Differential expression and localization of TIMP-1 and TIMP-4 in human gliomas

Groft, Lori Lynne; Muzik, Huong; Rewcastle, N. B.; Johnston, Robert Mackenzie; Knäuper, Vera; Lafleur, Michel; Forsyth, Peter; Edwards, Dylan R.

doi:10.1054/bjoc.2001.1854

Cited by 81 publications

(66 citation statements)

References 47 publications

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“…Independent of its MMP inhibitory activity, TIMP-3 suppresses angiogenesis by blocking the interaction of VEGF with VEGFR-2 (Qi et al, 2003). On the other hand, TIMP-4 can either promote Tunuguntla et al, 2003) or inhibit tumour progression, depending on the nature of the tumour and mode of delivery Celiker et al, 2001;Groft et al, 2001;Zhao et al, 2004).…”

Section: Timpsmentioning

confidence: 99%

Identification of degradome components associated with prostate cancer progression by expression analysis of human prostatic tissues

et al. 2005

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Extracellular proteases of the matrix metalloproteinase (MMP) and serine protease families participate in many aspects of tumour growth and metastasis. Using quantitative real-time RT -PCR analysis, we have undertaken a comprehensive survey of the expression of these enzymes and of their natural inhibitors in 44 cases of human prostate cancer and 23 benign prostate specimens. We found increased expression of MMP10, 15, 24, 25 and 26, urokinase plasminogen activator-receptor (uPAR) and plasminogen activator inhibitor-1 (PAI1), and the newly characterised serine proteases hepsin and matriptase-1 (MTSP1) in malignant tissue compared to benign prostate tissue. In contrast, there was significantly decreased expression of MMP2 and MMP23, maspin, and the protease inhibitors tissue inhibitor of metalloproteinase 3 (TIMP3), TIMP4 and RECK (reversion-inducing cysteine-rich protein with Kazal motifs) in the cancer specimens. The expression of MMP15 and MMP26 correlated positively with Gleason score, whereas TIMP3, TIMP4 and RECK expression correlated negatively with Gleason score. The cellular localisation of the expression of the deregulated genes was evaluated using primary malignant epithelial and stromal cell cultures derived from radical prostatectomy specimens. MMP10 and 25, hepsin, MTSP1 and maspin showed predominantly epithelial expression, whereas TIMP 3 and 4, RECK, MMP2 and 23, uPAR and PAI1 were produced primarily by stromal cells. These data provide the first comprehensive and quantitative analysis of the expression and localisation of MMPs and their inhibitors in human prostate cancer, leading to the identification of several genes involved in proteolysis as potential prognostic indicators, in particular hepsin, MTSP1, MMP26, PAI1, uPAR, MMP15, TIMP3, TIMP4, maspin and RECK.

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Section: Timpsmentioning

confidence: 99%

Identification of degradome components associated with prostate cancer progression by expression analysis of human prostatic tissues

et al. 2005

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“…2A, Lane 5). TIMP-4, reported to be negatively associated with astrocytoma malignancy (Rorive et al, 2006) and able to reduce glioblastoma invasion in vitro (Groft et al, 2001), inhibited partially this proteolytic activity of MMP-9 (Fig. 2B, Lane 6).…”

Section: Mmp-9 Proteolyzes the Igfbp2-igfii Complexmentioning

confidence: 88%

“…TIMP-4, widely present in the normal central nervous system (CNS) (Crocker et al, 2004), has been reported to be overexpressed in indolent noninvasive pilocytic astrocytomas (WHO grade I) as compared with diffuse astrocytomas (WHO grade II-IV) (Rorive et al, 2006). TIMP-4 is also known to reduce the invasive ability of astrocytoma cells in vitro (Groft et al, 2001). In contrast, TIMP-1 is not observed in normal CNS, but its expression increases dramatically with astrocytoma malignancy (Groft et al, 2001;Lampert et al, 1998;Nakano et al, 1995).…”

Section: Introductionmentioning

confidence: 99%

“…TIMP-4 is also known to reduce the invasive ability of astrocytoma cells in vitro (Groft et al, 2001). In contrast, TIMP-1 is not observed in normal CNS, but its expression increases dramatically with astrocytoma malignancy (Groft et al, 2001;Lampert et al, 1998;Nakano et al, 1995). While the ECM substrates of the MMPs have been largely well characterized, identification and study of nonmatrix MMP substrates (such as growth factors and nonmatrix growth factor binding proteins) may provide further valuable insights into the mechanisms of tumor cell proliferation and migration.…”

Section: Introductionmentioning

confidence: 99%

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Matrix metalloproteinase‐9 interplays with the IGFBP2–IGFII complex to promote cell growth and motility in astrocytomas

Rorive

Berton

D’Haene

et al. 2008

Glia

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Insulin-like growth factor II (IGFII) acts as a potent mitogen for several tumor types and has been reported to positively influence astrocytoma cell growth and motility. In the central nervous system, IGFII bioavailability is mainly modulated by insulin-like growth factor binding protein 2 (IGFBP2), which sequestrates IGFII and therefore prevents its interaction with the type-1 IGF receptor (IGF-IR). Proteolysis of IGFBP2 is the predominant mechanism recognized to reduce the binding affinity of IGFBP2 for IGFII, thus favoring dissociation of IGFII from the IGFBP2-IGFII complex. It is known that certain proteases involved in astrocytoma malignancy, such as matrix metalloproteinase-7 (MMP-7), plasmin, and cathepsin D, are able to proteolyze IGFBP2 in vitro. The present study aims to investigate whether other proteases expressed by astrocytomas, specifically MMP-2, MMP-9, and membrane-type 1 matrix metalloprotease (MT1-MMP), are able to proteolyze the IGFBP2-IGFII complex. Our results show the following: (i) MMP-9 proteolyzes the IGFBP2-IGFII complex in vitro, while MMP-2 and MT1-MMP do not; (ii) this MMP-9-induced IGFBP2-IGFII complex proteolysis releases free IGFII, which contributes to enhance the motility and the growth of LN229 astrocytoma cells. Furthermore, this study also highlights that the formation of the IGFBP2-IGFII complex inhibits IGFBP2's cell motility promoting effect by reducing the pool of free IGFBP2. In conclusion, MMP-9-induced IGFBP2 proteolysis may be regarded as an important post-translational event involved in astrocytoma aggressiveness. These new findings support drug targeting of MMP-9 as an interesting approach in the treatment of astrocytoma. V V C

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“…TIMP-1 is also involved in the development of neuroepithelial tumors (Gardner & Ghorpade, 2003;Lampert et al 1998;Kakagawa et al 1994;Pagentecher et al 1999). Groft et al (2001) showed that overexpression of TIMP-1 is associated with malignancy in gliomas and that TIMP-1 is detected mainly near the sites of blood vessel formation. These observations could be a result of interactions with pro-MMP-9 and the angiogenesispromoting ability of this MMP.…”

Section: The Role Of Timps In the Progression Of Astrocytic Tumorsmentioning

confidence: 99%

The Role of Matrix Metalloproteinases a nd Tissue Inhibitors of Metalloproteinases in the Progression of Astrocytomas

Motta¹,

Canalle²,

Pinto³

et al. 2011

Molecular Targets of CNS Tumors

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Differential expression and localization of TIMP-1 and TIMP-4 in human gliomas

Cited by 81 publications

References 47 publications

Identification of degradome components associated with prostate cancer progression by expression analysis of human prostatic tissues

Identification of degradome components associated with prostate cancer progression by expression analysis of human prostatic tissues

Matrix metalloproteinase‐9 interplays with the IGFBP2–IGFII complex to promote cell growth and motility in astrocytomas

The Role of Matrix Metalloproteinases a nd Tissue Inhibitors of Metalloproteinases in the Progression of Astrocytomas

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