2008, Number 1-2
Next >>
Rev Esp Cienc Salud 2008; 11 (1-2)
Src family kinases in cancer development
Soto CI
Language: Spanish
References: 65
Page: 3-9
PDF size: 263.41 Kb.
ABSTRACT
The Src family of non-receptor protein tyrosine kinases plays critical roles in a variety of cellular signal transduction pathways,
regulating such diverse processes as cell division, motility, adhesion, angiogenesis, and survival. Constitutively activated
variants of Src family kinases, including the viral oncoproteins v-Src and v-Yes, are capable of inducing malignant
transformation of a variety of cell types. Src family kinases, most notably although not exclusively c-Src, are frequently
overexpressed and/or aberrantly activated in a variety of epithelial and non-epithelial cancers. Activation is very common in
colorectal and breast cancers, and somewhat less frequent in melanomas, ovarian cancer, gastric cancer, head and neck
cancers, pancreatic cancer, lung cancer, brain cancers, and blood cancers. Further, the extent of increased Src family activity
often correlates with malignant potential and patient survival. Activation of Src family kinases in human cancers may occur
through a variety of mechanisms and is frequently a critical event in tumor progression. Exactly how Src family kinases
contribute to individual tumors remains to be defined completely, however they appear to be important for multiple aspects
of tumor progression, including proliferation, disruption of cell/cell contacts, migration, invasiveness, resistance to apoptosis,
and angiogenesis. This review details the evidence for Src family activation in human tumors, and emphasizes possible
consequences to tumor progression. Given the ability of Src and its family members to participate in so many aspects of tumor
progression and metastasis, Src family kinases are attractive targets for future anti-cancer therapeutics.
REFERENCES
Brown MT, Cooper JA. Regulation, substrates and functions of src. Biochim. Biophys. Acta 1996; 1287:121210.
Manning G, Whyte D, Martinez R, Hunter T, Sudarsanam S. The protein kinase complement of the human genome. Science 2002; 298:19121934.
Caenepeel S, Charydczak G, Sudarsanam S, Hunter T. The mouse kinome: discovery and comparative genomics of all mouse protein kinases. Proc. Natl. Acad. Sci. U. S. A. 2004; 101:1170711712.
Frame MC. Src in cancer: deregulation and consequences for cell behaviour. Biochim. Biophys. Acta 2002; 1602:114130.
Cohen P. Protein kinasesthe major drug targets of the twenty-first century. Nat. Rev. Drug. Discov. 2002; 1:309315.
Hunter T, Sefton BM. Transforming gene product of Rous sarcoma virus phosphrylates tyrosine. Proc. Natl. Acad. Sci. U. S. A. 1980; 77:13111315.
Parsons SJ, Parsons JT. Src family kinases, key regulators of signal transduction. Oncogene 2004; 23:79067909.
Chong YP, Ia KK, Mulhern TD, Cheng HC. Endogenous and synthetic inhibitors of the Src-family protein tyrosine kinases. Biochim. Biophys. Acta 2005; 1754:210220.
Boggon TJ, Eck MJ. Structure and regulation of Src family kinases. Oncogene 2004; 23:79187927.
Koegl M, Zlatkine P, Ley SC, Courtneidge SA, Magee AI. Palmitoylation of multiple Src-family kinases at a homologous Nterminal motif. Biochem. J. 1994; 303:749753.
Resh MD. Fatty acylation of proteins: new insights into membrane targeting of myristoylated and palmitoylated proteins. Biochim. Biophys. Acta 1999; 1451: 116.
Koch C, Anderson D, Moran M, Ellis C, Pawson T. SH2 and SH3 domains: elements that control interactions of cytoplasmic signalling proteins. Science 1991; 252:668674.
Sicheri F, Moarefi I, Kuriyan J. The crystal structure of the Src family tyrosine kinase Hck. Nature 1997; 385:602609.
Williams JC, Weijland A, Gonfloni S, Thompson A, Courtneidge SA, Superti-Furga G, Wierenga RK. The 2.35 A crystal structure of the inactivated form of chicken Src: a dynamic molecule with multiple regulatory interactions. J. Mol. Biol. 1997; 274:757775.
Xu W, Harrison SC, Eck MJ. Three dimensional structure of the tyrosine kinase c-Src. Nature 1997; 385:595602.
Smart E, Oppermann H, Czernilofsky AP, Purchio AF, Erikson RL, Bishop JM. Characterization of sites for tyrosine phosphorylation in the transforming protein of Rous sarcoma virus (pp60v-src) and its normal cellular homologue (pp60c-src). Proc. Natl. Acad. Sci. U. S. A. 1981; 78:60136017.
Yeatman TJ. A renaissance for SRC. Nat Rev Cancer 2004;4:470 80.
Frame MC. Newest findings on the oldest oncogene: how activated src does it. J Cell Sci 2004;117:98998.
Summy JM, Gallick GE. Src family kinases in tumor progression and metastasis. Cancer Metastasis Rev 2003;22:33758.
Shah AN, Gallick GE. Src, chemoresistance and epithelial to mesenchymal transition: are they related? Anticancer Drugs 2007;18:3715.
Avizienyte E, Brunton VG, Fincham VJ, Frame MC. The SRCinduced mesenchymal state in late-stage colon cancer cells. Cells Tissues Organs 2005;179:7380.
Desgrosellier J, Prevost N, Barnes L, Shattil S, Cheresh D. Disruption of an integrin αvβ3/c-src complex inhibits αvβ3-mediated tumor progression and metastasis. In: Proceedings of the 97th Annual Meeting of the American Association for Cancer Research, April 14- 18, 2007, Los Angeles, California. p. 2186.
Bolen JB, Veillette A, Schwartz AM, DeSeau V, Rosen N. Activation of pp60c-src protein kinase activity in human colon carcinoma. Proc Natl Acad Sci U S A. 1987;84:22515.
Maurer GD, Leupold JH, Schewe DM, et al. Analysis of specific transcriptional regulators as early predictors of independent prognostic relevance in resected colorectal cancer. Clin Cancer Res 2007;13:1123 32.
Aligayer H, Boyd DD, Heiss MM, Abdalla EK, Curley SA, Gallick GE. Activation of Src kinase in primary colorectal carcinoma: an indicator of poor clinical prognosis. Cancer 2002;94:34451.
Summy JM, Gallick GE. Src family kinases in tumor progression and metastasis. Cancer Metastasis Rev 2003;22:33758.
Verbeek BS, Vroom TM, Adriaansen-Slot SS, et al. c-Src protein expression is increased in human breast cancer. An immunohistochemical and biochemical analysis. J Pathol 1996;180:3838.
van Oijen MG, Rijksen G, ten Broek FW, Slootweg PJ. Overexpression of c-Src in areas of hyperproliferation in head and neck cancer, premalignant lesions and benign mucosal disorders. J Oral Pathol Med 1998;27:14752.
Thomas SM, Brugge JS. Cellular functions regulated by Src family kinases. Annu Rev Cell Dev Biol 1997;13:513609.
Bromann PA, Korkaya H, Courtneidge SA. The interplay between Src family kinases and receptor tyrosine kinases. Oncogene 2004;23:795768.
Blume-Jensen P, Hunter T. Oncogenic kinase signalling. Nature 2001;411:35565.
Avizienyte E, Frame MC. Src and FAK signalling controls adhesion fate and the epithelial-to-mesenchymal transition. Curr Opin Cell Biol 2005;17:5427.
Roche S, Fumagalli S, Courtneidge S A. Requirement for Src family protein tyrosine kinases in G2 for fibroblast cell division. Science 1995; 269:15671569.
Jones RJ, et al. Elevated c-Src is linked to altered cell-matrix adhesion rather than proliferation in KM12C human colorectal cancer cells. Br. J. Cancer 2002; 87:11281135.
Brunton VG, Ozanne BW, Paraskeva C, Frame MC. A role for epidermal growth factor receptor, c-Src and focal adhesion kinase in an in vitro model for the progression of colon cancer. Oncogene 1997; 14:283293.
Frame MC. Src in cancer: deregulation and consequences for cell behaviour. Biochim. Biophys. Acta 2002; 1602:114130.
Irby RB, Yeatman TJ. Role of Src expression and activation in human cancer. Oncogene 2000; 19:56365642.
Talamonti MS, Roh MS, Curley SA, Gallick GE. Increase in activity and level of pp60c-src in progressive stages of human colorectal cancer. J. Clin. Invest. 1993; 91:5360.
Weber TK, Steele G, Summerhayes IC. Differential pp60c-src activity in well and poorly differentiated human colon carcinomas and cell lines. J. Clin. Invest. 1992; 90:815821.
Maa MC, Leu TH, McCarley DJ, Schatzman RC, Parsons SJ. Potentiation of epidermal growth factor receptor-mediated oncogenesis by c-Src: implications for the etiology of multiple human cancers. Proc. Natl Acad. Sci. USA 1995; 92:69816985.
Mao W, et al. Activation of c-Src by receptor tyrosine kinases in human colon cancer cells with high metastatic potential. Oncogene 1997; 15:30833090.
Hynes NE. Tyrosine kinase signalling in breast cancer. Breast Cancer Res. 2000; 2:154157.
Wiener JR. et al. Activated SRC protein tyrosine kinase is overexpressed in late-stage human ovarian cancers. Gynecol. Oncol. 2003; 88:7379.
Masaki T, et al. pp60c-src activation in hepatocellular carcinoma of humans and LEC rats. Hepatology 1998; 27:12571264.
Masaki T, et al. Reduced C-terminal Src kinase (Csk) activities in hepatocellular carcinoma. Hepatology 1999; 29:379384.
Cam WR, et al. Reduced C-terminal Src kinase activity is correlated inversely with pp60(c-src) activity in colorectal carcinoma. Cancer 2001; 92:6170.
Jacobs G, Rubsamen H. Expression of pp60C-src protein kinase in adult and fetal human tissue: High activities in some sarcomas and mammary carcinomas. Cancer Res. 1983; 43:1696-1702.
Rosen N, Bolen JB, Schwartz AM, Cohen P, DeSeau V, Israel MA. Analysis of pp60C-src protein kinase activity in human tumor cell lines and tissues. J. Biol Chem. 1986; 261:13754-13759.
Lehrer S, OShaughnessy J, Song HK, Levine E, Savoretti P, Dalton J, Lipsztein R, Kalnicki S, Bloomer WD. Activity of pp60c-src protein kinase in human breast cancer. Mt Sinai J Med. 1989; 56:83- 85.
Koster A, Landgraf S, Leipold A, Sachse R, Gebhart E, Tulusan AH, Ronay G, Schmidt C, Dingermann T. Expression of oncogenes in human breast cancer specimens. Anticancer Res. 1991; 11:193-201.
Ottenhoff-Kalff AE, Rijksen g, van Beurden EA, Hennipman A, Michels AA, Staal GE. Characterization of protein tyrosine kinases from human breast cancer: involvement of the c-src oncogene product. Cancer Res. 1992; 52:4773-4778.
Verbeek BS, Vroom TM, Adriaansen-Slot SS, Ottenhoff-Kalff AE, Geertzerna JG, Hennipman A, Rijksen G. c-Src protein expression is increased in human breast cancer. An immunohistochemical and biochemical analysis. J Pathol. 1996; 180:383-388.
Reissig D, Clement J, Sanger J, Berndt A, Kosmehl H, Bohmer FD. Elevated activity and expression of Src family kinases in human breast carcinoma tissue versus matched non-tumor tissue. J. Cancer Res Clin Oncol. 2001; 127:226-230.
Biscardi JS, Ishizawar RC, Silva CM, Parsons SJ. Tyrosine kinase signaling in breast cancer: epidermal growth factor receptor and c-Src interactions in breast cancer. Breast Cancer Res. 2000; 2:203-210.
Alonso G, Koegl M., Mazurenko N, Courtneidge SA. Sequence requierements for binding of Src family tyrosine kinases to activated growth factor receptors. J. Biol. Chem. 1995; 270:9840-9848.
Courtneidge SA, Dhand R, Pilat D, Twamley GM, Waterfield MD, Roussel MF. Activation of Src family kinases by colony stimulating factor-1 and their association with its receptor. EMBO J. 1993; 12:943-950.
Kypta RM, Goldberg Y, Ulug ET, Courtneidge SA. Association between the PDGF receptor and membres of the src family kinases. Cell. 1990; 62:481-492.
Mori S, Ronnstrand L, Yokote K, Engstrom A, Courtneidge SA, Glaesson-Welsh L, Heldin CH. Identification of two juxtamembrane autophosphorylation sites in the PDGF beta receptor: involvement in the interaction with Src family tyrosine kinases. Embo J. 1993; 12:2257-2264.
Twamley GM, Kypta RM, Hall B, Courtneidge SA. Association of Fyn with the activated platelet-derived growth factor receptor: requirements for binding and phosphorylation. Oncogene. 1992; 7:1893-1901.
Egan C, Pang A, Durda D, Cheng HC, Wang JH, Fujita DJ. Activation of Src in human breast tumor cell lines: elevated levels of phosphotyrosine phosphatase activity that preferentially recognizes the Src carboxy terminal negative regulatory tyrosine 530. Oncogene. 1999; 18:1227-1237.
Bjorge JD, Pang A, Fujita DJ. Identification of protein tyrosine phosphatase 1B as the major tyrosine phosphatase activity capable of dephosphorylating and activating c-Src in several human breast cancer cell lines, J. Biol Chem. 2000; 275:41439-41446.
Golas, J. M. et al. SKI-606, a 4-anilino-3-quinolinecarbonitrile dual inhibitor of Src and Abl kinases, is a potent antiproliferative agent against chronic myelogenous leukemia cells in culture and causes regression of K562 xenografts in nude mice. Cancer Res. 2003; 63: 375 381.
Shakespeare, W. C. et al. Novel bone-targeted Src tyrosine kinase inhibitor drug discovery. Curr. Opin. Drug Discov. Devel. 2003; 6: 729741.
Avizienyte, E. et al. Src-induced de-regulation of E-cadherin in colon cancer cells requires integrin signalling. Nature Cell Biol. 2002; 4: 632638.
Golubovskaya, V. M. et al. Simultaneous inhibition of focal adhesion kinase and SRC enhances detachment and apoptosis in colon cancer cell lines. Mol. Cancer Res. 2003; 1: 755764.