Endorepellin, the C-terminal angiostatic module of perlecan, enhances collagen-platelet responses via the α2β1-integrin receptor

Blood

Volumn 109, Issue 9, 2007, Pages 3745-3748

  Bix, Gregory ^a   Iozzo, Rex A ^a   Woodall, Ben ^a   Burrows, Michelle ^a   McQuillan, Angela ^a   Campbell, Shelly ^a   Fields, Gregg B ^b   Iozzo, Renato V ^a  

^a THOMAS JEFFERSON UNIVERSITY   (United States)

^b FLORIDA ATLANTIC UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ANGIOSTATIC PROTEIN; COLLAGEN; ENDOREPELLIN; PEPTIDE FRAGMENT; PERLECAN; PROTEIN ANTIBODY; PROTEIN TYROSINE KINASE; UNCLASSIFIED DRUG; VERY LATE ACTIVATION ANTIGEN 2;

ARTICLE; CELL DIFFERENTIATION; CELL TYPE; IN VIVO STUDY; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN FUNCTION; PROTEIN INTERACTION; THROMBOCYTE ACTIVATION; THROMBOCYTE ADHESION;

EID: 34247330149     PISSN: 00064971     EISSN: 00064971     Source Type: Journal    
DOI: 10.1182/blood-2006-08-039925     Document Type: Article

References (25)

1. Iozzo RV, Murdoch AD. Proteoglycans of the extracellular environment: clues from the gene and protein side offer novel perspectives in molecular diversity and function. FASEB J. 1996;10:598-614.
2. Iozzo RV. Matrix proteoglycans: from molecular design to cellular function. Annu Rev Biochem. 1998;67:609-652.
3. Mongiat M, Sweeney S, San Antonio JD, Fu J, Iozzo RV. Endorepellin, a novel inhibitor of angiogenesis derived from the C terminus of perlecan. J Biol Chem. 2003;278:4238-4249.
4. Gonzalez EM, Reed CC, Bix G, et al. BMP-1/Tolloid-like metalloproteases process endorepellin, the angiostatic C-terminal fragment of perlecan. J Biol Chem. 2005;280:7080-7087.
5. Bix G, Fu J, Gonzalez E, et al. Endorepellin causes endothelial cell disassembly of actin cytoskeleton and focal adhesions through the α2β1 integrin. J Cell Biol. 2004;166:97-109.
6. Bix G, Iozzo RV. Matrix revolutions: "tails" of basement-membrane components with angiostatic functions. Trends Cell Biol. 2005;15:52-60.
7. Iozzo RV. Basement membrane proteoglycans: from cellar to ceiling. Nature Rev Mol Cell Biol. 2005;6:646-656.
8. Calderwood DA, Shattil SJ, Ginsberg MH. Integrins and actin filaments: reciprocal regulation of cell adhesion and signaling. J Biol Chem. 2000;275:22607-22610.
9. Senger DR, Perruzzi CA, Streit M, et al. The α1β1 and α2β1 integrins provide critical support for vascular endothelial growth factor signaling, endothelial cell migration, and tumor angiogenesis. Am J Pathol. 2002;160:195-204.
10. Eble JA. Collagen-binding integrins as pharmaceutical targets. Curr Pharm Design. 2005;11:867-880.
11. Holtkötter O, Nieswandt B, Smyth N, et al. Integrin α2-deficient mice develop normally, are fertile, but display partially defective platelet interaction with collagen. J Biol Chem. 2002;277:10789-10794.
12. Zhang ZG, Bothe I, Hirche F, et al. Interactions of primary fibroblasts and keratinocytes with extracellular matrix proteins: contribution of α2β1 integrin. J Cell Sci. 2006;119:1886-1895.
13. Oda O, Shinzato T, Ohbayashi K, et al. Purification and characterization of perlecan fragment in urine of end-stage renal failure patients. Clin Chim Acta. 1996;255:119-132.
14. Vuadens F, Benay C, Crettaz D, et al. Identification of biologic markers of the premature rupture of fetal membranes: proteomic approach. Proteomics. 2003;3:1521-1525.
15. Thadikkaran L, Crettaz D, Siegenthaler MA, et al. The role of proteomics in the assessment of premature rupture of fetal membranes. Clinica Chimica Acta. 2005;360:27-36.
16. Pieper R, Gatlin CL, McGrath AM, et al. Characterization of the human urinary proteome: a method for high-resolution display of urinary proteins on two-dimensional electrophoresis gels with a yield of nearly 1400 distinct protein spots. Proteomics. 2004;4:1159-1174.
17. Adkins JN, Varnum SM, Auberry KJ, et al. Toward a human blood serum proteome: analysis by multidimensional separation coupled with mass spectrometry. Mol Cell Proteom. 2002;1:947-955.
18. Laplante P, Raymond M-A, Labelle A, et al. Perlecan proteolysis induces α2β1 integrin and src-family kinases dependent anti-apoptotic pathway in fibroblasts in the absence of focal adhesion kinase activation. J Biol Chem. 2006;281:30383-30392.
19. Arias-Salgado EG, Lizano S, Sarkar S, et al. Src kinase activation by direct interaction with the integrin β cytoplasmic domain. Proc Natl Acad Sci U S A. 2003;100:13295-13302.
20. c-src-specific tyrosine kinase activity. Proc Natl Acad Sci U S A. 1986;83:852-856.
21. Inoue O, Suzuki-Inoue K, Dean WL, Frampton J, Watson SP. Integrin α2β1 mediates outside-in regulation of platelet spreading on collagen through activation of Src kinases and PLCγ2. J Cell Biol. 2003;160:769-780.
22. Farndale RW. Collagen-induced platelet activation. Blood Cells Mol Dis. 2006;36:162-165.
23. Jung SM, Moroi M. Platelets interact with soluble and insoluble collagens through characteristically different reactions. J Biol Chem. 1998;273:14827-14837.
24. Chen H, Kahn ML. Reciprocal signaling by integrin and nonintegrin receptors during collagen activation of platelets. Mol Cell Biol. 2003;23:4764-4777.
25. Van de Walle GR, Vanhoorelbeke K, Majer Z, et al. Two functional active conformations of the integrin α2β1, depending on activation condition and cell type. J Biol Chem. 2005;280:36873-36882.