Insulin-like growth factors decrease oxygen-regulated erythropoietin production by human hepatoma cells (Hep G2)

URN to cite this document:

urn:nbn:de:bvb:355-epub-269468 Copy

DOI to cite this document:

10.5283/epub.26946 Copy

Scholz, H. ; Baier, W. ; Ratcliffe, P. ; Eckardt, K. ; Zapf, J. ; Kurtz, Armin ; Bauer, C.

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Date of publication of this fulltext: 04 Dec 2012 13:52

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Details

Item type:	Article
Journal or Publication Title:	The American journal of physiology. Cell pyhsiology
Publisher:	American Physiological Society (APS)
Volume:	263
Number of Issue or Book Chapter:	2 Pt 1
Page Range:	C474-C479
Date:	1992
Institutions:	Biology, Preclinical Medicine > Institut für Physiologie > Prof. Dr. Armin Kurtz
Identification Number:	Value Type 1325119 PubMed ID
Classification:	Notation Type Animals MESH Culture Media MESH Dose-Response Relationship, Drug MESH Erythropoietin/biosynthesis MESH Humans MESH Insulin/pharmacology MESH Insulin-Like Growth Factor I/pharmacology MESH Insulin-Like Growth Factor II/pharmacology MESH Liver Neoplasms/pathology MESH Liver Neoplasms, Experimental/pathology MESH Oxygen/pharmacology MESH Receptor, Insulin/metabolism MESH Receptors, Cell Surface/metabolism MESH Receptors, Somatomedin MESH Somatomedins/pharmacology MESH Tumor Cells, Cultured MESH
Dewey Decimal Classification:	500 Science > 570 Life sciences 600 Technology > 610 Medical sciences Medicine
Status:	Published
Refereed:	Yes, this version has been refereed
Created at the University of Regensburg:	Unknown
Item ID:	26946

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Abstract

We examined the effects of insulin-like growth factors (IGFs) and insulin on erythropoietin (EPO) production by human hepatoma cells (Hep G2). Compared with normoxia (20% O2), EPO production by Hep G2 cells during a 72-h incubation was stimulated fivefold by exposure to low oxygen tension (1% O2) and nearly threefold by exposure to cobalt chloride (100 microM). IGF-I caused a ...

Abstract

We examined the effects of insulin-like growth factors (IGFs) and insulin on erythropoietin (EPO) production by human hepatoma cells (Hep G2). Compared with normoxia (20% O2), EPO production by Hep G2 cells during a 72-h incubation was stimulated fivefold by exposure to low oxygen tension (1% O2) and nearly threefold by exposure to cobalt chloride (100 microM). IGF-I caused a concentration-dependent attenuation of EPO formation under normoxic conditions and inhibited (maximally 50%) EPO production stimulated by either low oxygen tension or cobalt [half-maximal effect (ED50) approximately 5 nM]. The increase of EPO mRNA levels in response to hypoxia was significantly reduced by IGF-I. Similarly to IGF-I, IGF-II (ED50 approximately 8 nM) and insulin (ED50 approximately 80 nM) also inhibited EPO formation in Hep G2 cells. IGF-I (100 pM-100 nM) stimulated the incorporation of radiolabeled alanine as a measure for total protein synthesis, 3H-labeled thymidine incorporation into DNA, and glycogen synthesis at 20 and 1% O2 in a concentration-dependent fashion. IGF-I exhibited a high affinity for the IGF-I receptor (apparent Kd approximately 3 nM). Unlabeled insulin was greater than 100-fold less potent than IGF-I in competing for 125I-IGF-I binding (apparent Kd approximately 360 nM). Conversely, insulin bound to the insulin receptor with high affinity (apparent Kd approximately 0.3 nM), whereas IGF-I was less than 1% as potent in competing for 125I-insulin binding. In summary, IGFs and insulin exert a negative control function on oxygen-regulated EPO production in Hep G2 cells. The inhibitory effect of IGFs and insulin on EPO formation appears to be mediated via the IGF-I receptor.

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