Cellular origin and distribution of transforming growth factor-?1 in the normal rat myocardium

1989 ◽  
Vol 256 (3) ◽  
Author(s):  
M. Eghbali
Keyword(s):  
Growth Factor ◽  
Transforming Growth Factor ◽  
Rat Myocardium ◽  
Cellular Origin ◽  
Normal Rat

scholarly journals Effects of hypertonic stress on transforming growth factor-β activity in normal rat kidney cells

1998 ◽  
Vol 53 (6) ◽  
pp. 1654-1660 ◽  
Author(s):  
Toshihiro Sugiura ◽  
Atsushi Yamauchi ◽  
Hiroshi Kitamura ◽  
Yasuko Matusoka ◽  
Masaru Horio ◽  
...  
Keyword(s):  
Growth Factor ◽  
Transforming Growth Factor ◽  
Rat Kidney ◽  
Transforming Growth Factor Β ◽  
Kidney Cells ◽  
Hypertonic Stress ◽  
Normal Rat

scholarly journals Neuroblastoma cells express c-sis and produce a transforming growth factor antigenically related to the platelet-derived growth factor.

1985 ◽  
Vol 5 (9) ◽  
pp. 2289-2297 ◽  
Author(s):  
E J van Zoelen ◽  
W J van de Ven ◽  
H J Franssen ◽  
T M van Oostwaard ◽  
P T van der Saag ◽  
...  
Keyword(s):  
Growth Factors ◽  
Growth Factor ◽  
Transforming Growth Factor ◽  
Rat Kidney ◽  
Molecular Size ◽  
Platelet Derived Growth Factor ◽  
Kidney Cells ◽  
Transforming Growth Factors ◽  
Normal Rat ◽  
Epidermal Growth

Mouse neuroblastoma Neuro-2A cells produce transforming growth factors during exponential growth in a defined hormone-free medium, which, on Bio-Gel columns in 1 M HAc, elute at a molecular size of 15 to 20 kilodaltons (kDa). These neuroblastoma-derived transforming growth factors have strong mitogenic activity, but they do not compete with epidermal growth factor for receptor binding (E. J. J. van Zoelen, D. R. Twardzik, T. M. J. van Oostwaard, P. T. van der Saag, S. W. de Laat, and G. J. Todaro, Proc. Natl. Acad. Sci. U.S.A. 81:4085-4089, 1984). In this study approximately 80% of the mitogenic activity was immunoprecipitated by antibodies raised against platelet-derived growth factor (PDGF). Immunoblotting indicated a true molecular size of 32 kDa for this PDGF-like growth factor. Analysis of poly(A)+ RNA from Neuro-2A cells demonstrated the expression of the c-sis oncogene in this cell line, whereas in vitro translation of the RNA yielded a 20-kDa protein recognized by anti-PDGF antibodies. Separation by reverse-phase high-pressure liquid chromatography demonstrated the presence of two distinct mitogenic activities in neuroblastoma-derived transforming growth factor preparations, one of which is antigenically related to PDGF. Both activities had the ability to induce anchorage-independent growth in normal rat kidney cells, both in the presence and in the absence of epidermal growth factor. It is concluded that Neuro-2A cells express c-sis with concomitant production and secretion of a PDGF-like growth factor, which plays a role in the induction of phenotypic transformation on normal rat kidney cells.

scholarly journals An agent or agents produced by virus-transformed cells cause unregulated ruffling in untransformed cells.

1986 ◽  
Vol 102 (4) ◽  
pp. 1224-1229 ◽  
Author(s):  
S E Myrdal ◽  
N Auersperg
Keyword(s):  
Growth Factor ◽  
Transforming Growth Factor ◽  
Rat Kidney ◽  
Rabbit Igg ◽  
Murine Sarcoma Virus ◽  
Normal Rat ◽  
Sarcoma Virus ◽  
Epidermal Growth ◽  
Factor Type ◽  
Kinetics Of

KNRK cells (a normal rat kidney [NRK] cell line transformed by Kirsten murine sarcoma virus) in sparse culture exhibit a highly ruffled morphology, but the cause of this ruffling is unknown. In this study, we have demonstrated that the continuous, excess ruffling on KNRK cells is caused by one or more soluble agents secreted by the KNRK cells themselves. To do this study, an assay for ruffling responses in live cell cultures was defined, and its reproducibility was demonstrated. This assay permitted observation of the kinetics of ruffling responses (percentage of cells ruffled as a function of time after stimulation). This method was used to compare the kinetics of ruffling induced by insulin, epidermal growth factor, fibroblast growth factor, glucose, and KNRK cell conditioned medium (CM). Ruffling was elicited on NRK cells by each of the polypeptide mitogens and nutrients, but, in each case, this ruffling subsided spontaneously within an hour. CM from KNRK cells also caused ruffling movements on untransformed NRK cells, but this ruffling continued for at least 20 h. This response was largely blocked by premixing the KNRK cell CM with rabbit IgG against rat transforming growth factor, type alpha, (TGF-alpha). KNRK cells made quiescent (ruffle free) by a pH shift (from 7.4 to 8.4) responded to insulin, glucose, and KNRK cell CM with kinetics similar to those observed for each of these factors in NRK cells. The unusual feature for the ruffle-inducing agent(s) produced by KNRK cells was that this activity was not subject, in either NRK or KNRK cells, to the cellular off-regulation that limits the responses to insulin or glucose. Thus, the continuous ruffling of KNRK cells is caused by their own unregulated ruffle-inducing agent or agents, which appear to include TGF-alpha. This work also demonstrates that kinetic analysis of cellular responses to exogenous factors can provide new insights into the regulatory mechanisms involved in the normal limitation of these responses.

Synergistic effects of endothelin-1 (ET-1) and transforming growth factor alpha (TGF-α) or epidermal growth factor (EGF) on DNA replication and G1 to S phase transition

1991 ◽  
Vol 11 (3) ◽  
pp. 171-180 ◽  
Author(s):  
Yun-Chi Yeh ◽  
E. Robert Burns ◽  
John Yeh ◽  
Hsing-Wu Yeh
Keyword(s):  
Growth Factor ◽  
Transforming Growth Factor ◽  
Synergistic Effects ◽  
Rat Kidney ◽  
Transforming Growth Factor Β ◽  
S Phase ◽  
Detectable Effect ◽  
Thymidine Incorporation Assay ◽  
Normal Rat ◽  
Incorporation Assay

The cooperative cell kinetic actions of ET-1 with TGF-α or EGF in normal rat kidney fibroblasts (NRK-49F) and KNRK cells (Kirsten MSV transformed) were analyzed by [3H]-thymidine incorporation assay and flow cytometry. A marked synergistic effect of TGF-α and ET-1 (or EGF and ET-1) on DNA synthesis and G1 to S transition was observed in NRK cells; 15–20% S for TGF-α and 12% S for ET-1 alone but 45–50% S in combination. There was no detectable effect on cell cycle kinetics by TGF-α (1 ng/ml) or EGF (1 ng/ml) plus ET-1 (1 ng/ml) in KNRK cells treated for 22 hours. Insulin, insulin-like growth factor I (IGF-I), fibroblast growth factor (FGF), platelet derived growth factor (PDGF), and transforming growth factor β (TGF-β) were also tested and found to have no significant synergistic effects on ET-1 actions. Our findings suggest that the combination of TGF-α (EGF) and ET-1 is an important part of an intricate network which coordinates progression of G1 to S phase in normal cells.

Production of transforming growth factor-alpha by normal rat small intestine

1991 ◽  
Vol 261 (6) ◽  
pp. C994-C1000 ◽  
Author(s):  
J. A. Barnard ◽  
W. H. Polk ◽  
H. L. Moses ◽  
R. J. Coffey
Keyword(s):  
Growth Factor ◽  
Egf Receptor ◽  
Transforming Growth Factor ◽  
Transforming Growth Factor Alpha ◽  
Single Class ◽  
Receptor Mrna ◽  
Normal Rat ◽  
Epidermal Growth ◽  
Factor Alpha ◽  
Stimulation Of

Transforming growth factor-alpha (TGF-alpha) and epidermal growth factor (EGF) are similar in structure and biological activity. In the present study, the distributions of TGF-alpha mRNA, TGF-alpha immunoreactivity, and TGF-alpha-EGF receptor mRNA were examined in epithelial and nonepithelial compartments of the jejunum, and the effect of TGF-alpha on growth of a jejunal crypt cell line (IEC-6) was determined. Epithelial cells eluted from the rat jejunal cryptvillus axis expressed TGF-alpha mRNA at twofold higher levels in the villus tip than in the crypt and EGF receptor mRNA at sevenfold higher levels in the villus tip. Expression of these two mRNA transcripts in the subepithelium was low. Immunohistochemical staining showed TGF-alpha immunoreactivity predominantly in the epithelium and muscularis. Immunostaining of villus cells was uniform, whereas crypt cells did not stain. IEC-6 cells bound 125I-EGF to a single class of high-affinity (dissociation constant = 833 pM) receptors. EGF and TGF-alpha (10 ng/ml) only modestly stimulated IEC-6 cell growth in the presence of 5% serum but increased expression of the protooncogenes c-jun and c-myc threefold over control cells. These findings suggest that, among the potential physiological roles for TGF-alpha produced by the jejunal epithelium, promotion of cell migration and modulation of fluid and electrolyte transport may be as relatively important as stimulation of cell proliferation.

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