Effects of SHIP-1 on MMP2 Secretion and Invasion of SR3Y1 Cells

Wanjin Xing; Michinari Hamaguchi

doi:10.1016/S1673-8527(07)60030-7

Volume 34 Issue 4

Apr. 2007

Turn off MathJax

Article Contents

Abstract

References

Article Navigation > Journal of Genetics and Genomics > 2007 > 34(4): 285-293

PDF( 379 KB)

Effects of SHIP-1 on MMP2 Secretion and Invasion of SR3Y1 Cells

doi: 10.1016/S1673-8527(07)60030-7

Wanjin Xing^a,
Michinari Hamaguchi^b

a
Department of Biology, Life Science College, Inner Mongolia University, Hohhot 010021, China
b
Department of Molecular Pathology, Medical School of Nagoya University, Nagoya 466–8550, Japan

More Information

Corresponding author: E-mail address: xwanjin@163.com (Wanjin Xing)
Received Date: 2006-09-07
Accepted Date: 2006-11-29

Available Online: 2007-05-09

Publish Date: 2007-04-20

Abstract

Abstract

SHIP-1 is an SH2 domain containing inositol-5-phosphatase that appears to be a negative regulator of hematopoiesis. To the potential effects of SHIP-1 on MMP2 secretion and migration of cancer cells, three murine SHIP-1 mutants were made: ΔSH2-SHIP-1, ΔPtase-SHIP-1, ΔCter-SHIP-1. These mutant forms were subcloned as well as the wild type (WT) of murine SHIP-1 cDNA were subcloned into pcDNA3 expression vector, then transfected into and overexpressed SHIP-1 and its mutants in a Src-transformed 3Y1 cell line (SR3Y1). The results showed that overexpression of wild type of SHIP-1 does not affect the MMP2 secretion in both SR3Y1 and 3Y1 cells, but can induce MMP9 secretion, while either WT SHIP-1, the SH2 domain, phosphatase domain, or C terminus deletion mutants could significantly block the MMP2 and MMP9 secretion in SR3Y1 cells and suppress cell invasion ability. The results confirmed SHIP-1 as a negative regulator for cell migration and invasion in transformed cells, and implied that it may function through each of its three domains.
- SHIP-1,
- transfection,
- SR3Y1,
- invasion,
- MMP2

FullText(HTML)

References(32)

References

[1]	Damen, JE, Liu, et al. The 145-kDa protein induced to associate with Shc by multiple cytokines is an inositol tetraphosphate and phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase Proc Natl Acad Sci USA, 93 (1996),pp. 1689-1693
[2]	Kavanaugh, WM, Pot, et al. Multiple forms of an inositol polyphosphate 5-phosphatase form signaling complexes with Shc and Grb2 Curr Biol, 6 (1996),pp. 438-445
[3]	Lioubin, MN, Algate, et al. p 150 SHIP, a signal transduction molecule with inositol polyphosphate-5-phosphatase activity Genes and Develop, 10 (1996),pp. 1084-1095
[4]	Liu, L, Damen, et al. The Src homology 2 (SH2) domain of SH2-containing inositol phosphatase (SHIP) is essential for tyrosine phosphorylation of SHIP, its association with Shc, and its induction of apoptosis J Biol Chem, 272 (1997),pp. 8983-8988
[5]	Liu, L, Damen, et al. SHIP, a new player in cytokine-induced signaling Leukemia, 11 (1997),pp. 181-184
[6]	Tridandapani, S, Kelley, et al. Recruitment and phosphorylation of SH2-containing inositol phosphatase and Shc to the B-cell Fc gamma immunoreceptor tyrosine-based inhibition motif peptide motif Mol Cell Biol, 17 (1997),pp. 4305-4311
[7]	Vely, F, Olivero, et al. Differential association of phosphatases with hematopoietic co-receptors bearing immunoreceptor tyrosine-based inhibition motifs Eur J Immunol, 27 (1997),pp. 1994-2000
[8]	Ono, M, Bolland, et al. Role of the inositol phosphatase SHIP in negative regulation of the immune system by the receptor Fc(RIIB Nature, 383 (1996),pp. 263-266
[9]	Ono, M, Okada, et al. Deletion of SHIP or SHP-1 reveals two distinct pathways for inhibitory signaling Cell, 90 (1997),pp. 293-301
[10]	Aman, MJ, Lamkin, et al. The inositol phosphatase SHIP inhibits Akt/PKB activation in B cells J Biol Chem, 273 (1998),pp. 33922-33928
[11]	Hunter, MG, Avalos, et al. Phosphatidylinositol 3′-kinase and SH2-containing inositol phosphatase (SHIP) are recruited by distinct positive and negative growth-regulatory domains in the granulocyte colony-stimulating factor receptor J Immunol, 160 (1998),pp. 4979-4987
[12]	Rameh, LE, Cantley, et al. The role of phosphoinositide 3-kinase lipid products in cell function J Biol Chem, 274 (1999),pp. 8347-8350
[13]	Helgason, CD, Damen, et al. Targeted disruption of SHIP leads to hemopoietic perturbations, lung pathology, and a shortened life span Genes Dev, 12 (1998),pp. 1610-1620
[14]	Kim, CH, Hangoc, et al. Altered responsiveness to chemokines due to targeted disruption of SHIP J Clin Invest, 104 (1999),pp. 1751-1759
[15]	Sattler, M, Verma, et al. BCR/ABL directly inhibits expression of SHIP, an SH2-containing polyinositol-5-phosphatase involved in the regulation of hematopoiesis Mol Cell Biol, 19 (1999),pp. 7473-7480
[16]	Phee, H, Jacob, et al. Enzymatic activity of the Src homology 2 domain-containing inositol phosphatase is regulated by a plasma membrane location J Biol Chem, 275 (2000),pp. 19090-19097
[17]	Liu, L, Damen, et al. Multiple cytokines stimulate the binding of a common 145-kilodalton protein to Shc at the Grb 2 recognition site of Shc Mol Cell Biol, 14 (1994),pp. 6926-6935
[18]	Liu, L, Damen, et al. Interleukin-3 induces the association of the inositol 5-phosphatase SHIP with SHP2 J Biol Chem, 272 (1997),pp. 10998-11001
[19]	Sattler, M, Salgia, et al. The phosphatidylinositol polyphosphate 5-phosphatase SHIP and the protein tyrosine phosphatase SHP-2 form a complex in hematopoietic cells which can be regulated by BCR/ABL and growth factors Oncogene, 15 (1997),pp. 2379-2384
[20]	Sattler, M, Salgia, et al. Activation of hematopoietic growth factor signal transduction pathways by the human oncogene BCR/ABL Cytokine Growth Factor Rev,, 8 (1997),pp. 63-79
[21]	Verfaillie, CM, McCarthy, et al. Mechanisms underlying abnormal trafficking of malignant progenitors in chronic myelogenous leukemia. Decreased adhesion to stroma and fibronectin but increased adhesion to the basement membrane components laminin and collagen type IV J Clin Invest, 90 (1992),pp. 1232-1241
[22]	Salgia, R, Li, et al. BCR/ABL induces multiple abnormalities of cytoskeletal function J Clin Invest, 100 (1997),pp. 46-57
[23]	Noguchi, T, Matozaki, et al. Tyrosine phosphorylation of p62Dok induced by cell adhesion and insulin: possible role in cell migration EMBO J, 18 (1999),pp. 1748-1760
[24]	Uemura, N, Griffin, et al. The adapter protein Crkl links Cbl to C3G after integrin ligation and enhances cell migration J Biol Chem, 274 (1999),pp. 37525-37532
[25]	Stetler-Stevenson, WG Matrix metalloproteinases in angiogenesis: a moving target for therapeutic intervention J Clin Invest, 103 (1999),pp. 1237-1241
[26]	Mancini, A, Koch, et al. The SH2-containing inositol 5-phosphatase (SHIP)-1 is implicated in the control of cell-cell junction and induces dissociation and dispersion of MDCK cells Oncogene, 21 (2002),pp. 1477-1484
[27]	Kong, D, Suzuki, et al. PTEN 1 is frequently mutated in primary endometrial carcinomas Nat Genet, 17 (1997),pp. 143-144
[28]	Li, J, Yen, et al. PTEN, a putative protein tyrosine phosphatase gene mutated in human brain, breast, and prostate cancer Science, 275 (1997),pp. 1943-1947
[29]	Steck, PA, Pershouse, et al. Identification of a candidate tumour suppressor gene, MMAC1, at chromosome 10q23.3 that is mutated in multiple advanced cancers Nat Genet, 15 (1997),pp. 356-362
[30]	Weidner, KM, Sachs, et al. The met receptor tyrosine kinase transduces motility, proliferation, and morphogenic signals of scatter factor/hepatocyte growth factor in epithelial cells J Cell Biol, 121 (1993),pp. 145-154
[31]	Stefan, M, Koch, et al. Src homology 2-containing inositol 5-phosphatase 1 binds to the multifunctional docking site of c-met and potentiates hepatocyte growth factor-induced branching tubulogenesis J Biol Chem, 276 (2001),pp. 3017-3023
[32]	Wada, T, Sasaoka, et al. Role of the Src homology 2 (SH2) domain and cterminus tyrosine phosphorylation sites of SH2-containing inositol phosphatase (SHIP) in the regulation of insulin-induced mitogenesis Endocrinology, 140 (1999),pp. 4585-4594