Decreased production of insulin‐like growth factor‐binding protein (IGFBP)‐6 by transfection of colon cancer cells with an antisense IGFBP‐6 cDNA construct leads to stimulation of cell proliferation

Kim, Eun J.; Schaffer, Beverly S.; Kang, Young Jong; MacDonald, Richard G.; Park, Jung H.Y.

doi:10.1046/j.1440-1746.2002.02703.x

Cited by 16 publications

(10 citation statements)

References 31 publications

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“…IGFBP-6 binds and inhibits the activity of IGF-II cell proliferation by preventing IGF-II interaction with the IGF-I receptor (36). The complete degradation of IGFBP-6 into multiple fragments by MMP-2 should disrupt IGF-II binding and so increase IGF-II bioavailability.…”

Section: Discussionmentioning

confidence: 99%

Identification of Candidate Angiogenic Inhibitors Processed by Matrix Metalloproteinase 2 (MMP-2) in Cell-Based Proteomic Screens: Disruption of Vascular Endothelial Growth Factor (VEGF)/Heparin Affin Regulatory Peptide (Pleiotrophin) and VEGF/Connective Tissue Growth Factor Angiogenic Inhibitory Complexes by MMP-2 Proteolysis

Dean

Butler

Hamma-Kourbali

et al. 2007

Molecular and Cellular Biology

192

159

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Matrix metalloproteinases (MMPs) exert both pro-and antiangiogenic functions by the release of cytokines or proteolytically generated angiogenic inhibitors from extracellular matrix and basement membrane remodeling. In the Mmp2 ؊/؊ mouse neovascularization is greatly reduced, but the mechanistic aspects of this remain unclear. Using isotope-coded affinity tag labeling of proteins analyzed by multidimensional liquid chromatography and tandem mass spectrometry we explored proteome differences between Mmp2 Matrix metalloproteinase 2 (MMP-2) (also known as gelatinase A), like many of the 23 MMPs in humans, has long been associated with angiogenesis, tumor progression, and metastasis (20, 50). More recently the critical importance of MMP-2 in breast cancer metastasis was shown by Minn et al. (52), who found that the MMP2 gene was one of the four key genes in the genomic signature associated with the most virulent breast cancer lung metastases. In this model, the development of angiogenesis was highly dependent upon MMP-2 expression (23). With other new functions of MMPs that promote cancer cell growth, invasion, metastasis, and immune cell evasion (20, 50) a more complex role for MMPs than just degradation of extracellular matrix proteins is being revealed (12, 56).Contrary to their many carcinogenic roles, several MMPs are now being recognized as cancer antitargets due to their normal physiological roles in cell signaling and tissue homeostasis that are protective against cancer (62). MMP-3 overexpression reduces 12-dimethylbenz[a]anthracene (DMBA)-induced skin carcinogenesis (76); Mmp8 Ϫ/Ϫ mice treated with DMBA and the phorbol ester 12-myristate 13-acetate develop more skin papillomas and fibrosarcomas than wild-type mice (4), and Mmp12 Ϫ/Ϫ mice show increased lung carcinogenesis (30). The detailed study of individual MMPs is therefore necessary to understand their specific functions in different physiological and pathological processes, information that is necessary for protease drug target validation (62). Elucidation of each protease substrate repertoire or degradome is crucial to understanding the biological roles of MMPs (44). Genetic models of disease in mice are powerful, yet time-consuming (20,60,64), so high-content proteomic approaches using human cell systems offer great promise in understanding the biological functions of human proteases (60,70).

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Section: Discussionmentioning

confidence: 99%

Identification of Candidate Angiogenic Inhibitors Processed by Matrix Metalloproteinase 2 (MMP-2) in Cell-Based Proteomic Screens: Disruption of Vascular Endothelial Growth Factor (VEGF)/Heparin Affin Regulatory Peptide (Pleiotrophin) and VEGF/Connective Tissue Growth Factor Angiogenic Inhibitory Complexes by MMP-2 Proteolysis

Dean

Butler

Hamma-Kourbali

et al. 2007

Molecular and Cellular Biology

192

159

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“…With TCDD-induced expression of IGFBP-6, a high degree of IGFBP-6 elevation appeared to enhance apoptosis, whereas a reduction of IGFBP-6 inhibited TCDD from inducing apoptosis in thymoma cells (53). Inactivating the expression of IGFBP-6 in colon cancer cells resulted in a gain of cell proliferation, suggesting that IGFBP-6 may be inhibitory for cell growth (43). Whether IGFBP-6 mediates growth arrest or apoptosis induced by H 2 O 2 treatment remains to be determined.…”

Section: Discussionmentioning

confidence: 99%

Proteomic Identification of Insulin-like Growth Factor-binding Protein-6 Induced by Sublethal H2O2 Stress from Human Diploid Fibroblasts

Xie

Tsaprailis²,

Chen

2005

Molecular & Cellular Proteomics

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Fibroblasts are the most ubiquitous cell types within our body. They produce various factors to maintain the texture and structure of a particular organ or tissue. To identify protein factors secreted by fibroblasts and alteration of these protein factors upon oxidative stress, HCA 3 human skin diploid fibroblasts were exposed to a sublethal dose of H 2 O 2 , which induces a prematurely senescent phenotype. Conditioned media from prematurely senescent cells versus control cells were analyzed for proteins using an LC-MS/MS-based proteomic technique. Collagen ␣1(VI), collagen ␣2(I), fibronectin, lumican, and matrix metalloproteinase 2 were among the proteins consistently detected from control and H

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“…Together, IGFBP-4, -5 and -6 constitute less than 25% of the total IGF-binding capacity in serum and they appear to have preference for IGF-II [3]. In vitro studies suggest that IGF-I mediated actions are generally inhibited by IGFBP-4 and -6, but potentiated by IGFBP-5 [2,80]. Accordingly, serum free IGF-I has been reported to correlate inversely with IGFBP-4 and positively with IGFBP-5, whereas the relationship between free IGF-I and IGFBP-6 is less settled [81,82].…”

Section: The Regulation Of Free and Total Igf-i: Effects Of Gh Insulmentioning

confidence: 99%

Free insulin-like growth factors – measurements and relationships to growth hormone secretion and glucose homeostasis

Frystyk¹

2004

Growth Hormone & IGF Research

302

267

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Decreased production of insulin‐like growth factor‐binding protein (IGFBP)‐6 by transfection of colon cancer cells with an antisense IGFBP‐6 cDNA construct leads to stimulation of cell proliferation

Abstract: : Our findings are consistent with the hypothesis that IGFBP-6 inhibits cell growth by binding to endogenously produced IGF-II, thereby preventing IGF-II from interacting with the IGF-I receptor to stimulate cellular proliferation by an autocrine mechanism.

Cited by 16 publications

References 31 publications

Proteomic Identification of Insulin-like Growth Factor-binding Protein-6 Induced by Sublethal H2O2 Stress from Human Diploid Fibroblasts

Free insulin-like growth factors – measurements and relationships to growth hormone secretion and glucose homeostasis

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