Essential roles of IGFBP-3 and IGFBP-rP1 in breast cancer

Burger, Angelika M.; Leyland‐Jones, Brian; Banerjee, Kris; Spyropoulos, Demetri D.; Seth, Arun

doi:10.1016/j.ejca.2005.04.023

Cited by 126 publications

(141 citation statements)

References 82 publications

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“…The wounded surface was washed with 1Â PBS and incubated in DMEM with 10% fetal bovine serum. A series of time frame (2,4,8,12, and 24 h) of migration pattern at the wound edge were monitored by phase microscopy using an Axiovert 200M microscope with digital camera (Carl Zeiss, Thornwood, NY). The images were captured by AxioVision 4.0 software (Carl Zeiss).…”

Section: Scratch-wound Assaymentioning

confidence: 99%

Association of insulin-like growth factor binding protein-3 expression with melanoma progression

Nakajima

Hamil

et al. 2006

Molecular Cancer Therapeutics

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Previous studies from our laboratory have identified several endothelial cell -associated marker genes implicated in human melanoma metastasis via tumor vasculogenic mimicry. In this study, we used dual model systems composed of melanoma cell lines and clinical melanoma samples to validate the importance of insulin-like growth factor binding protein-3 (IGFBP-3) as a marker involved in disease progression. Gene expression analysis was done using a microarray approach for both primary and metastatic melanoma samples. The expression of IGFBP-3 was decreased using a small interfering RNA (siRNA) knockdown approach and quantified with real-time quantitative reverse transcription-PCR analysis. The expression of insulin-like growth factor binding protein 3 (IGFBP-3) was up-regulated by nearly 16-fold in WM266-4 compared with WM35 cells. A subsequent parallel analysis using freshly isolated primary and metastatic melanoma cell samples and melanoma tissue array confirmed the previous findings. The functional significance of IGFBP-3 in melanoma invasion was further investigated using a siRNA gene knockdown approach, with the expression of IGFBP-3 markedly reduced. Additionally, siRNA knockdown resulted in a significant reduction in cell motility, migration, and invasive capacity of WM266-4 cells in vitro. These results strongly suggest that IGFBP-3 expression may be a vital cell motility, migration, and proliferation factor necessary for melanoma metastasis and is an important biomarker in human melanoma. [Mol Cancer Ther 2006;5(12):3078 -84]

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Section: Scratch-wound Assaymentioning

confidence: 99%

Association of insulin-like growth factor binding protein-3 expression with melanoma progression

Nakajima

Hamil

et al. 2006

Molecular Cancer Therapeutics

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“…In the aggregate to IGF-binding, a number of IGF-independent functions have been described for IGFBPs, many of which occur through interaction with extracellular matrix (ECM) components (Miyakoshi et al, 2001;Bach et al, 2005). Alternatively, IGFBPs can translocate to the nucleus with the help of importin b and act as transcriptional regulators (Mohan and Baylink, 2002;Burger et al, 2005). Such IGF-independent functions have implications not only in cell growth inhibition, the promotion of apoptosis and the modulation of cell adhesion and migration, but also in cancer.…”

Section: Introductionmentioning

confidence: 99%

“…Binding is exerted through both domains, which are linked by a non-conserved connecting mid-region or Ldomain (Hwa et al, 1999). IGFBPs modulate IGF transport and IGFR binding, dramatically slowing down IGF clearance, but also hindering their mitogenic activity (Burger et al, 2005). Among these proteins, IGFBP-2 and -6 have a higher affinity for IGF-II than for IGF-I, while IGFBP-1, -3, -4 and -5 prefer IGF-I over IGF-II (Durai et al, 2005) and none of them binds insulin.…”

Section: Introductionmentioning

confidence: 99%

“…IGFBPPs are present both in circulation and in interstitial fluids, and their activity is kept in check by endogenous protease activators and inhibitors Bunn and Fowlkes, 2003;Holly, 2004). Among the IGFBPPs reported are serine proteinases (complement protein 1s; kallikreins such as prostate-specific antigen, human kallikrein 2 and 7S nerve growth factor; plasmin; a HtrA-related protease; seminal plasma trypsin; cathepsin G and neutrophil elastase; and thrombin), cysteine proteinases (cathepsins and calpain), and metalloproteases (MPs) from the adamalysin/ADAM (ADAM-9, -12 and -28) and matrix metalloprotease (MMP) families (Fowlkes et al, 1994;Maile and Holly, 1999;Bunn and Fowlkes, 2003;Fang et al, 2004;Burger et al, 2005;Nakamura et al, 2005). The latter two families are involved in the regulation of other growth factor families through the shedding of ectodomains of membrane-anchored growth factors, cytokines and receptors to increase their circulating forms (Gomis-Rü th et al, 1998;Overall and Ló pez-Otín, 2002;Arribas and Merlos-Suá rez, 2003;Blobel, 2005).…”

Section: Introductionmentioning

confidence: 99%

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Activity of ulilysin, an archaeal PAPP-A-related gelatinase and IGFBP protease

Tallant

García‐Castellanos

Marrero

et al. 2007

BCHM

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Human growth and development are conditioned by insulin-like growth factors (IGFs), which have also implications in pathology. Most IGF molecules are sequestered by IGF-binding proteins (IGFBPs) so that exertion of IGF activity requires disturbance of these complexes. This is achieved by proteolysis mediated by IGFBP proteases, among which the best characterised is human PAPP-A, the first member of the pappalysin family of metzincins. We have previously identified and studied the only archaeal homologue found to date, Methanosarcina acetivorans ulilysin. This is a proteolytically functional enzyme encompassing a pappalysin catalytic domain and a pro-domain involved in maintenance of latency of the zymogen, proulilysin. Once activated, the protein hydrolyses IGFBP-2 to -6 and insulin chain b in vitro. We report here that ulilysin is also active against several other substrates, viz (azo)casein, azoalbumin, and extracellular matrix components. Ulilysin has gelatinolytic but not collagenolytic activity. Moreover, the proteolysis-resistant skeletal proteins actin and elastin are also cleaved, as is fibrinogen, but not plasmin and a1-antitrypsin from the blood coagulation cascade. Ulilysin develops optimal activity at pH 7.5 and strictly requires peptide bonds preceding an arginine residue, as determined by means of a novel fluorescence resonance energy transfer assay, thus pointing to biotechnological applications as an enzyme complementary to trypsin.These two authors contributed equally to this work. a

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“…IGFBP7 was identified as one of the genes overexpressed in senescent human mammary epithelial cells (HMEC) (10 fold higher than quiescent cells of the same origin), and which was upregulated in normal mammary epithelial cells by all-trans-retinoic acid [34,80]. We cloned the gene for IGFBP7 by subtractive hybridization from the Hs568T breast cancer cell line and found IGFBP7 to be downregulated in primary breast cancer tissues.…”

Section: Breast Cancermentioning

confidence: 99%