-53735
20. Mangala L.S., and Mehta K. Tissue transglutaminase (TG2) in cancer biology. Prog. Exp. Tumor Res. 38 (2005) 125-138
21. Mann A.P., et al. Overexpression of tissue transglutaminase leads to constitutive activation of nuclear factor-kappaB in cancer cells: delineation of a novel pathway. Cancer Res. 66 (2006) 8788-8795
22. Mehta K. Biological and therapeutic significance of tissue transglutaminase in pancreatic cancer. Amino. Acids 36 (2009) 709-716
23. Mosher D.F., and Johnson R.B. Specificity of fibronectin-fibrin cross-linking. Ann. N. Y. Acad Sci. 408 (1983) 583-594
24. Nilsson L.A., et al. Induction of anti-secretory factor in mice by the nonintestinal parasite Schistosoma mansoni. J. Parasitol. 78 (1992) 1055-1058
25. Pisano J.J., et al. [Cross-link in fibrin polymerized by factor 13: epsilon-(gamma-glutamyl)lysine.]. Science 160 (1968) 892-893
26. Poon R.T., et al. Clinical significance of thrombospondin 1 expression in hepatocellular carcinoma. Clin. Cancer Res. 10 (2004) 4150-4157
27. Ruoslahti E. Fibronectin and its integrin receptors in cancer. Adv. Cancer Res. 76 (1999) 1-20
28. Sabherwal Y., et al. Integrin alpha2beta1 mediates the anti-angiogenic and anti-tumor activities of angiocidin, a novel tumor-associated protein. Exp. Cell Res. 312 (2006) 2443-2453
29. Sabherwal Y., et al. Clinical significace of serum angiocidin levels in hepatocellular carcinoma. Proc. Am. Assoc. Cancer Res. 46 (2005) 1319
30. Sabherwal Y., et al. Clinical significance of serum angiocidin levels in hepatocellular carcinoma. Cancer Lett. 251 (2007) 28-35
31. Sane D.C., et al. Roles of transglutaminases in cardiac and vascular diseases. Front. Biosci. 12 (2007) 2530-2545
32. Siegel M., and Khosla C. Transglutaminase 2 inhibitors and their therapeutic role in disease states. Pharmacol. Ther. 115 (2007) 232-245
33. Summey Jr. B.T., et al. Tissue transglutaminase localization and activity regulation in the extracellular matrix of articular cartilage. J. Orthop. Res. 20 (2002) 76-82
34. Tuszynski G.P., and Nicosia R.F. Localization of thrombospondin and its cysteine-serine-valine-threonine-cysteine-glycine-specific receptor in human breast carcinoma. Lab. Invest. 70 (1994) 228-233
35. Tuszynski G.P., et al. Biological activities of peptides and peptide analogues derived from common sequences present in thrombospondin, properdin, and malarial proteins. J. Cell Biol. 116 (1992) 209-217
36. Tuszynski G.P., et al. Identification and characterization of a tumor cell receptor for CSVTCG, a thrombospondin adhesive domain. J. Cell Biol. 120 (1993) 513-521
37. Tuszynski G.P., et al. The interaction of human platelet thrombospondin with fibrinogen. Thrombospondin purification and specificity of interaction. J. Biol. Chem. 260 (1985) 12240-12245
38. Verma A., and Mehta K. Tissue transglutaminase-mediated chemoresistance in cancer cells. Drug Resist. Updat 10 (2007) 144-151
39. Verma A., et al. Increased expression of tissue transglutaminase in pancreatic ductal adenocarcinoma and its implications in drug resistance and metastasis. Cancer Res 66 (2006) 10525-10533
40. Wakiyama T., et al. The localization of thrombospondin-1 (TSP-1), cysteine-serine-valine-threonine-cysteine-glycine (CSVTCG) TSP receptor, and matrix metalloproteinase-9 (MMP-9) in colorectal cancer. Histol. Histopathol. 16 (2001) 345-351
41. Young P., et al. Characterization of two polyubiquitin binding sites in the 26 S protease subunit 5a. J. Biol. Chem. 273 (1998) 5461-5467
42. Yuan L., et al. Tissue transglutaminase 2 inhibition promotes cell death and chemosensitivity in glioblastomas. Mol. Cancer Ther. 4 (2005) 1293-1302
43. Zhou J., et al. Cloning and characterization of angiocidin, a tumor cell binding protein for thrombospondin-1. J. Cell Biochem. 92 (2004) 125-146