Insulin-like growth factors and their binding proteins

Sara, Vicki R.; Hall, Kerstin

doi:10.1152/physrev.1990.70.3.591

Cited by 754 publications

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“…1B). Affinity crosslinking using labeled IGF-II followed by SDS͞PAGE, at reducing conditions, showed specific IGF-II binding to a 250-kDa protein, likely to be the IGF-II͞M-6-P receptor (3,4,7,8) (Fig. 1C).…”

Section: Resultsmentioning

confidence: 99%

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Insulin-like growth factor II signaling through the insulin-like growth factor II/mannose-6-phosphate receptor promotes exocytosis in insulin-secreting cells

Zhang

Tally

Larsson

et al. 1997

Proc. Natl. Acad. Sci. U.S.A.

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The insulin-like growth factor II (IGF-II)͞ mannose-6-phosphate (M-6-P) receptor is known to participate in endocytosis as well as sorting of lysosomal enzymes and is involved in membrane trafficking through rapid cycling between cytosolic membrane compartments and the plasma membrane. Here we demonstrate that IGF-II, acting through the IGF-II͞M-6-P receptor, promotes exocytosis of insulin in the pancreatic ␤ cell. The effect of IGF-II was evoked at nonstimulatory concentrations of glucose, was mediated by a pertussis toxin sensitive GTP-binding protein, was dependent on protein kinase C-induced phosphorylation, and was independent of changes in cytoplasmic free Ca 2؉ concentration. Since the applied concentration of IGF-II is within the range normally found free in circulation in humans, this novel signaling pathway for the IGF-II͞M-6-P receptor is likely to be involved in modulation of insulin exocytosis under physiological conditions.

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Section: Resultsmentioning

confidence: 99%

“…IGF-II circulates bound to specific IGF-binding proteins (IGFBPs) (3). IGF-II binds to the cation-independent mannose-6-phosphate (M-6-P) receptor and crossreacts, although with a lower affinity, with the insulin and the IGF-I receptors (4,5).…”

mentioning

confidence: 99%

Insulin-like growth factor II signaling through the insulin-like growth factor II/mannose-6-phosphate receptor promotes exocytosis in insulin-secreting cells

Zhang

Tally

Larsson

et al. 1997

Proc. Natl. Acad. Sci. U.S.A.

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“…Insulin-like growth factor I (IGF-I) plays crucial roles in somatic growth, cell proliferation, metabolism, and cell differentiation (Humbel 1990;Sara and Hall 1990). These general activities are relevant to the kidney because IGF-I promotes nephrogenesis (Hammerman 1995), improves recovery from ischemic renal injury (Miller et al 1994), induces mesangial cell (MC) proliferation (Abrass et al 1988;Conti et al 1988a,b) and alters glomerular matrix synthesis (Feld et al 1995).…”

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confidence: 99%

“…Therefore, they can be stimulated by endo-crine and autocrine pathways (Camussi et al 1993;Catanese et al 1993). Autocrine and paracrine IGF-I may be particularly important during tissue repair and localized growth (Bang and Hall, 1992;Sara and Hall 1990). Although ligand occupancy of the IGF-I receptor initiates activation of various signal transduction pathways (Humbel 1990), little is known about the specific signals that induce growth, differentiation, or cytoskeletal organization.…”

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confidence: 99%

Insulin-like Growth Factor I (IGF-I) Induces Unique Effects in the Cytoskeleton of Cultured Rat Glomerular Mesangial Cells

Berfield

Aspray

Abrass

1997

J Histochem Cytochem.

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SUMMARYResident glomerular mesangial cells (MCs) have complex cytoskeletal organizations that maintain functional and structural integrity. The ability of cells to replicate, coordinate movement, change shape, and interact with contiguous cells or extracellular matrix depends on cytoskeletal organization. MCs synthesize insulin-like growth factor (IGF-I), express IGF-I receptors, and respond to IGF-I with increased proliferation. We noted that IGF-I treatment of mesangial cells was associated with a change in morphology. Therefore, these studies were undertaken to define specific IGF-I-mediated changes in cytoskeletal protein organization. Rat MCs were propagated from birth in culture without supplemental insulin. Quiescent, subconfluent cultures were treated with IGF-I (100 nM) for 1 hr. Rearrangements in f-actin, ␣ -smooth muscle actin, ␤ -actin, vimentin, and vinculin were seen by fluorescence microscopy. As the cytoskeleton rearranged, ␣ -smooth muscle actin dissociated from the f-actin bundles and ␤ -actin became polymerized under the leading lamellar edge. Ultrastructural changes were consistent with increased membrane turnover and metabolic activity. The normally sessile mesangial cell was induced by IGF-I to express a woundhealing phenotype characterized by movement and increased pinocytosis. These changes are different from those induced by insulin and have important implications for mesangial cell function. ( J Histochem Cytochem 45:583-593, 1997)

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“…Tyrosine kinase receptors are one new group of targets and can be targeted by small-molecule tyrosine kinase inhibitors (TKI) or monoclonal antibodies. Insulin-like growth factor-I receptor (IGF-IR) signaling is able to potently stimulate tumor progression and cellular differentiation (3) and is a promising new molecular target in human malignancies (2,4).…”

Section: Introductionmentioning

confidence: 99%

Insulin-like growth factor-I receptor blockade by a specific tyrosine kinase inhibitor for human gastrointestinal carcinomas

Piao

Wang

Adachi

et al. 2008

Molecular Cancer Therapeutics

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Insulin-like growth factor-I receptor (IGF-IR) signaling is required for carcinogenicity and proliferation of gastrointestinal (GI) cancers. In this study, we sought to evaluate the effect of a new tyrosine kinase inhibitor of IGF-IR, NVP-AEW541, on the signal transduction and the progression of GI carcinomas. We assessed the effect of NVP-AEW541 on signal transduction, proliferation, survival, and migration in four GI cancer cells: colorectal adenocarcinoma HT29, pancreatic adenocarcinoma BxPC3, esophageal squamous cell carcinoma TE1, and hepatoma PLC/PRF/5. The effects of NVP-AEW541 alone and with chemotherapy were studied in vitro and in nude mouse xenografts. We also analyzed the effects of NVP-AEW541 on insulin signals and hybrid receptor formation between IGF-IR and insulin receptor. NVP-AEW541 blocked autophosphorylation of IGF-IR and both Akt and extracellular signal-regulated kinase activation by IGF but not by insulin. NVP-AEW541 suppressed proliferation and tumorigenicity in vitro in a dose-dependent manner in all cell lines. The drug inhibited tumor as a single agent and, when combined with stressors, up-regulated apoptosis in a dose-dependent fashion and inhibited mobility. NVP-AEW541 augmented the effects of chemotherapy on in vitro growth and induction of apoptosis. Moreover, the combination of NVP-AEW541 and chemotherapy was highly effective against tumors in mice. This compound did not influence hybrid receptor formation. Thus, NVP-AEW541 may have significant therapeutic utility in human GI carcinomas both alone and in combination with chemotherapy. [Mol Cancer Ther 2008;7(6):1483 -93]

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Insulin-like growth factors and their binding proteins

Cited by 754 publications

References 0 publications

Insulin-like growth factor II signaling through the insulin-like growth factor II/mannose-6-phosphate receptor promotes exocytosis in insulin-secreting cells

Insulin-like growth factor II signaling through the insulin-like growth factor II/mannose-6-phosphate receptor promotes exocytosis in insulin-secreting cells

Insulin-like Growth Factor I (IGF-I) Induces Unique Effects in the Cytoskeleton of Cultured Rat Glomerular Mesangial Cells

Insulin-like growth factor-I receptor blockade by a specific tyrosine kinase inhibitor for human gastrointestinal carcinomas

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