Integrins: cell adhesion molecules in cancer

Bibliography

• FAASSEN AE, DRAKE SL, IIDA J, KNUTSON JR, MCCARTHY JB: Mechanisms of normal cell adhesion to the extra-cellular matrix and alterations associated with tumor invasion and metastasis. Adv. Pathol. Lab. Med. (1992) 5:229–259.
   Google Scholar
• SONNENBERG A: Integrins and their ligands. Curr. Top-ics Microbiol. Immunol (1993) 184:7–35.
   PubMedGoogle Scholar
• HYNES RO: Integrins: versatility, modulation, and sig-nalling in cell adhesion. Cell (1992) 69:11–25.
   PubMed Web of Science ®Google Scholar
• SCHWARTZ MA, SCHALLER MD, GINSBERG MH: In-tegrins: emerging paradigms of signal transduction. Ann. Rev. Cell Dev. Biol. (1995) 11:549–599.
   PubMed Web of Science ®Google Scholar
• O'TOOLE TE: Integrin signalling: building connections beyond the focal contact? MatrixBiol. (1997) 16:165–171.
   Google Scholar
• HEAVNER GA: Active sequences in cell adhesion mole-cules: targets for therapeutic intervention. Drug Design Today (1996) 1:295–304.
   Web of Science ®Google Scholar
• RUOSLAHTI E: Integrins as signalling molecules and targets for tumor therapy. Kidney Int. (1997) 51:1414–1417.
   Google Scholar
• WOODHOUSE EC, CHUAQUI RF, LIOTTA LA: General mechanisms of metastasis. Cancer (1997) 80:1529–1537.
   PubMed Web of Science ®Google Scholar
• KUHN K, EBLE J: The structural bases of integrin-ligand interactions. Trends Cell Biol. (1994) 4:256–261.
   PubMedGoogle Scholar
• HUMPHRIES MJ: The molecular basis and specificty of integrin-ligand interactions. J. Cell ScL (1990) 97:585–592.
   PubMed Web of Science ®Google Scholar
• YAMADA KM: Adhesive recognition sequences. J. Biol. Chem. (1991) 266:12809–12812.
   PubMed Web of Science ®Google Scholar
• FIELDS GB: Synthetic peptides and tumor cell metasta-sis. Peptide Res. (1993) 6:115–120.
   PubMedGoogle Scholar
• PASQUALINI R, KOIVUNEN E, RUOSLAHTI E: Peptides in cell adhesion: powerful tools for the study of integrin- ligand interactions. Brazilian J. Med. Biol. Res. (1996) 29:1151–1158.
   PubMed Web of Science ®Google Scholar
• DIAZ-GONZALEZ F, FORSYTH J, STEINER B, GINSBERG,MH: Trans-dominant inhibition of integrin function. Mol. Biol. Cell. (1996) 7:1939–1951.
   PubMed Web of Science ®Google Scholar
• RUOSLAHTI E: Fibronectin and its receptors. Ann. Rev.Biochem. (1988) 57:375–413.
   PubMed Web of Science ®Google Scholar
• BARON C, MAYO K, SKUBITZ, APN, FURCHT, LT: NMR as-signment and secondary structure of the cell adhesion Type III module of fibronectin. Biochemistry (1992) 31:2068–2073.
   PubMed Web of Science ®Google Scholar
• PIERSCHBACHER MD, RUOSLAHTI E: Cell attachment ac-tivity of fibronectin can be duplicated by small syn-thetic fragments of the molecule. Nature (1984) 309:30–33.
   PubMed Web of Science ®Google Scholar
• GEHLSEN KR, ARGRAVES WS, PIERSCHBACHER MD, RUO-SLAHTI E: Inhibition of in vitro tumor cell invasion by Arg-Gly-Asp-containing synthetic peptides. J. Cell Biol. (1988) 106:925–930.
   PubMed Web of Science ®Google Scholar
• HUMPHRIES MJ, OLDEN K, YAMADA, KM: A syntheticpeptide from fibronectin inhibits experimental metas-tasis of murine melanoma cells. Science (1986) 233:467–470.
   PubMed Web of Science ®Google Scholar
• JOHNSON WC, PAGANO TG, BASSON CT et al.: Biologi-cally active Arg-Gly- Asp oligopeptides assume a Type II tl-turn in solution. Biochemistry (1993) 32:268–273.
   PubMedGoogle Scholar
• KUMAGAI H, TAJIMA M, UENO Y, GIGA-HAMA Y, OHBA M: Effect of cyclic RGD peptide on cell adhesion and tu-mor metastasis. Biochem. Biophys. Res. Commun. (1991) 177:74–82.
   PubMed Web of Science ®Google Scholar
• D'SOUZA SE, GINSBERG MH, PLOW EF: Arginyl-glycyl-aspartic acid (RGD): a cell adhesion motif. Trends Bio-med. ScL (1991) 16:246–250.
   PubMed Web of Science ®Google Scholar
• RUOSLAHTI E: Integrins as receptors for extracellularmatrix. In: Cell Biology of the Extracellular Matrix. May ED (Ed.), Plenum Press, New York (1991):343–363.
   Google Scholar
• PIERSCHBACHER MD, RUOSLAHTI E: Influence of stereochemistry of the sequence Arg-Gly-Asp-Xaa on binding specificity in cell adhesion. J. Biol. Chem. (1987) 262:17297–17298.
   Google Scholar
• AUMAILLEY M, GURRATH M, MULLER G et al.: Arg-Gly-Asp constrained within cyclic pentapeptides. FEBS Lett. (1991) 291:50–54.
   PubMed Web of Science ®Google Scholar
• PFAFF M, TANGEMANN K, MULLER B et al.: Selective rec-ognition of cyclic RGD peptides of NMR defined con-formation by a1Ib,613, aV,613, and a5,611 integrins. J. Biol. Chem. (1994) 269:20233–20238.
   PubMed Web of Science ®Google Scholar
• SAGE EH: Pieces of eight: bioactive fragments of extra-cellular proteins as regulators of angiogenesis. Trends Cell Biol. (1997) 7:182–186.
   Google Scholar
• KOIVUNEN E, GAY DA, RUOSLAHTI E: Selection of pep-tides binding to the a5,31 integrin from phage display library. J. Biol. Chem. (1993) 268:20205–20210.
   PubMed Web of Science ®Google Scholar
• KOIVUNEN E, WANG B, RUOSLAHTI E: Isolation of a highly specific ligand for the a5,611 integrin from a phage display library. J. Cell Biol. (1994) 124:373–380.
   PubMed Web of Science ®Google Scholar
• KOIVUNEN E, WANG B, RUOSLAHTI E: Phage libraries displaying cyclic peptides with different ring sizes: ligand specificities of the RGD-directed integrins. Bio-technology (1995) 13:265–270.
   PubMedGoogle Scholar
• MOULD AP, ASHARI JA, CRAIG, SE et al.: Integrin a4,81-mediated melanoma cell adhesion and migration on vascular cell adhesion molecule-1 (VCAM-1) and the al-ternatively spliced IIICS region of fibronectin. j Biol Chem. (1994) 269:27224–27230.
   PubMed Web of Science ®Google Scholar
• HUMPHRIES MJ, KOMORIY A, AKIYAMA SK, OLDEN K,YAMADA KM: Identification of two distinct regions of the Type IIICS connecting segment of human plasma fibronectin that promote cell type-specific adhesion. J. Biol. Chem. (1987) 262:6886–6892.
   PubMed Web of Science ®Google Scholar
• MOULD AP, WHELDON LA, KOMORIYAMA A et al.: Affin-ity chromatographic isolation of the melanoma cell adhesion receptor for the IIICS region of fibronectin and its identification as the integrin a4,611. J. Biol. Chem. (1990) 265:4020–4024.
   PubMed Web of Science ®Google Scholar
• YAMAMOTO S, KANEDA Y, OKADA N et al.: Antimeta-static effects of synthetic peptides containing the core sequence of the Type III connecting segment domain III (CS) of fibronectin. AntiCancer Drugs (1994) 5:424–428.
   Google Scholar
• MCCARTHY JB, CHELBERG MK, MICKELSON DJ, FURCHTLT: Localization and chemical synthesis of fibronectin peptides with melanoma adhesion and heparin bind-ing activities. Biochemistry (1988) 27:1380–1388.
   PubMedGoogle Scholar
• IIDA J, SKUBITZ APN, FURCHT LT, WAYNER E, MCCAR-THY JB: Coordinate role for cell surface chondroitin sulfate proteoglycan and a4,611 integrin in mediating melanoma cell adhesion to fibronectin. J. Cell Biol. (1992) 118:431–444.
   Google Scholar
• DRAKE SL, VARNUM J, MAYO KH et al.: Structural fea-tures of fibronectin synthetic peptide FN-C/H II, re-sponsible for cell adhesion, neurite extension, and heparan sulfate binding. J. Biol. Chem. (1993) 268:15859–15867.
   Google Scholar
• PASQUALINI R, BOURDOULOUS S, KOIVUNEN E, WOODS VL, RUOSLAHTI E: A polymeric form of fi-bronectin has antimetastatic effects against multiple tumor types. Nature Med. (1996) 2:1197–1203.
   PubMed Web of Science ®Google Scholar
• CARDARELLI PM, COBB RR, NOWLIN, DM et al.: CyclicRGD peptide inhibits a4,611 interaction with connect-ing segment 1 and vascular cell adhesion molecule. J. Biol. Chem. (1994) 269:18668–18673.
   PubMed Web of Science ®Google Scholar
• NOWLIN DM, GORCSAN F, MOSCINSKI M et al.: A novelcyclic pentapeptide inhibits a4,611 and a5,611 integrin-mediated cell adhesion. J. Biol. Chem. (1993) 268:20352–20359.
   PubMed Web of Science ®Google Scholar
• PATTARMALAI S, SKUBITZ KM, SKUBITZ APN: A novelrecognition site on laminin for the a3,611 integrin. Exp. Cell Res. (1996) 222:281–290.
   Google Scholar
• GEHLSEN KR, SRIRAMARAO P, FURCHT LT, SKUBITZ APN:A synthetic peptide derived from the carboxy termi-nus of the laminin A chain represents a binding site for the AO 1 integrin. J. Cell Biol. (1992) 117:449–459.
   PubMed Web of Science ®Google Scholar
• UNDERWOOD PA, BENNETT FA, KIRKPATRICK A, BEANPA, MOSS BA: Evidence for the location of a binding se-quence for the a2,611 integrin of endothelial cells, in the, 611 subunit of laminin. Biochem. J. (1995) 309:765–771.
   Google Scholar
• STAATZ WD, FOK KF, ZUTTER MM et al.: Identification of a tetrapeptide recognition sequence for the a2,611 in-tegrin in collagen. J. Biol. Chem. (1991) 266:7363–7367.
   PubMed Web of Science ®Google Scholar
• QIAN JJ, BHATNAGAR RS: Enhanced cell attachment to anorganic bone mineral in the presence of a synthetic peptide related to collagen. J. Biomed. Materials Res. (1996) 31:545–554.
   PubMedGoogle Scholar
• BHATNAGAR RS, QIAN JJ, GOUGH CA: The role in cell binding of a tl-bend within the triple helical region in collagen (a 10 chain: structural and biological evi-dence for conformational tautomerism on fiber sur-face. J. Biomol. Struct. Dynam. (1997) 14:547–560.
   PubMed Web of Science ®Google Scholar
• GRAB B, MILES AJ, FURCHT LT, FIELDS GB: Promotion of fibroblast adhesion by triple-helical peptide models of Type I collagen-derived sequences. J. Biol. Chem. (1996) 271:12234–12240.
   PubMed Web of Science ®Google Scholar
• CHELBERG MK, MCCARTHY JB, SKUBITZ APN, FURCHTLT, TSILIBARY EC: Characterization of a synthetic pep-tide from Type IV collagen that promotes melanoma cell adhesion, spreading, and motility. J. Cell Biol. (1990) 111:261–270.
   PubMed Web of Science ®Google Scholar
• MAYO KH, PARRA-DIAZ D, MCCARTHY JB, CHELBERG M:Cell adhesion promoting peptide GVKGDKGNPG-WPGAP from the collagen Type IV triple helix. Biochemistry (1991) 30:8251–8267.
   PubMed Web of Science ®Google Scholar
• FIELDS CG, MICKELSON DJ, DRAKE SL, MCCARTHY, JB,FIELDS GB: Melanoma cell adhesion and spreading ac-tivities of a synthetic 124-residue triple-helical 'mini-collagen'. J Biol. Chem. (1993) 268:14153–14160.
   PubMed Web of Science ®Google Scholar
• YU Y-C, PAKALNS T, DORI Y et al.: Construction of bio-logically active protein molecular architecture using self-assembling peptide-amphiphiles. Meth. Enzymol. (1997) 289:571–587.
   Google Scholar
• KNUTSON JR, FIELDS GB, IIDA J, MILES AJ, MCCARTHY JB:A Type IV collagen-derived synthetic peptide, IV-H1, interacts with human melanoma CD44/chondroitin sulfate proteoglycan and inhibits invasion of base-ment membranes. Proc. Am. Assoc. Cancer Res. (1995) 36.
   Google Scholar
• LESLEY J, HYMAN R, ENGLISH N, CATTERALL JB, TURNERGA: CD44 in inflammation and metastasis. Glycoconju-gate J. (1997) 14:611–622.
   PubMed Web of Science ®Google Scholar
• KINCADE PW, ZHENG Z, KATOH S, HANSON L: The im-portance of cellular environment to function of the CD44 matrix receptor. Curr. Opin. Cell Biol. (1997) 9:635–642.
   PubMed Web of Science ®Google Scholar
• FAASSEN AE, SCHRAGER JA, KLEIN DJ et al. A cell surface chondroitin sulfate proteoglycan, immunologically related to CD44, is involved in Type I collagen- mediated melanoma cell motility and invasion. J. Cell Biol. (1992) 116:521–531.
   PubMed Web of Science ®Google Scholar
• KNUTSON JR, IIDA J, FIELDS GB, MCCARTHY JB:CD44/chondroitin sulfate proteoglycan and a2,611 in-tegrin mediate human melanoma cell migration on Type IV collagen and invasion of basement mem-branes. Mol. Biol. Cell. (1996) 7:383–396.
   PubMed Web of Science ®Google Scholar
• MILES AJ, SKUBITZ APN, FURCHT LT, FIELDS GB: Promo-tion of cell adhesion by single-stranded and triple-helical peptide models of basement membrane colla-gen a 1 (IV)531-543: evidence for conformationally de-pendent and conformationally independent Type IV collagen cell adhesion sites. J. Biol. Chem. (1994) 269:30939–30945.
   Google Scholar
• MILES AJ, KNUTSON JR, SKUBITZ APN et al.: A peptidemodel of basement membrane collagen al (IV)531-543 binds the a3,611 integrin. J. Biol. Chem. (1995) 270:29047–29050.
   PubMed Web of Science ®Google Scholar
• LI C, MCCARTHY JB, FURCHT LT, FIELDS GB: An all-D amino acid peptide model of al (IV)531-543 from Type IV collagen binds the a3,611 integrin and mediates tu-mor cell adhesion, spreading, and motility. Biochemis-try (1997) 36:15404–15410.
   PubMed Web of Science ®Google Scholar
• FIELDS GB: The collagen triple-helix: correlation of conformation with biological activities. Connect. Tissue Res. (1995) 31:235–243.
   PubMed Web of Science ®Google Scholar
• FIELDS CG, LOVDAHL CM, MILES AJ, MATTHIAS-HAGEN VL, FIELDS GB: Solid-phase synthesis and stability of triple-helical peptides incorporating native collagen sequences. Biopolymers (1993) 33:1695–1707.
   PubMed Web of Science ®Google Scholar
• GOLI UB, FIELDS GB, VAN WART HE: Synthetic triple-helical models for the collagen cleavage site in intersti-tial collagens. Collagen Rel. Res. Suppl. (1992) 1:71–72.
   Google Scholar
• MORTON LF, PEACHEY AR, KNIGHT CG, FARNDALE RW,BARNES MJ: The platelet reactivity of synthetic pep-tides based on the collagen III fragment al (IIDCB4. J. Biol. Chem. (1997) 272:11044–11048.
   PubMed Web of Science ®Google Scholar
• CARDERELLI PM, YAMAGATA S, TAGUCHI I et al.: The col-lagen receptor can, from MG-63 and 11T1080 cells, in-teracts with a cyclic RGD peptide. J. Biol. Chem. (1992) 267:23159–23164.
   Google Scholar
• SANCHEZ-MATEOS P, CABANAS C, SANCHEZ-MADRID F:Regulation of integrin function. Sem. Cancer Biol. (1996) 7:99–109.
   PubMed Web of Science ®Google Scholar
• WEITZMAN JB, PUJADES C, HEMLER ME: Integrin a chain cytoplasmic tails regulate 'antibody-redirected' cell adheison, independently of ligand binding. Eur. J. Im-munol. (1997) 27:78–84.
   Google Scholar
• GINSBERG MH, DU X, PLOW EF: Inside-out integrin sig-nalling. Curr. Opin. Cell Biol. (1992) 4:766–770.
   PubMedGoogle Scholar
• PULLMAN WE, BODMER WF: Cloning and characteriza-tion of a gene that regulates cell adhesion. Nature (1992) 356:529–532.
   PubMed Web of Science ®Google Scholar
• YAMAMOTO H, ITOH F, HINODA Y, IMAI K: Inverse as-sociation of cell adhesion regulator messenger RNA cer. Cancer Res. (1996) 56:3605–3609.
   Google Scholar
• LAUER JL, FURCHT LT, FIELDS GB: Inhibition of mela- noma cell binding to Type IV collagen by analogs of cell adhesion regulator. J. Med. Chem. (1997) 40:3077–3084.
   Google Scholar
• UN YZ, YAO SY, YEACH RA, TORGERSON TR, HAWIGER J: Inhibition of nuclear translocation of transcription factor NF-x13 by a synthetic peptide containing a cell membrane-permeable motif and nuclear localization sequence. J. Biol. Chem. (1995) 270:14255–14258.
   PubMed Web of Science ®Google Scholar
• WANGE RL, ISAKOV N, BURKE TR et al.: F2(Pmp)2-TAIdt-3, a novel competetive inhibitor of the binding of ZAP-70 to the T cell antigen receptor, blocks early T cell signal-ling. J. Biol. Chem. (1995) 270:944–948.
   PubMedGoogle Scholar
• DAMAJ BB, MCCOLL SR, MAHANA W, CROUCH MF, NAC-CACHE PH: Physical association of Giza with interleukin-8 receptors. J. Biol. Chem. (1996) 271:12783–12789.
   PubMed Web of Science ®Google Scholar
• LORET EP, VIVES E, HO PS et al: Activating region of11IV-1 Tat protein: vacuum UV circular dichroism and energy minimization. Biochemistry (1991) 30:6013–6023.
   PubMed Web of Science ®Google Scholar
• DEROSSIN D, JOLIOT AH, CHASSAING G, PROCHIANTZ A: The third helix of the antennapedia homeodomain translocates through biological membranes. J. Biol. Chem. (1994) 267:10444–10450.
   Google Scholar
• FAWELL S, SEERY J, DAIKH Y et al.: Tat-mediated delivery of heterologous proteins into cells. Proc. Natl. Acad. Sci. USA (1994) 91:664–668.
   PubMed Web of Science ®Google Scholar
• MOUSLI M, HUGLI TE, LANDRY Y, BRONNER C: Peptider-gic pathway in human skin and rat peritoneal mast cell activation. Immunopharmacology (1994) 27:1–11.
   Google Scholar
• IZARD JW, DOUGHTY MB, KENDALL DA: Physical and conformational properties of synthetic idealized sig-nal sequences parallel their biological function. Bio-chemistry (1995) 34:9904–9912.
   Google Scholar
• CROSS LJ, ENNIS M, KRAUSE E et al: Influence of a-heli-city, amphipathicity and D-amino acid incorporation on the peptide-induced mast cell activation. Eur. J. Pharmacol. (1995) 291:291–300.
   Google Scholar
• THEODORE L, DEROSSI D, CHASSAING G etal.: Intraneu-ronal delivery of protein kinase C pseudosubstrate leads to growth cone collapse. J. Neurosci. (1995) 15:7158–7167.
   Google Scholar
• SALEH MT, FERGUSON J, BOGGS JM, GARIEPY J: Inser-tion and orientation of a synthetic peptide represent-ing the C-terminus of the Al domain of shiga toxin into phospholipid membranes. Biochemistry (1996) 35:9325–9334.
   Google Scholar
• DU C, YAO S, ROJAS M, LIN YZ: Conformational and topological requirements of cell-permeable peptide function. J. Peptide Res. (1998) 51:235–243.
   PubMedGoogle Scholar
• BODOR N, PROKAI L, WU WM et al: A strategy for deliv-ering peptides into the central nervous system by se-quential metabolism. Science (1992) 257:1698–1700.
   PubMed Web of Science ®Google Scholar
• FORNARO M, LANGUINO LR: Alternatively spliced vari-ants: a new view of the integrin cytoplasmic domain. Matrix Biol. (1997) 16:185–193.
   PubMed Web of Science ®Google Scholar
• AMIDON GL, LEE HJ: Absorption of peptide and pepti-domimetic drugs. Ann. Rev. Pharmacol. Toxicol. (1994) 34:321–341.
   PubMed Web of Science ®Google Scholar
• MCDONNELL JJ: Towards a better understanding of bio-technology patent issues. Curr. Opin. Biotech. (1992) 3:216–217.
   Google Scholar