Insulin-Like Growth Factor I Receptors Are Expressed by the Enteroendocrine Cell Line STC-1: Relationship with Proliferation and Cholecystokinin Expression

1998 ◽  
Vol 50 (3) ◽  
pp. 183-189 ◽  
Author(s):  
Fei Ye ◽  
Anne-Marie Chevrier ◽  
Dominique Langlois ◽  
Jean-Claude Cuber ◽  
Jose M. Saez ◽  
...  
Keyword(s):  
Growth Factor ◽  
Cell Line ◽  
Insulin Like Growth Factor ◽  
Enteroendocrine Cell ◽  
Factor I ◽  
Growth Factor I

Transdifferentiation of NRP-152 rat prostatic basal epithelial cells toward a luminal phenotype: regulation by glucocorticoid, insulin-like growth factor-I and transforming growth factor-beta

1999 ◽  
Vol 112 (2) ◽  
pp. 169-179 ◽  
Author(s):  
D. Danielpour
Keyword(s):  
Growth Factor ◽  
Epithelial Cells ◽  
Tight Junction ◽  
Cell Line ◽  
Transforming Growth Factor ◽  
Insulin Like Growth Factor ◽  
Tgf Beta ◽  
Factor I ◽  
Growth Factor I ◽  
Basal Epithelial Cells

The role of basal epithelial cells in prostatic function, development and carcinogenesis is unknown. The ability of basal prostatic epithelial cells to acquire a luminal phenotype was explored in vitro using the NRP-152 rat dorsal-lateral prostate epithelial cell line as a model system. NRP-152, which was spontaneously immortalized and clonally derived, is an androgen-responsive and nontumorigenic cell line that has a basal cell phenotype under normal growth conditions. However, when placed in mitogen-deficient media, these cells undergo a dramatic morphological change to a luminal phenotype. Under these growth-restrictive conditions, immunocytochemical analysis shows that NRP-152 cells acquire the luminal markers Z0-1 (a tight-junction associated protein), occludin (integral tight-junction protein), and cytokeratin 18, and lose the basal markers cytokeratins 5 and 14. Total protein and mRNA levels of cytokeratins 8, 18, c-CAM 105 (the calcium-independent cell adhesion molecule) and Z0-1, as detected by western and/or northern blot analyses, respectively, are induced, while cytokeratin 5 and 15 are lost, and occludin is unchanged. Concomitant with this differentiation, expression of transforming growth factor-beta2 (TGF-beta2), TGF-beta3, and TGF-beta receptor type II (TbetaRII) is induced, while those of TGF-beta1 and TbetaRI remain essentially unchanged. Mitogens, such as insulin-like growth factor-I and dexamethasone inhibit luminal differentiation, while exogenous TGF-beta induces such differentiation. These data together with TGF-beta neutralization experiments using pan-specific antibody implicate an important role for autocrine TGF-beta in the induction of the luminal differentiation.

Receptor synergy of interleukin-6 (IL-6) and insulin-like growth factor-I in myeloma cells that highly express IL-6 receptor α

Blood ◽  
2004 ◽  
Vol 103 (6) ◽  
pp. 2291-2298 ◽  
Author(s):  
Saeid Abroun ◽  
Hideaki Ishikawa ◽  
Naohiro Tsuyama ◽  
Shangqin Liu ◽  
Fu-Jun Li ◽  
...  
Keyword(s):  
Growth Factor ◽  
Cell Line ◽  
Interleukin 6 ◽  
Janus Kinase ◽  
Insulin Like Growth Factor ◽  
Myeloma Cells ◽  
Factor I ◽  
Igf I ◽  
Growth Factor I ◽  
Human Myeloma Cells

Abstract Interleukin-6 (IL-6) is a growth and antiapoptotic factor for human myeloma cells. The autocrine loop and increased expression of the growth factor receptors have been postulated as the mechanisms of tumorigenesis. Here we show that IL-6 stimulation induced the phosphorylation of insulin-like growth factor-I (IGF-I) receptors in a human myeloma cell line, NOP2, highly expressing IL-6 receptor α (IL-6Rα) and in the IL-6Rα–transfected U266 cell line. IL-6–dependent complex formation of IL-6Rα with IGF-I receptor β was found in NOP2 where IL-6Rα colocalized with IGF-I receptors at lipid rafts. Moreover, the IL-6–induced phosphorylation of IGF-I receptor β was not blocked by a Janus kinase 2 (Jak2) inhibitor. In addition to the activation of the signal transducer and activator of transcription 3 and extracellular signal-regulated kinase 1/2, IL-6 stimulation led to the activation of Akt, presumably following the phosphorylation of IGF-I receptors. Thus, our results suggest that in NOP2, IL-6Rα and IGF-I receptors exist on the plasma membrane in close proximity, facilitating the efficient assembly of 2 receptors in response to IL-6. The synergistic effects of highly expressed IL-6Rα on IGF-I receptor–mediated signals provide a novel insight into the Jak-independent IL-6 signaling mechanism of receptor cross-talk in human myeloma cells.

scholarly journals Characterization of Insulin-Like Growth Factor I Receptors on Human Erythroleukemia Cell Line (K-562 Cells)

1987 ◽  
Vol 34 (1) ◽  
pp. 81-88 ◽  
Author(s):  
NAOMI HIZUKA ◽  
IZUMI SUKEGAWA ◽  
KAZUE TAKANO ◽  
KUMIKO ASAKAWA ◽  
REIKO HORIKAWA ◽  
...  
Keyword(s):  
Growth Factor ◽  
Cell Line ◽  
Insulin Like Growth Factor ◽  
Factor I ◽  
Erythroleukemia Cell ◽  
Growth Factor I ◽  
K 562 Cells

scholarly journals Insulin-like growth factor I activates insulin receptor substrate 1 and Ras in human osteosarcoma cells.

1999 ◽  
Vol 46 (1) ◽  
pp. 117-123 ◽  
Author(s):  
W Lopaczynski ◽  
C Terry
Keyword(s):  
Growth Factor ◽  
Cell Line ◽  
Osteosarcoma Cell ◽  
Insulin Like Growth Factor ◽  
Factor I ◽  
Human Osteosarcoma ◽  
Nuclear Extracts ◽  
Human Osteosarcoma Cells ◽  
Igf I ◽  
Growth Factor I

Insulin-like growth factor I (IGF-I) stimulates multiplication of the human osteosarcoma cell line, MG-63, by acting through IGF-I receptor. We have characterized IGF-I stimulated phosphorylation of IRS-1, activation of Ras cycle and phosphorylation of c-Jun in this cell line. Serum starved MG-63 cells were (1) IGF-I stimulated and lysates were immunoprecipitated with polyclonal IRS-1 antibody or (2) metabolically labeled with [32P]orthophosphoric acid and then cells were treated with IGF-I. Cell lysates were immunoprecipitated with p21Ras antibody (Y13-259) and bound nucleotides were analysed by thin-layer chromatography. We demonstrated tyrosine phosphorylation of IRS-1/2 immunoprecipitated from MG-63 cells stimulated with IGF-I. We also showed an increased level of GTP in p21Ras immunoprecipitates from IGF-I treated cells. Nuclear extracts prepared from 32P-labeled cells before and after addition of IGF-I were immunoprecipitated with c-Jun antibody. After electrophoresis and autoradiography, phosphorylation of the c-Jun band was seen to be IGF-I independent. Phosphoamino acid analysis of the c-Jun band showed that phosphoserine was the major species.

Sign in / Sign up

Export Citation Format

Share Document