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Article ; Online: IGFBP-3: a cell fate pivot in cancer and disease.

Johnson, Michael A / Firth, Sue M

Growth hormone & IGF research : official journal of the Growth Hormone Research Society and the International IGF Research Society

2014 Volume 24, Issue 5, Page(s) 164–173

Abstract: One of the hallmarks in the advancement of cancer cells is an ability to overcome and acquire resistance to adverse conditions. There has been a large amount of cancer research on IGFBP-3 as a pro-apoptotic molecule in vitro. These pro-apoptotic ... ...

Abstract	One of the hallmarks in the advancement of cancer cells is an ability to overcome and acquire resistance to adverse conditions. There has been a large amount of cancer research on IGFBP-3 as a pro-apoptotic molecule in vitro. These pro-apoptotic properties, however, do not correlate with several studies linking high IGFBP-3 levels in breast cancer tissue to rapid growth and poor prognosis. Evidence is emerging that IGFBP-3 also exhibits pro-survival and growth-promoting properties in vitro. How IGFBP-3 pivots cell fate to either death or survival, it seems, comes down to a complex interplay between cells' microenvironments and the presence of cellular IGFBP-3 binding partners and growth factor receptors. The cytoprotective actions of IGFBP-3 are not restricted to cancer but are also observed in other disease states, such as retinopathy and brain ischaemia. Here we review the literature on this paradoxical nature of IGFBP-3, its pro-apoptotic and growth-inhibitory actions versus its cytoprotective and growth-potentiating properties, and discuss the implications of targeting IGFBP-3 for treatment of disease.
MeSH term(s)	Animals ; Apoptosis/genetics ; Cell Differentiation/genetics ; Cell Proliferation/genetics ; Disease/genetics ; Endoplasmic Reticulum/metabolism ; Genes, Switch ; Humans ; Insulin-Like Growth Factor Binding Protein 3/physiology ; Neoplasms/genetics
Chemical Substances	IGFBP3 protein, human ; Insulin-Like Growth Factor Binding Protein 3
Language	English
Publishing date	2014-10
Publishing country	Scotland
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1436781-6
ISSN	1532-2238 ; 1096-6374
ISSN (online)	1532-2238
ISSN	1096-6374
DOI	10.1016/j.ghir.2014.04.007
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Zs.A 3319: Show issues

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Article ; Online: Involvement of insulin-like growth factor binding protein-3 in peroxisome proliferator-activated receptor gamma-mediated inhibition of breast cancer cell growth.

Pon, Cindy K / Firth, Sue M / Baxter, Robert C

Molecular and cellular endocrinology

2015 Volume 399, Page(s) 354–361

Abstract: We have previously reported that insulin-like growth factor binding protein-3 (IGFBP-3), a protein with dichotomous effects on both cell proliferation and cell survival, interacts with peroxisome proliferator-activated receptor gamma (PPARγ) and inhibits ...

Abstract	We have previously reported that insulin-like growth factor binding protein-3 (IGFBP-3), a protein with dichotomous effects on both cell proliferation and cell survival, interacts with peroxisome proliferator-activated receptor gamma (PPARγ) and inhibits adipogenic PPARγ signaling. We now show that IGFBP-3 and PPARγ interact in breast cancer cells, through amino- and carboxyl-terminal residues of IGFBP-3. IGFBP-3 and the PPARγ ligands, rosiglitazone or 15-deoxy-Δ(12,14)-prostaglandin J2, separately inhibited the proliferation of MCF-7, MDA-MB-231 and MDA-MB-468 breast cancer cells. However, growth inhibition by IGFBP-3 and PPARγ ligand combined was greater than by either alone. Two IGFBP-3 mutants with reduced PPARγ binding caused no growth inhibition when used alone and abolished the inhibitory effect of rosiglitazone when used in combination with PPARγ ligand. Cell growth inhibition by PPARγ ligands was substantially blocked by IGFBP-3 siRNA and restored by exogenous IGFBP-3. We conclude that the interaction between IGFBP-3 and PPARγ is important for the growth-inhibitory effect of PPARγ ligands in human breast cancer cells, suggesting that IGFBP-3 expression by breast tumors may regulate their sensitivity toward PPARγ ligands.
MeSH term(s)	Breast Neoplasms/genetics ; Breast Neoplasms/metabolism ; Breast Neoplasms/pathology ; Cell Line, Tumor ; Female ; Gene Expression Regulation, Neoplastic/drug effects ; Humans ; Hypoglycemic Agents/pharmacology ; Insulin-Like Growth Factor Binding Protein 3/genetics ; Insulin-Like Growth Factor Binding Protein 3/metabolism ; Mutation ; Neoplasm Proteins/agonists ; Neoplasm Proteins/genetics ; Neoplasm Proteins/metabolism ; PPAR gamma/agonists ; PPAR gamma/genetics ; PPAR gamma/metabolism ; Thiazolidinediones/pharmacology
Chemical Substances	Hypoglycemic Agents ; IGFBP3 protein, human ; Insulin-Like Growth Factor Binding Protein 3 ; Neoplasm Proteins ; PPAR gamma ; Thiazolidinediones ; rosiglitazone (05V02F2KDG)
Language	English
Publishing date	2015-01-05
Publishing country	Ireland
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	187438-x
ISSN	1872-8057 ; 0303-7207
ISSN (online)	1872-8057
ISSN	0303-7207
DOI	10.1016/j.mce.2014.10.023
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Zs.A 1127: Show issues

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Article: Dosage Sensitivity of RPL9 and Concerted Evolution of Ribosomal Protein Genes in Plants.

Devis, Deborah / Firth, Sue M / Liang, Zhe / Byrne, Mary E

Frontiers in plant science

2015 Volume 6, Page(s) 1102

Abstract: The ribosome in higher eukaryotes is a large macromolecular complex composed of four rRNAs and eighty different ribosomal proteins. In plants, each ribosomal protein is encoded by multiple genes. Duplicate genes within a family are often necessary to ... ...

Abstract	The ribosome in higher eukaryotes is a large macromolecular complex composed of four rRNAs and eighty different ribosomal proteins. In plants, each ribosomal protein is encoded by multiple genes. Duplicate genes within a family are often necessary to provide a threshold dose of a ribosomal protein but in some instances appear to have non-redundant functions. Here, we addressed whether divergent members of the RPL9 gene family are dosage sensitive or whether these genes have non-overlapping functions. The RPL9 family in Arabidopsis thaliana comprises two nearly identical members, RPL9B and RPL9C, and a more divergent member, RPL9D. Mutations in RPL9C and RPL9D genes lead to delayed growth early in development, and loss of both genes is embryo lethal, indicating that these are dosage-sensitive and redundant genes. Phylogenetic analysis of RPL9 as well as RPL4, RPL5, RPL27a, RPL36a, and RPS6 family genes in the Brassicaceae indicated that multicopy ribosomal protein genes have been largely retained following whole genome duplication. However, these gene families also show instances of tandem duplication, small scale deletion, and evidence of gene conversion. Furthermore, phylogenetic analysis of RPL9 genes in angiosperm species showed that genes within a species are more closely related to each other than to RPL9 genes in other species, suggesting ribosomal protein genes undergo convergent evolution. Our analysis indicates that ribosomal protein gene retention following whole genome duplication contributes to the number of genes in a family. However, small scale rearrangements influence copy number and likely drive concerted evolution of these dosage-sensitive genes.
Language	English
Publishing date	2015-12-16
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2711035-7
ISSN	1664-462X
ISSN	1664-462X
DOI	10.3389/fpls.2015.01102
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Article ; Online: Contrasting effects of IGF binding protein-3 expression in mammary tumor cells and the tumor microenvironment.

Scully, Tiffany / Scott, Carolyn D / Firth, Sue M / Pintar, John E / Twigg, Stephen M / Baxter, Robert C

Experimental cell research

2018 Volume 374, Issue 1, Page(s) 38–45

Abstract: IGFBP-3 has both stimulatory and inhibitory effects on cancer progression. The growth of EO771 mammary carcinoma cells as syngeneic tumors in C57BL/6 mice is reduced in Igfbp3-null (BP3KO) mice, suggesting that systemic IGFBP-3 enhances tumor progression. ...

Abstract	IGFBP-3 has both stimulatory and inhibitory effects on cancer progression. The growth of EO771 mammary carcinoma cells as syngeneic tumors in C57BL/6 mice is reduced in Igfbp3-null (BP3KO) mice, suggesting that systemic IGFBP-3 enhances tumor progression. In this study we assessed the growth of EO771 cells expressing human IGFBP-3 in BP3KO mice. Cells expressing hIGFBP-3 showed decreased proliferation in vitro and increased levels of IGF-1 receptor (IGF1R) protein but not mRNA, consistent with sequestration of endogenous IGF by IGFBP-3. The growth rate of these cells was restored by exposure to IGF-1 or analogues with reduced affinity for IGFBP-3 (long Arg
MeSH term(s)	Adaptive Immunity ; Adipose Tissue/pathology ; Animals ; Antibodies/blood ; Antibodies/metabolism ; Cell Line, Tumor ; Cell Proliferation ; Female ; Gene Expression Regulation, Neoplastic ; Humans ; Insulin-Like Growth Factor Binding Protein 3/metabolism ; Lymphocytes, Tumor-Infiltrating/immunology ; Mammary Neoplasms, Animal/blood ; Mammary Neoplasms, Animal/genetics ; Mammary Neoplasms, Animal/metabolism ; Mammary Neoplasms, Animal/pathology ; Mice, Inbred C57BL ; Mice, Knockout ; Tumor Microenvironment/immunology
Chemical Substances	Antibodies ; Insulin-Like Growth Factor Binding Protein 3
Language	English
Publishing date	2018-11-09
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1493-x
ISSN	1090-2422 ; 0014-4827
ISSN (online)	1090-2422
ISSN	0014-4827
DOI	10.1016/j.yexcr.2018.11.006
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Zs.A 563: Show issues

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Article ; Online: Enhancement of mammary tumour growth by IGFBP-3 involves impaired T cell accumulation.

Scully, Tiffany / Scott, Carolyn D / Firth, Sue M / Sedger, Lisa M / Pintar, John E / Twigg, Stephen M / Baxter, Robert C

Endocrine-related cancer

2017 Volume 25, Issue 2, Page(s) 111–122

Abstract: Epidemiological studies show an association between obesity and poor breast cancer prognosis. We previously demonstrated that global IGFBP-3 deficiency, in IGFBP-3-null mice, resulted in a 50% reduction in mammary tumour growth over 3 weeks relative to ... ...

Abstract	Epidemiological studies show an association between obesity and poor breast cancer prognosis. We previously demonstrated that global IGFBP-3 deficiency, in IGFBP-3-null mice, resulted in a 50% reduction in mammary tumour growth over 3 weeks relative to tumours in wild-type (WT) C57BL/6 mice. This growth reduction was ameliorated by high fat feeding-induced obesity. This study aimed to examine how IGFBP-3 promotes tumour growth by influencing the immune tumour microenvironment in healthy and obese mice. Syngeneic EO771 cells, which lack detectable IGFBP-3 expression, were grown as orthotopic tumours in WT and IGFBP-3-null C57BL/6 mice placed on either a control chow or a high-fat diet (HFD), and examined by quantitative PCR and immunohistochemistry. In WT mice, increased stromal expression of IGFBP-3 was positively associated with tumour growth, supporting the hypothesis that IGFBP-3 in the microenvironment promotes tumour progression. Examining markers of immune cell subsets, gene expression of
MeSH term(s)	Animals ; CD8-Positive T-Lymphocytes/immunology ; Diet, High-Fat ; Female ; Gene Expression Profiling ; Insulin-Like Growth Factor Binding Protein 3/genetics ; Insulin-Like Growth Factor Binding Protein 3/immunology ; Mammary Neoplasms, Experimental/genetics ; Mammary Neoplasms, Experimental/immunology ; Mammary Neoplasms, Experimental/pathology ; Mice, Inbred C57BL ; Mice, Knockout
Chemical Substances	Insulin-Like Growth Factor Binding Protein 3
Language	English
Publishing date	2017-12-07
Publishing country	England
Document type	Journal Article
ZDB-ID	1218450-0
ISSN	1479-6821 ; 1351-0088
ISSN (online)	1479-6821
ISSN	1351-0088
DOI	10.1530/ERC-17-0384
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Zs.A 4192: Show issues

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Article ; Online: Post-weaning high-fat diet results in growth cartilage lesions in young male rats.

Haysom, Samuel S / Vickers, Mark H / Yu, Lennex H / Reynolds, Clare M / Firth, Elwyn C / McGlashan, Sue R

PloS one

2017 Volume 12, Issue 11, Page(s) e0188411

Abstract: To determine if a high-fat diet (HF) from weaning would result in a pro-inflammatory state and affect joint cartilage, we fed male rats either HF or Chow diet post-weaning, and voluntary wheel exercise (EX) or cage only activity (SED) after 9 weeks of ... ...

Abstract	To determine if a high-fat diet (HF) from weaning would result in a pro-inflammatory state and affect joint cartilage, we fed male rats either HF or Chow diet post-weaning, and voluntary wheel exercise (EX) or cage only activity (SED) after 9 weeks of age. At 17 weeks body composition, plasma biomarkers and histomorphology scores of femoro-tibial cartilages of HF-SED, HF-EX, Chow-SED and Chow-EX groups were compared. Food intake and activity were not significantly different between groups. HF diet resulted in significantly higher weight gain, %fat, fat:lean ratio, and plasma leptin, insulin and TNFα concentrations, with significant interactions between diet and exercise. No abnormal features were detected in the hyaline articular cartilage or in the metaphyseal growth plate in all four groups. However, collagen type X- positive regions of retained epiphyseal growth cartilage (EGC) was present in all HF-fed animals and significantly greater than that observed in Chow-fed sedentary rats. Most lesions were located in the lateral posterior aspect of the tibia and/or femur. The severity of lesions was greater in HF-fed animals. Although exercise had a significantly greater effect in reducing adiposity and associated systemic inflammation in HF-fed rats, it had no effect on lesion incidence or severity. Lesion incidence was also significantly associated with indices of obesity and plasma markers of chronic inflammation. Clinically, EGC lesions induced by HF feeding in rats from very early in life, and possibly by insufficient activity, is typical of osteochondrosis in animals. Such lesions may be the precursor of juvenile osteochondritis dissecans requiring surgery in children/adolescents, conservative management of which could benefit from improved understanding of early changes in cellular and gene expression.
Language	English
Publishing date	2017
Publishing country	United States
Document type	Journal Article
ISSN	1932-6203
ISSN (online)	1932-6203
DOI	10.1371/journal.pone.0188411
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: D440N mutation in the acid-labile subunit of insulin-like growth factor complexes inhibits secretion and complex formation.

Firth, Sue M / Yan, Xiaolang / Baxter, Robert C

Molecular endocrinology (Baltimore, Md.)

2010 Volume 25, Issue 2, Page(s) 307–314

Abstract: The acid-labile subunit (ALS) regulates IGF bioavailability by forming heterotrimeric complexes with IGFs and IGF-binding protein-3 (IGFBP-3). A homozygous missense mutation (D440N) resulting in undetectable circulating levels of ALS with a concomitant ... ...

Abstract	The acid-labile subunit (ALS) regulates IGF bioavailability by forming heterotrimeric complexes with IGFs and IGF-binding protein-3 (IGFBP-3). A homozygous missense mutation (D440N) resulting in undetectable circulating levels of ALS with a concomitant reduction in IGF-I and IGFBP-3 has been reported to cause mild growth retardation. To understand how this particular mutation affects ALS circulating levels and IGF-transport function, we expressed recombinant ALS and its variants, D440N-ALS, T442A-ALS, and D440N/T442A-ALS, using adenovirus vectors. Compared with wild-type ALS, the secretion of D440N-ALS was 80% lower. The D440N mutation was proposed to generate an N-glycosylation site additional to the seven existing motifs in ALS. D440N-ALS appeared larger than ALS, attributable to N-linked glycans because deglycosylation with N-glycosidase F reduced both proteins to the same molecular mass. When ALS was incubated with IGF-I and IGFBP-3, 70-80% of IGF-I was detected by gel-filtration chromatography in forms corresponding to the 150-kDa ternary complex. In contrast, when D440N-ALS was tested, less than 30% of IGF-I was found in high molecular mass complexes. Two other ALS variants mutated in the same putative glycosylation site, D440N/T442A-ALS and T442A-ALS, showed similar chromatographic profiles to wild-type ALS. The D440N mutation in ALS generates a hyperglycosylated form with impaired secretion and complex formation, potentially leading to dysregulation of endocrine IGF, thus contributing to the growth retardation observed in the affected patient. This is the first study to explain how a natural mutation, D440N, in ALS impairs its function.
MeSH term(s)	Adenoviridae/genetics ; Carrier Proteins/blood ; Carrier Proteins/genetics ; Carrier Proteins/metabolism ; Glycoproteins/blood ; Glycoproteins/genetics ; Glycoproteins/metabolism ; Glycosylation ; Humans ; Insulin-Like Growth Factor Binding Protein 3/genetics ; Insulin-Like Growth Factor Binding Protein 3/metabolism ; Insulin-Like Growth Factor I/genetics ; Insulin-Like Growth Factor I/metabolism ; Mutation, Missense ; Protein Binding ; Recombinant Proteins/metabolism
Chemical Substances	Carrier Proteins ; Glycoproteins ; Insulin-Like Growth Factor Binding Protein 3 ; Recombinant Proteins ; insulin-like growth factor binding protein, acid labile subunit ; Insulin-Like Growth Factor I (67763-96-6)
Language	English
Publishing date	2010-12-22
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	639167-9
ISSN	1944-9917 ; 0888-8809
ISSN (online)	1944-9917
ISSN	0888-8809
DOI	10.1210/me.2010-0295
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Zs.A 2261: Show issues

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Article ; Online: Involvement of pregnancy-associated plasma protein-A2 in insulin-like growth factor (IGF) binding protein-5 proteolysis during pregnancy: a potential mechanism for increasing IGF bioavailability.

Yan, Xiaolang / Baxter, Robert C / Firth, Sue M

The Journal of clinical endocrinology and metabolism

2010 Volume 95, Issue 3, Page(s) 1412–1420

Abstract: Context: During pregnancy, circulating IGF binding protein-5 (IGFBP-5) undergoes substantial molecular redistribution from ternary complexes to either binary complexes or the uncomplexed protein.: Objective: This study aimed to characterize the ... ...

Abstract	Context: During pregnancy, circulating IGF binding protein-5 (IGFBP-5) undergoes substantial molecular redistribution from ternary complexes to either binary complexes or the uncomplexed protein. Objective: This study aimed to characterize the proteolysis of circulating IGFBP-5 during pregnancy and to determine whether it can increase IGF bioavailability. Design: Biochemical methods were used to purify and characterize IGFBP-5 fragments and IGFBP-5-specific proteolytic activity from pregnancy plasma. Results: Circulating IGFBP-5 was fully proteolyzed at all stages of pregnancy. Cleavage after either Ser143 or Lys144 resulted in two complementary fragments. Of two pools of proteolytic activity (>150 kDa and approximately 40 kDa) identified in pregnancy plasma, only the greater than 150-kDa proteolytic activity was specific to pregnancy. The approximately 40-kDa proteolytic activity, also present in nonpregnancy plasma, appeared largely inactive against IGF-I-complexed IGFBP-5. The greater than 150-kDa proteolytic activity was inhibited by alpha-PAPP-A2 but not alpha-PAPP-A1 antibody, cleaved recombinant IGFBP-5 at Ser143-Lys144 similar to PAPP-A2, and was inactive against IGFBP-5 (Ala128), a PAPP-A2-resistant analog. Compared to nonpregnancy plasma, incubation with pregnancy plasma resulted in release of more bioactive IGF-I from IGF-I-IGFBP-5 complexes as measured by stimulation of IGF-I receptor phosphorylation. Conclusions: Circulating IGFBP-5 is proteolyzed by PAPP-A2 during pregnancy, resulting in increased IGF bioavailability, which may have important consequences for the development of the fetus and/or the well-being of the mother.
MeSH term(s)	Blotting, Western ; Chromatography, Gel ; Female ; Humans ; Insulin-Like Growth Factor Binding Protein 5/metabolism ; Insulin-Like Growth Factor I/metabolism ; Insulin-Like Growth Factor I/pharmacology ; Peptide Fragments/metabolism ; Phosphorylation ; Pregnancy ; Pregnancy-Associated Plasma Protein-A/metabolism ; Protein Binding ; Receptor, IGF Type 1/metabolism
Chemical Substances	Insulin-Like Growth Factor Binding Protein 5 ; Peptide Fragments ; Insulin-Like Growth Factor I (67763-96-6) ; Receptor, IGF Type 1 (EC 2.7.10.1) ; PAPPA2 protein, human (EC 3.4.-) ; Pregnancy-Associated Plasma Protein-A (EC 3.4.24.-)
Language	English
Publishing date	2010-03
Publishing country	United States
Document type	Journal Article
ZDB-ID	3029-6
ISSN	1945-7197 ; 0021-972X
ISSN (online)	1945-7197
ISSN	0021-972X
DOI	10.1210/jc.2009-2277
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Article ; Online: Post-weaning high-fat diet results in growth cartilage lesions in young male rats.

Samuel S Haysom / Mark H Vickers / Lennex H Yu / Clare M Reynolds / Elwyn C Firth / Sue R McGlashan

PLoS ONE, Vol 12, Iss 11, p e

2017 Volume 0188411

Abstract	To determine if a high-fat diet (HF) from weaning would result in a pro-inflammatory state and affect joint cartilage, we fed male rats either HF or Chow diet post-weaning, and voluntary wheel exercise (EX) or cage only activity (SED) after 9 weeks of age. At 17 weeks body composition, plasma biomarkers and histomorphology scores of femoro-tibial cartilages of HF-SED, HF-EX, Chow-SED and Chow-EX groups were compared. Food intake and activity were not significantly different between groups. HF diet resulted in significantly higher weight gain, %fat, fat:lean ratio, and plasma leptin, insulin and TNFα concentrations, with significant interactions between diet and exercise. No abnormal features were detected in the hyaline articular cartilage or in the metaphyseal growth plate in all four groups. However, collagen type X- positive regions of retained epiphyseal growth cartilage (EGC) was present in all HF-fed animals and significantly greater than that observed in Chow-fed sedentary rats. Most lesions were located in the lateral posterior aspect of the tibia and/or femur. The severity of lesions was greater in HF-fed animals. Although exercise had a significantly greater effect in reducing adiposity and associated systemic inflammation in HF-fed rats, it had no effect on lesion incidence or severity. Lesion incidence was also significantly associated with indices of obesity and plasma markers of chronic inflammation. Clinically, EGC lesions induced by HF feeding in rats from very early in life, and possibly by insufficient activity, is typical of osteochondrosis in animals. Such lesions may be the precursor of juvenile osteochondritis dissecans requiring surgery in children/adolescents, conservative management of which could benefit from improved understanding of early changes in cellular and gene expression.
Keywords	Medicine ; R ; Science ; Q
Language	English
Publishing date	2017-01-01T00:00:00Z
Publisher	Public Library of Science (PLoS)
Document type	Article ; Online
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Article: Involvement of insulin-like growth factor binding protein-3 in peroxisome proliferator-activated receptor gamma-mediated inhibition of breast cancer cell growth

Pon, Cindy K / Robert C. Baxter / Sue M. Firth

Molecular and Cellular Endocrinology. 2015 Jan. 05, v. 399

2015

Abstract	We have previously reported that insulin-like growth factor binding protein-3 (IGFBP-3), a protein with dichotomous effects on both cell proliferation and cell survival, interacts with peroxisome proliferator-activated receptor gamma (PPARÎ³) and inhibits adipogenic PPARÎ³ signaling. We now show that IGFBP-3 and PPARÎ³ interact in breast cancer cells, through amino- and carboxyl-terminal residues of IGFBP-3. IGFBP-3 and the PPARÎ³ ligands, rosiglitazone or 15-deoxy-Î12,14-prostaglandin J2, separately inhibited the proliferation of MCF-7, MDA-MB-231 and MDA-MB-468 breast cancer cells. However, growth inhibition by IGFBP-3 and PPARÎ³ ligand combined was greater than by either alone. Two IGFBP-3 mutants with reduced PPARÎ³ binding caused no growth inhibition when used alone and abolished the inhibitory effect of rosiglitazone when used in combination with PPARÎ³ ligand. Cell growth inhibition by PPARÎ³ ligands was substantially blocked by IGFBP-3 siRNA and restored by exogenous IGFBP-3. We conclude that the interaction between IGFBP-3 and PPARÎ³ is important for the growth-inhibitory effect of PPARÎ³ ligands in human breast cancer cells, suggesting that IGFBP-3 expression by breast tumors may regulate their sensitivity toward PPARÎ³ ligands.
Keywords	breast neoplasms ; cell growth ; cell proliferation ; cell viability ; humans ; ligands ; mutants ; neoplasm cells ; peroxisome proliferator-activated receptors ; small interfering RNA ; somatomedins
Language	English
Dates of publication	2015-0105
Size	p. 354-361.
Publishing place	Elsevier Ireland Ltd
Document type	Article
ZDB-ID	187438-x
ISSN	1872-8057 ; 0303-7207
ISSN (online)	1872-8057
ISSN	0303-7207
DOI	10.1016/j.mce.2014.10.023
Database	NAL-Catalogue (AGRICOLA)

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