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Abstract The insulin-like growth factor (IGF) signaling pathway may be of importance for the proliferation of different tumours (e.g. breast cancer and Wilms tumour). The bioavailability of both IGF-I...
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Title of Dissertation: FUNCTION OF INSULIN-LIKE GROWTH FACTOR BINDING PROTEIN 7(IGFBP7) IN HEPATOCELLULAR CARCINOMA By Dong Chen. Purpose: Hepatocellular carcinoma (HCC) is a highly virulent malignancy with no effective treatment, thus requiring the development of innovative and effective targeted therapies. The oncogene Astrocyte Elevated Gene-1 (AEG-1) plays a seminal role in hepatocarcinogenesis and profoundly downregulates Insulin-like Growth Factor Binding Protein-7 (IGFBP7). The present study focuses on analyzing potential tumor suppressor functions of IGFBP7 in HCC and the relevance of IGFBP7 downregulation in mediating AEG-1 function. Experimental Design: IGFBP7 expression was detected by immunohistochemistry in HCC tissue microarrays by real-time PCR and ELISA in human HCC cell lines. Dual Fluorescence in situ hybridization was performed to detect loss of heterozygosity at the IGFBP7 locus. Stable IGFBP7- overexpressing clones were established in the background of AEG-1- overexpressing human
TY - JOUR. T1 - Biochemical analysis of prostate specific antigen-proteolyzed insulin-like growth factor binding protein-3. AU - Fielder, P. J.. AU - Rosenfeld, R. G.. AU - Graves, H. C.B.. AU - Grandbois, K.. AU - Maack, C. A.. AU - Sawamura, S.. AU - Ogawa, Y.. AU - Sommer, A.. AU - Cohen, P.. PY - 1994/12/1. Y1 - 1994/12/1. N2 - Prostate specific antigen (PSA) has been shown to proteolyze. IGFBP-3. However, the cleavage sites and mechanism of proteolysis are unknown. In this study, we proteolyzed recombinant human IGFBP-3 with PSA bound to a solid phase support. The reaction mixture was separated by centrifugation, with PSA remaining in the solid phase and the proteolyzed IGFBP-3 in the aqueous phase, The IGPBP-3 fragments were functionally analyzed by affinity labeling and Western ligand blotting (WLB). Further biochemical analyses were provided by silver staining of total protein and Western immunoblotting (WIB) of immunoreactive fragments with an IGFBP-3 specific antiserum (α-BP-3 gl). ...
The views presented here are those of the author and are not to be construed as official or reflecting the views of the Uniformed Services University of the Health Sciences, the Department of Defense or the U.S. Government ...
Methods of treating a tumor in a subject include identifying a subject having, at risk for, or suspected of having a tumor, and administering to the subject an effective amount of an IGFBP7 agent if t
Plasmid constructions. The IGFBP-3 sequences were excised from pSF202, pSF210, pSF211, and pSF207 containing the sequences for IGFBP-3 wild type, IGFBP-3KED253-255RGD, IGFBP-3 228KGRKR232NLS228MDGEA232, and IGFBP-3 Δ185-264, respectively ( 20) by NheI/HindIII and inserted into the cytomegalovirus (CMV) promoter-driven expression vector pX using SpeI/HindIII to generate pXIGFBP-3, pXIGFBP-3KED253-255RGD, and pXIGFBP-3 228KGRKR232NLS228MDGEA232. pXΔls-IGFBP-3 plasmids series: (a) To generate a new ATG start-site for the IGFBP-3 open reading frames without signal peptide (Δls), the oligonucleotide 5′-AATTCCATATGGGCGCGAGCTCGATATCA-3′ (MWG Biotech, Ebersberg, Germany) was inserted into the plasmid pUC19 digested with EcoRI and HindIII. The resulting plasmid is referred to pUC19-ATGnew. (b.1) To generate pXΔls-IGFBP-3, pXΔls-IGFBP-3KED253-255RGD, and pXΔls-IGFBP-3228KGRKR232NLS228MDGEA232, the plasmids pSF202, pSF210, and pSF211 were digested with HindIII and partially digested with SacI, ...
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TY - JOUR. T1 - Measurement of insulin-like growth factor-II in physiological fluids and tissues. II. extraction and quantification in rat tissues. AU - Lee, Wei Hua. AU - Bowsher, Ronald R.. AU - Apathy, John M.. AU - Smith, Michele C.. AU - Henry, David P.. PY - 1991/2. Y1 - 1991/2. N2 - The tissue distribution and developmental patterns of insulin-like growth factor-II (IGF-II) have not been investigated in rat tissues, primarily because of the lack of an efficient extraction method for IGF-II and a sensitive RIA. IGF- II was extracted from rat tissues by formic acid, and the extract was heated at an acidic pH and treated with acetone. The removal of binding proteins was demonstrated by fast protein liquid chromatography size exclusion column and the elimination of a dilutional bias in the RIA. Using rat IGF-II as standard, we optimized a RIA for the quantification of IGF-II in rat tissues. In adult rats, IGF-II was found in all 15 tissues examined, with the highest concentration in the ...
Rabbit anti Human IGFBP-5 antibody recognizes human Insulin-like growth factor-binding protein 5, also known as IGFBP-5 or IGF-binding pro
IGFBP7 antibody [3N37] (insulin-like growth factor binding protein 7) for WB. Anti-IGFBP7 mAb (GTX52799) is tested in Human samples. 100% Ab-Assurance.
IGFBP3 (phospho Ser183) antibody (insulin-like growth factor binding protein 3) for WB. Anti-IGFBP3 (phospho Ser183) pAb (GTX55408) is tested in Human, Rat samples. 100% Ab-Assurance.
The protein encoded by this gene is a member of the DOK family of membrane proteins, which are adapter proteins involved in signal transduction. The encoded protein interacts with phosphorylated receptor tyrosine kinases to mediate neurite outgrowth and activation of the MAP kinase pathway. Unlike other DOK family proteins, this protein does not interact with RASGAP. This protein is up-regulated in patients with systemic sclerosis and is associated with fibrosis induced by insulin-like growth factor binding protein 5. Alternative splicing of this gene results in multiple transcript variants. [provided by RefSeq, Jun 2014 ...
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TY - JOUR. T1 - Insulin-like growth factor binding protein-6 (IGFBP-6) interacts with DNA-end binding protein Ku80 to regulate cell fate. AU - Iosef, Cristiana. AU - Vilk, Gregory. AU - Gkourasas, Theofanis. AU - Lee, Kyung Jong. AU - Chen, Benjamin P C. AU - Fu, Ping. AU - Bach, Leon A.. AU - Lajoie, Gilles. AU - Gupta, Madhulika B.. AU - Li, Shawn S C. AU - Han, Victor K.. N1 - Funding Information: This work was supported by grants from the Canadian Institutes of Health Research and the Canada Research Chairs Program (to V.K.M.H. and S.S.-C.L.); and Cancer Council Victoria (to L.A.B.).. PY - 2010/7. Y1 - 2010/7. N2 - Insulin-like growth factor binding protein-6 (IGFBP-6) is a growth inhibitory protein that regulates the availability of insulin-like growth factors (IGFs). We recently reported that IGFBP-6 exerts intracellular actions via its translocation to the nucleus. We now show that IGFBP-6 co-purifies by tandem-affinity with nuclear proteins involved in DNA stability and repair such as ...
Insulin-like growth factor binding protein-6 (IGFBP-6) is a growth inhibitory protein that regulates the availability of insulin-like growth factors (IGFs). We recently reported that IGFBP-6 exerts intracellular actions via its translocation to the nucleus. We now show that IGFBP-6 co-purifies by tandem-affinity with nuclear proteins involved in DNA stability and repair such as Ku80, Ku70, histone H2B and importin-alpha. Furthermore, this report shows that IGFBP-6 and Ku80 interact specifically using two active binding sites for Ku80 in IGFBP-6. One of the binding sites [196RKR199], as part of the NLS-sequence in IGFBP-6 also binds importin-alpha which may selectively compete with Ku80 regulating its trafficking to the nucleus. Moreover, IGFBP-6 co-localized with Ku80 based on a cell cycle pattern. Overexpression of IGFBP-6 increased the nuclear Ku80 in mitotic cells and reduced it post-mitosis. It is known that if highly expressed IGFBP-6 induces apoptosis and in our model, the down-regulation of Ku80
The insulin-like growth factors (IGFs), their receptors, and their binding proteins play key roles in regulating cell proliferation and apoptosis. Insulin-like growth factor binding protein-3 (IGFBP3, OMIM #146732) is one of the proteins that bind to the IGFs. IGFBP3 is a modulator of IGF bioactivity, and direct growth inhibitor in the extravascular tissue compartment. We identified twenty-two novel single nucleotide polymorphisms (SNPs) in IGFBP3 gene in Korean cattle (Hanwoo, Bos taurus coreanae) by direct sequencing of full gene including -1,500 bp promoter region. Among the identified SNPs, five common SNPs were screened in 650 Korean cattle; one SNP in promoter (IGFBP3 G-854C), one in 5`UTR region (IGFBP3 G-100A), two in intron 1 (IGFBP3 G+421T, IGFBP3 T+1636A), and one in intron 2 (IGFBP3 C+3863A). The frequencies of each SNP were 0.357 (IGFBP3 G-854C), 0.472 (IGFBP3 G-100A), 0.418 (IGFBP3 G+421T), 0.363 (IGFBP3 T+1636A) and 0.226 (IGFBP3 C+3863A), respectively. Haplotypes and their ...
Expression of insulin-like growth factor binding protein 5 (IGFBP5) is strongly induced upon activation of hepatic stellate cells and their transdifferentiation into myofibroblasts in vitro. This was confirmed in vivo in an animal model of liver fibrosis. Since IGFBP5 has been shown to promote fibrosis in other tissues, the aim of this study was to investigate its role in the progression of liver fibrosis. The effect of IGFBP5 was studied in LX2 cells, a model for partially activated hepatic stellate cells, and in human primary liver myofibroblasts. IGFBP5 signalling was modulated by the addition of recombinant protein, by lentiviral overexpression, and by siRNA mediated silencing. Furthermore, the addition of IGF1 and silencing of the IGF1R was used to investigate the role of the IGF-axis in IGFBP5 mediated effects. IGFBP5 enhanced the survival of LX2 cells and myofibroblasts via a |50% suppression of apoptosis. This effect of IGFBP5 was not modulated by the addition of IGF1, nor by silencing of the
Insulin-like growth factor binding protein-3 (IGFBP-3) has both IGF-dependent and -independent effects on cell growth, which are frequently growth-inhibitory. Interestingly, the development of a more aggressive phenotype in breast cancer cells (BCCs) correlates positively with elevated expression of IGFBP-3 and is often associated with all-trans-retinoic acid (atRA)-resistance. IGFBP-3 was previously demonstrated to interact directly with retinoid X receptor (RXR). In this study we have shown that IGFBP-5 also interacts with RXR and that both IGFBPs interact with retinoic acid receptor (RAR). To investigate whether the presence of IGFBP-3 regulates breast cancer cell responsiveness to atRA, we immuno-neutralized the IGFBP-3 expressed by the atRA-resistant Hs578T and MDA-MB-231 BCCs (which express IGFBP-3 constitutively) and showed that they become more sensitive to the growth-inhibitory effects of atRA. Similarly, in Hs578T cells expressing a reporter gene under the control of an RAR response element
AIM: To investigate the role of insulin-like growth factor binding protein-7 (IGFBP-7) in the activation and transdifferentiation of hepatic stellate cells (HSC) in vitro. METHODS: Rat HSC-T6 cells were cultured in separate dishes and treated with various concentration of transforming growth factor (TGF)-β1, IGFBP-7 or anti-IGFBP-7 antibody for 24 h. The supernatant or a cytoplasm suspension was obtained from cultured HSC, followed by transfer of cells to form cell-coated dishes. Immunocytochemistry and Western blotting were used to analyze the expression of IGFBP-7 induced by TGF-β1 and the level of fibronectin, collagen I and (α-smooth muscle actin (SMA). The pro-apoptotic effect of anti-IGFBP-7 antibody was determined by flow cytometry. RESULTS: Immunocytochemistry and Western blotting revealed that the expression of IGFBP-7 in TGF-β1 treated HSC was significantly up-regulated compared to that in the control group. In addition, fibronectin, collagen I and α-SMA also showed ...
Borai, A, Livingstone, C, Mehta, S, Zarif, H, Abdelaal, F and Ferns, G (2009) Biological variation in fasting serum insulin-like growth factor binding protein-1 (IGFBP-1) among individuals with a varying glucose tolerance ...
We have investigated the expression and secretion of insulin-like growth factor binding proteins (IGFBPs-1 to -6) in human vascular smooth muscle cells (hVSMCs) cultured from human renal arteries. Solution hybridization was used to determine IGFBP nRNA levels and Western immunoblot to detect the corresponding peptides. The hVSMCs expressed mRNAs for IGFBPs-2 to -6, IGFBP-1 mRNA was not detected. IGFBPs-3, -4 and -6 mRNAs were the most abundant, IGFBP-5 was also highly expressed, whereas the IGFBP-2 mRNA was just above the limit of detection. Serum starvation for 48 h significantly decreased the mRNA levels of IGFBPs-2 to -5 and tended to decrease IGFBP-6 mRNA also. IGFBPs-2, -4, -5 and -6 peptides could be detected in conditioned medium, but IGFBP-3 peptide was not detected. IGFBP-4 was the only peptide detected without any concentration step. Low-molecular-mass immunoreactive degradation products were found for IGFBPs-2 and -4. Exogenous IGFBPs-1, -3 and -4 in concentrations of 50 ng/ml ...
Insulin-like growth factor binding protein-1 predicts preterm premature rupture of membranes in twin pregnancies Academic Article ...
We have previously demonstrated that insulin-like growth factor binding protein-5 (IGFBP-5) is upregulated following treatment of the mouse mammary epithelial cell line HC11 with lactogenic hormones (dexamethasone, insulin, and prolactin-DIP). In addition, we have also shown that IGFBP-5 is upregulated in mammary epithelial cells in vivo during involution of the rodent mammary gland. We have, therefore, postulated that there may be a dual regulation of IGFBP-5 expression during the temporally separated processes of differentiation and apoptosis of mammary epithelial cells. To test this hypothesis further, we have used a phenotypically differentiated model, which comprises primary cultures of mouse mammary epithelial cells grown on a layer of EHS (Engelbreth-Holm-Swarm) extracellular matrix. We show that lactogenic hormone treatment hydrocortisone, insulin, and prolactin-HIP) of these cultures induces the upregulation of IGFBP-5 thus replicating the results obtained with the HC11 cell line. In ...
The present study establishes the cellular sites of expression of several components of the IGF system in adult rat liver, a predominant source of circulating IGF-I in adult rat and other mammals (17, 19). As expected, IGF-I mRNA was highly expressed in hepatocytes. IGF-I mRNAs were also demonstrated in Kupffer cells and hepatic endothelial cells. These findings indicate that IGF-I secreted from nonparenchymal cells may contribute to the circulating pool of IGF-I derived from liver, albeit at lower levels than IGF-I derived from hepatocytes. Kupffer and endothelial cells play a key role in immune recognition, cytokine production, and immune cell recruitment within the liver (11). In other systems, IGF-I expression by macrophages and endothelial cells may participate in processes such as wound healing (28) and vascular repair after endothelial damage (43) and in the pathogenesis of pulmonary and intestinal fibrosis (29, 51). Our present findings raise the possibility that IGF-I derived from ...
CTGF is a cysteine-rich mitogen secreted by human umbilical vein endothelial (HUVE) cells. It was initially purified from conditioned media of HUVE cells subjected to PDGF-IgG affinity chromatography, but it was shown to not be composed of PDGF A or B chain peptides (10). Subsequent expression screening of an HUVE cell cDNA library with the anti-PDGF antibody led to the cloning and sequencing of a cDNA with an open reading frame encoding a 38-kDa protein (10). This cysteine-rich protein was shown to be the major PDGF-related mitogen and chemotactic factor secreted by HUVE cells and to compete with PDGF for binding to the PDGF cell-surface receptor on fibroblasts (10, 22). CTGF has, in fact, little peptide sequence homology with PDGF; it is believed that CTGF and PDGF monomers must share ternary structure, resulting in both common antigenic epitopes and competition for receptor binding. CTGF contains 39 cysteine residues, suggesting the presence of multiple intramolecular disulfide bonds and a ...
Background: Immunization against self-antigens can induce regulatory responses that inhibit the development of desirable Type I antitumor immune responses. Removing epitopes that bias toward a regulatory phenotype may enhance vaccine efficacy. We developed a novel IGFBP-2 targeting DNA plasmid vaccine capable of selectively inducing Type I immunity. IGFBP-2 is an important regulator of ovarian cancer invasiveness and metastases. Eradication of cancer cells expressing IGFBP-2 through effective immunization could prevent disease relapse or metastatic spread. Methods: In a single-arm non-randomized study of advanced stage (III/IV) or recurrent ovarian cancer patients treated to complete remission after primary or salvage therapy, 25 patients received 3 monthly doses of an IGFBP-2 DNA vaccine by intradermal injection. All adverse events (AE) were reported using the Common Terminology Criteria for Adverse Events Version 4.0. Overall survival (OS) was analyzed using the Kaplan-Meier method. ELISPOT ...
Allander SV، Larsson C، Ehrenborg E، Suwanichkul A، Weber G، Morris SL، Bajalica S، Kiefer MC، Luthman H، Powell DR (May 1994). Characterization of the chromosomal gene and promoter for human insulin-like growth factor binding protein-5. J Biol Chem. 269 (14): 10891-8. PMID 7511611. الوسيط ...
1657 The effects of insulin-like growth factor binding protein-5 (IGFBP-5) on pancreatic cancer (PaC) cell lines transfected with vector (/Vec) or expressing a low (/BP5L) or high (/BP5H) level of IGFBP-5 showed that IGFBP-5 can inhibit (PANC-1) or enhance (MIA PaCa-2 and BxPC-3) cell growth. Cell cycle analysis revealed that in PANC-1 cells, IGFBP-5 induced G2/M cell cycle arrest independent of growth conditions. In MIA PaCa-2 cells, IGFBP-5 expression resulted in fewer cells in S phase compared to control cells (with or without serum) and an increase of cells in G2/M under normal growth conditions; whereas an increase of cells in G0/G1 was observed under serum-free conditions. In BxPC-3 cells grown with serum IGFBP-5 expression produced fewer cells in G0/G1 and an increase of cells in S phase. When grown without serum these effects were enhanced and lead to an increase of cells in G2/M. The PI3K and MAPK pathways were examined by western analysis to detect the activation status of Akt or ...
J:20162 Schuller AG, Groffen C, van Neck JW, Zwarthoff EC, Drop SL, cDNA cloning and mRNA expression of the six mouse insulin-like growth factor binding proteins. Mol Cell Endocrinol. 1994 Aug;104(1):57-66 ...
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TY - JOUR. T1 - Structural and immunological comparison of insulin-like growth factor binding proteins of cerebrospinal and amniotic fluids. AU - Rosenfeld, R. G.. AU - Pham, H.. AU - Conover, Cheryl A. AU - Hintz, R. L.. AU - Baxter, R. C.. PY - 1989. Y1 - 1989. N2 - The insulin-like growth factors (IGFs) found in plasma and a variety of other body fluids are complexed to specific binding proteins (BPs). The cDNA for a 25K IGF-BP was recently cloned and sequenced, and the primary structure of the BP deduced. This BP is found in amniotic fluid, decidual tissues, conditioned medium from HepG2 human hepatoma cells, and fetal plasma. An additional small IGF-BP has been identified in human cerebrospinal fluid (CSF). We now demonstrate that the IGF-BP found in CSF is structurally and immunologically distinct from that found in HepG2 conditioned medium. While the latter BP has approximately equal affinities for IGF-I, and -II, the CSF BP has a 10- to 20-fold greater affinity for IGF-II. In affinity ...
The primary aim of this text is to gain insight on how cellular activation by a insulin-like growth factor (IGF-I), in the presence of insulin-like growth factor binding protein-3 (IGFBP-3), is influenced by heparan sulfate proteoglycans (HSPG). Initial research will be presented, assumptions and hypotheses that were included in the development of mathematical models will be discussed, and the future enhancements of the models will be explored. There are many potential scenarios for how each component might influence the others. Mathematical modeling techniques will highlight the contributions made by numerous extracellular parameters on IGF-I cell surface binding. Tentative assumptions can be applied to modeling techniques and predictions may aid in the direction of future experiments. Experimentally, it was found that IGFBP-3 inhibited IGF-I Bovine Aortic Endothelial (BAE) cell surface binding while p9 HS slightly increased IGF-I BAE cell surface binding. IGFBP-3 has a higher binding affinity ...
TY - JOUR. T1 - Circulating insulin-like growth factor-I, insulin-like growth factor binding protein-3 and terminal duct lobular unit involution of the breast. T2 - A cross-sectional study of women with benign breast disease. AU - Horne, Hisani N.. AU - Sherman, Mark E.. AU - Pfeiffer, Ruth M.. AU - Figueroa, Jonine D.. AU - Khodr, Zeina G.. AU - Falk, Roni T.. AU - Pollak, Michael. AU - Patel, Deesha A.. AU - Palakal, Maya M.. AU - Linville, Laura. AU - Papathomas, Daphne. AU - Geller, Berta. AU - Vacek, Pamela M.. AU - Weaver, Donald L.. AU - Chicoine, Rachael. AU - Shepherd, John. AU - Mahmoudzadeh, Amir Pasha. AU - Wang, Jeff. AU - Fan, Bo. AU - Malkov, Serghei. AU - Herschorn, Sally. AU - Hewitt, Stephen M.. AU - Brinton, Louise A.. AU - Gierach, Gretchen L.. PY - 2016/2/18. Y1 - 2016/2/18. N2 - Background: Terminal duct lobular units (TDLUs) are the primary structures from which breast cancers and their precursors arise. Decreased age-related TDLU involution and elevated mammographic ...
Insulin-like growth factor binding proteins (IGFBPs) are known to be important modulators of the insulin-like growth factor (IGF-I). However, their precise role is as yet unclear. Further, recent studies have indicated that IGFBP-3 has a receptor mediated growth inhibitory response of its own. In the present study, we quantified the binding characteristics of IGFBP-3 to bovine aortic endothelial (BAE) cells. Binding studies at 4 oC were conducted and a specific binding curve for IGFBP-3 was obtained. IGFBP-3 was found to bind with an equilibrium dissociation constant (KD) value of 3.1 x 10-10 M. The role of heparan sulfate proteoglycans (HSPG) in the IGFBP-3 binding mechanism was also examined. It was seen that inactivation of the cell surface HSPGs with 75 mM sodium chlorate did not affect IGFBP-3 binding. Further, there have been reports of inhibition of IGFBP-3 binding by heparin in the media. Hence, the most probable interaction of HSPG with IGFBP-3 occurs in the extracellular region, with ...
Insulin-like growth factor-binding protein 6 contains a PF00086 domain.. Insulin-like growth factor-binding protein 6 contains a PF00219 domain.. Insulin-like growth factor-binding protein 6 is proteolytically cut by matrix metallopeptidase-2 (M10.003) cleavage. CLRR-EGQP.. ...
The actions and bioavailability of the insulin-like growth factors (IGFs) are regulated by a family of six IGF binding proteins. IGFBP-3, the major circulating IGFBP, is unique in combining with a glycoprotein, the acid-labile subunit (ALS), to form a ternary complex with IGF-I or IGF-II. Each compo …
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Insulin-like growth factor (IGF) binding protein-1 (BP-1) inhibits IGF-mediated proliferation of some breast cancer cell lines in vitro. Here we examined whether recombinant human wild-type IGFBP-1 (WT-BP-1) and IGFBP-1 conjugated with polyethylene glycol (PEG-BP-1) could inhibit breast cancer growt …
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In this analysis of women with BBD, we observed an inverse association between plasma IGF-1 and the IGF-1:IGFBP-3 ratio with predominant type 1/no type 3 lobules. Interestingly, only IGF-1 levels in the highest quartile were associated with a decreased odds of predominant type 1/no type 3 lobules, suggesting a potential threshold effect. However, we observed more of a linear trend for the IGF-1:IGFBP-3 ratio, which may better represent available IGF-1. The results did not materially change when we restricted our analysis to parous women or premenopausal women (Supplemental Tables 2 to 4 in Additional file 1).. Our findings are consistent with a study reporting that transgenic mice with IGF-1 overexpression in mammary tissue had inhibited postlactational involution [6]. In vivo studies in animals suggest that inhibition of postlactational involution increases the risk of subsequent mammary tumors [16]. In addition, recent studies in women have found that lobule type or degree of age-related ...
anti-Insulin-Like Growth Factor Binding Protein, Acid Labile Subunit (IGFALS) (Middle Region) antibody ABIN634631 from antibodies-online
The insulin-like growth factor-II/mannose-6-phosphate (IGF-II/M6P) receptor is a multifunctional transmembrane glycoprotein, which interacts with a number of molecules, including IGF-II and M6P-containing lysosomal enzymes. The receptor is widely distributed throughout the brain and is known to be involved in lysosomal enzyme trafficking, cell growth, internalization and degradation of IGF-II. In the present study, using autoradiographic, Western blotting and immunocytochemical methods, we provide the first report that IGF-II/M6P receptors are discretely distributed at all major segmental levels of the spinal cord and dorsal root ganglia of the adult rat. In the spinal cord, a high density of [125I]IGF-II binding sites was evident in the ventral horn (lamina IX) and in areas around the central canal (lamina X), whereas intermediate grey matter and dorsal horn were associated with moderate receptor levels. The dorsal root ganglia exhibited rather high density of [125I]IGF-II binding sites. ...
Insulin-like growth factor binding protein-5 (IGFBP-5) is an osteoblast secretory protein that becomes incorporated into the mineralized bone matrix. In osteoblast cultures, IGFBP-5 stimulates cell proliferation by an IGF-independent mechanism. To ev
IGFBP3 - IGFBP3 (untagged)-Human insulin-like growth factor binding protein 3 (IGFBP3), transcript variant 1 available for purchase from OriGene - Your Gene Company.
IGFBP1 - IGFBP1 (untagged)-Human insulin-like growth factor binding protein 1 (IGFBP1) available for purchase from OriGene - Your Gene Company.
This gene is a member of the insulin-like growth factor binding protein (IGFBP) family and encodes a protein with an IGFBP domain and a thyroglobulin type-I domain. The protein binds both insulin-like growth factors (IGFs) I and II and circulates in the plasma. Binding of this protein prolongs the half-life of the IGFs and alters their interaction with cell surface receptors. [provided by RefSeq, Jul 2008 ...
IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors. Activates the MAPK signaling pathway and induces cell migration.
IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors.
IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors ...
PAPPA Full-Length MS Protein Standard (NP_002572), Labeled with [U- 13C6, 15N4]-L-Arginine and [U- 13C6, 15N2]-L-Lysine, was produced in human 293 cells (HEK293) with fully chemically defined cell culture medium to obtain incorporation efficiency at Creative-Proteomics. This gene encodes a secreted metalloproteinase which cleaves insulin-like growth factor binding proteins (IGFBPs). It is thought to be involved in local proliferative processes such as wound healing and bone remodeling. Low plasma level of this protein has been suggested as a biochemical marker for pregnancies with aneuploid fetuses.
The longer a person lives with diabetes, the higher their risk of digestive issues. For a long time, it was unclear why, but an international study has found a possible culprit. Study researchers believe they have found that the liver of a person with Type 1 may produce an excessive amount of a protein that can hamper digestion, according to a Science Daily report.. By comparing the intestinal tissue of people with and without diabetes, researchers realized that the cells lining the intestinal tract of people with diabetes were damaged by a substance called insulin-like growth factor binding protein 3 (IGFBP3). Excess IGFBP3 can cause gastrointestinal issues like irritable bowel syndrome, delayed bowel movements, bloating, and lack of bowel control; collectively, these problems are known as diabetic enteropathy. IGFBP3 cells attach themselves to colonic stem cells, which are coincidentally responsible for repairing wounds in the intestinal lining. As these stem cells are damaged, they lose the ...
J:58580 van Kleffens M, Groffen CA, Dits NF, Lindenbergh-Kortleve DJ, Schuller AG, Bradshaw SL, Pintar JE, Zwarthoff EC, Drop SL, van Neck JW, Generation of antisera to mouse insulin-like growth factor binding proteins (IGFBP)-1 to -6: comparison of IGFBP protein and messenger ribonucleic acid localization in the mouse embryo. Endocrinology. 1999 Dec;140(12):5944-52 ...
Loss of Imprinting of Insulin-like Growth Factor-II in Wilms Tumor Commonly Involves Altered Methylation but not Mutations of CTCF or Its Binding ...
Low serum levels of insulin-like growth factor-1 (IGF-1) and insulin-like growth factor binding protein-3 (IGFBP-3) are associated with Alzheimers Disease in men, but not women, according to a recent study accepted for publication ...
TY - JOUR AU - Resanović, Ivana AU - Gluvić, Zoran AU - Zarić, Božidarka AU - Sudar-Milovanović, Emina AU - Vučić, Vesna AU - Arsić, Aleksandra AU - Nedić, Olgica AU - Šunderić, Miloš AU - Gligorijević, Nikola AU - Milačić, Davorka AU - Isenović, Esma R. PY - 2020 UR - http://vinar.vin.bg.ac.rs/handle/123456789/8567 T2 - Canadian Journal of Diabetes T1 - Effect of Hyperbaric Oxygen Therapy on Fatty Acid Composition and Insulin-like Growth Factor Binding Protein 1 in Adult Type 1 Diabetes Mellitus Patients: A Pilot Study VL - 44 IS - 1 SP - 22 EP - 29 DO - 10.1016/j.jcjd.2019.04.018 ER ...
IGFB3 : Container/Tube: Preferred: Red top Acceptable: Serum gel Specimen Volume: 0.8 mL Collection Instructions: Spin down promptly. Additional Information: Indicate patients age and sex.
Sigma-Aldrich offers abstracts and full-text articles by [Qiang You, Yan Wu, Nannan Yao, Guannan Shen, Ying Zhang, Liangguo Xu, Guiying Li, Cynthia Ju].
The KOMP Repository is located at the University of California Davis and Childrens Hospital Oakland Research Institute. Question? Comments? For Mice, Cells, and germplasm please contact us at [email protected], US 1-888-KOMP-MICE or International +1-530-752-KOMP, or for vectors [email protected] or +1-510-450-7917 ...
AMP-IBP5 (Human) Insulin-Like Growth Factor-Binding Protein 5 (Human, 193-214 Amide)(Porcine, Rat, Mouse, Bovine)4468-s 0.1 mg | 100.00 EUR ...
check for insulin growth factor-1 (IGF-1) and insulin growth factor binding proteins (IGFBP) as relevant intermediate biomarkers for prostate ...