scholarly journals Hormonal effects on cell proliferation in a human erythroleukemia cell line (K562)

Blood ◽  
1980 ◽  
Vol 56 (5) ◽  
pp. 886-891 ◽  
Author(s):  
C Gauwerky ◽  
DW Golde
Keyword(s):  
Growth Hormone ◽  
Cell Proliferation ◽  
Colony Formation ◽  
Human Growth ◽  
K562 Cells ◽  
Colony Growth ◽  
Inhibitory Effect ◽  
Erythroid Progenitors ◽  
Adrenergic Antagonist

Abstract We have investigated the hormonal responsiveness of K562 cells using a serum-substituted in vitro clonogenic assay. Dexamethasone inhibited colony formation by the K562 cells, and the inhibitory effect could be reversed by progesterone (10(-6) M). Fluoxymesterone caused a prominent enhancement of K562 colony growth, whereas estriol had no effect. Stimulation by triiodothyronine was maximal at 10(-7) M, and the thyroid effect could be abrogated by the beta 2-adrenergic antagonist butoxamine in equimolar concentrations. Using standard tissue culture conditions, the beta-adrenergic agent isoproterenol, but not the alpha catecholamine phenylephrine, enhanced the proliferation of K562 cells. When K562 cells were grown under hormone-depleted conditions, they developed responsiveness to phenylephrine and were no longer stimulated by isoproterenol. DbcAMP and prostaglandins of the E series also caused K562 colony enhancement. Prostaglandin F2 alpha had no effect on cell proliferation. Insulin was an effective stimulant of colony formation of K562 cells, as were human growth hormone and ovine prolacin. Bovine growth hormone had no effect. Our results are consistent with the identificaiton of K562 as an erythroid line, and they indicate that K562 cells respond to endocrine hormones in a manner analogous to normal erythroid progenitors.

scholarly journals Hormonal effects on cell proliferation in a human erythroleukemia cell line (K562)

Blood ◽  
1980 ◽  
Vol 56 (5) ◽  
pp. 886-891
Author(s):  
C Gauwerky ◽  
DW Golde
Keyword(s):  
Growth Hormone ◽  
Cell Proliferation ◽  
Colony Formation ◽  
Human Growth ◽  
K562 Cells ◽  
Colony Growth ◽  
Inhibitory Effect ◽  
Erythroid Progenitors ◽  
Adrenergic Antagonist

We have investigated the hormonal responsiveness of K562 cells using a serum-substituted in vitro clonogenic assay. Dexamethasone inhibited colony formation by the K562 cells, and the inhibitory effect could be reversed by progesterone (10(-6) M). Fluoxymesterone caused a prominent enhancement of K562 colony growth, whereas estriol had no effect. Stimulation by triiodothyronine was maximal at 10(-7) M, and the thyroid effect could be abrogated by the beta 2-adrenergic antagonist butoxamine in equimolar concentrations. Using standard tissue culture conditions, the beta-adrenergic agent isoproterenol, but not the alpha catecholamine phenylephrine, enhanced the proliferation of K562 cells. When K562 cells were grown under hormone-depleted conditions, they developed responsiveness to phenylephrine and were no longer stimulated by isoproterenol. DbcAMP and prostaglandins of the E series also caused K562 colony enhancement. Prostaglandin F2 alpha had no effect on cell proliferation. Insulin was an effective stimulant of colony formation of K562 cells, as were human growth hormone and ovine prolacin. Bovine growth hormone had no effect. Our results are consistent with the identificaiton of K562 as an erythroid line, and they indicate that K562 cells respond to endocrine hormones in a manner analogous to normal erythroid progenitors.

Failure of Human Growth Hormone and Human Placental Lactogen to Affect Glucose Consumption by Human Erythrocytes and Leucocytes In Vitro

1972 ◽  
Vol 50 (10) ◽  
pp. 1014-1017
Author(s):  
Catherine L. Tanser ◽  
Nannie K. M. de Leeuw
Keyword(s):  
Growth Hormone ◽  
Glucose Oxidase ◽  
Human Growth Hormone ◽  
Glucose Utilization ◽  
Human Growth ◽  
Glucose Consumption ◽  
Inhibitory Effect ◽  
Placental Lactogen ◽  
Human Placental Lactogen

The effect of human growth hormone (HGH) and human placental lactogen (HPL) on glucose consumption by erythrocytes and leucocytes in vitro was investigated. Glucose consumption was measured by determining glucose utilization during 3 h incubation at 37 °C, using the glucose oxidase method.HGH and HPL showed no effect on glucose consumption by erythrocytes, and HPL showed no effect on glucose consumption by leucocytes in vitro. Our results do not confirm previous reports of an inhibitory effect of HGH on glucose consumption by erythrocytes in vitro.

scholarly journals Stimulation of monocyte chemotaxis by human growth hormone and its deactivation by somatostatin

Blood ◽  
1993 ◽  
Vol 82 (3) ◽  
pp. 954-960 ◽  
Author(s):  
CJ Wiedermann ◽  
N Reinisch ◽  
H Braunsteiner
Keyword(s):  
Growth Hormone ◽  
Human Growth Hormone ◽  
Recombinant Human Growth Hormone ◽  
Human Growth ◽  
Inhibitory Effect ◽  
Boyden Chamber ◽  
Recombinant Growth Hormone ◽  
Monocyte Chemotaxis ◽  
Long Acting

Monocyte infiltration occurs early in the course of inflammation and is a prerequisite for optimal repair of tissue damage. In this study, human recombinant growth hormone was shown to be a potent chemoattractant for human monocytes, inducing migration at picomolar concentrations of recombinant human growth hormone. Chemotaxis of monocytes was measured in vitro by a modified Boyden chamber assay using nitrocellulose micropore filters and measuring microscopically the migration depth of the leading front of monocytes. Somatostatin, which inhibits the release of growth hormone, and its long-acting analogue, octreotide, also stimulated chemotaxis of monocytes; however, the effective peptide concentration was in the micromolar range. When tested for chemotaxis in combination or in experiments using pretreatment with somatostatin and washing of treated cells, somatostatin significantly antagonized the chemotactic responses of monocytes to growth hormone. The inhibitory effect on growth hormone- stimulated chemotaxis was dose dependent and occurred at concentrations severalfold lower than the chemotactically active concentration of somatostatin. Combinations of growth hormone with interferon or substance P also deactivated the chemotactic responses. These observations suggest that human growth hormone may have a regulatory role in monocyte chemotaxis.

scholarly journals K562 cells produce and respond to human erythroid-potentiating activity

Blood ◽  
1988 ◽  
Vol 71 (6) ◽  
pp. 1720-1725 ◽  
Author(s):  
BR Avalos ◽  
SE Kaufman ◽  
M Tomonaga ◽  
RE Williams ◽  
DW Golde ◽  
...  
Keyword(s):  
Colony Formation ◽  
Calf Serum ◽  
K562 Cells ◽  
Biologically Active ◽  
Northern Hybridization ◽  
Erythroid Progenitors ◽  
Surface Receptors ◽  
Erythroleukemia Cell ◽  
Semi Solid

Human erythroid-potentiating activity (EPA) is a 28,000 mol wt glycoprotein that stimulates the growth of erythroid progenitors in vitro and enhances colony formation by the K562 human erythroleukemia cell line. EPA has potent protease inhibitory activity, and is also referred to as tissue inhibitor of metalloproteinases (TIMP). We observed that colony formation by K562 cells in semi-solid medium containing reduced fetal calf serum (FCS) is not directly proportional to the number of cells plated, suggesting production of autostimulatory factors by K562 cells. Using radioimmunoprecipitation and a bioassay for EPA, medium conditioned by K562 cells was found to contain high levels of biologically active EPA; Northern hybridization analysis confirmed the expression of EPA mRNA. Radiolabeled EPA was used to identify cell surface receptors on K562 cells. Together, these results suggest that EPA may act as an autocrine growth factor for K562 cells.

Effects of Hepcidin, Ferritin, and Iron Deprivation on Erythroid Colony Formation in Vitro.

Blood ◽  
2004 ◽  
Vol 104 (11) ◽  
pp. 3704-3704
Author(s):  
Robert T. Means ◽  
Gail A. Dallalio ◽  
Thomas W. Fleury
Keyword(s):  
Colony Formation ◽  
Interleukin 1 ◽  
Colony Growth ◽  
Limiting Factor ◽  
Red Cell ◽  
Erythroid Progenitors ◽  
Anemia Of Chronic Disease ◽  
Iron Deprivation ◽  
Erythropoietic Response

Abstract The anemia of chronic disease (ACD) results from a combination of three pathologic processes. In ACD, a modest shortening of red cell survival creates an increased demand for red cell production, which is not met because of an impaired erythropoietic response and defects in reticuloendothelial iron mobilization and utilization. The impaired erythropoietic response, in turn, has two components: a blunted erythropoietin response, and an impaired response of erythroid progenitors to erythropoietin. Recombinant human erythropoietin (rhEPO) can reverse this impaired progenitor response in vitro, and can also correct ACD in patients. These processes have generally been considered effects of the cytokines which mediate the immune and inflammatory response, such as tumor necrosis factor, interleukin-1, and the interferons. It has recently been proposed that hepcidin, a mediator of innate immunity with the iron regulatory properties, is the factor responsible for ACD. If this is the case, then hepcidin should be able to induce the pathophysiologic mechanisms implicated in ACD. We therefore evaluated the effects of hepcidin and associated phenomena on human CFU-E colony formation in vitro. All CFU-E cultures were performed in plasma clots in serum-containing medium with rhEPO 1 U/mL. Hepcidin at concentrations 10 ng/mL -10 μg/mL had no effect on CFU-E colony formation. A number of studies have demonstrated that increased hepcidin message expression and protein production are strongly associated with increases in serum ferritin concentrations, and so the effect of added ferritin on erythroid colony formation was studied. Neither ferritin nor apo-ferritin 10 – 1000 ng/mL had inhibitory effects on CFU-E colony formation. The effect of iron deprivation on erythroid colony formation was evaluated with using desferrioxamine. Desferrioxamine 0.01mM decreased CFU-E colony formation to 60% of control values, while higher concentrations completely ablated colony growth. In summary, hepcidin does not appear to inhibit CFU-E colony formation directly or indirectly through ferritin. It may exert such an effect by decreasing availability of iron for erythropoiesis; however, such a finding would be difficult to reconcile with the observed clinical response of ACD to rhEPO, given that iron availability is typically a limiting factor in the erythropoietic response to rhEPO. The role of hepcidin in the overall pathogenesis of ACD remains to be fully determined.

scholarly journals RNA m6A reader YTHDF2 facilitates lung adenocarcinoma cell proliferation and metastasis by targeting the AXIN1/Wnt/β-catenin signaling

2021 ◽  
Vol 12 (5) ◽  
Author(s):  
Yin Li ◽  
Hao Sheng ◽  
Feng Ma ◽  
Qiang Wu ◽  
Jianfang Huang ◽  
...  
Keyword(s):  
Cell Proliferation ◽  
Lung Adenocarcinoma ◽  
Colony Formation ◽  
Critical Role ◽  
Xenograft Model ◽  
Inhibitory Effect ◽  
Negative Regulator ◽  
Tumor Xenograft ◽  
And Migration

AbstractLung adenocarcinoma (LUAD) remains a leading cause of cancer-related deaths worldwide. YTHDF2 is a reader of N6-methyladenosine (m6A) on RNA and plays a critical role in the initiation and propagation of myeloid leukemia; however, whether YTHDF2 controls the development of LUAD remains to be explored. Here, we found that YTHDF2 was significantly upregulated in LUAD compared with paracancerous normal tissues, and YTHDF2 knockdown drastically inhibited, while its overexpression promoted, cell growth, colony formation and migration of LUAD cells in vitro. In addition, YTHDF2 knockdown significantly inhibited tumorigenesis in a murine tumor xenograft model. Through the integrative analysis of RNA-seq, m6A-seq, CLIP-seq, and RIP-seq datasets, we identified a set of potential direct targets of YTHDF2 in LUAD, among which we confirmed AXIN1, which encodes a negative regulator of the Wnt/β-catenin signaling, as a direct target of YTHDF2. YTHDF2 promoted AXIN1 mRNA decay and subsequently activated the Wnt/β-catenin signaling. Knockout of AXIN1 sufficiently rescued the inhibitory effect of YTHDF2 depletion on lung cancer cell proliferation, colony-formation, and migration. These results revealed YTHDF2 to be a contributor of LUAD development acting through the upregulation of the AXIN1/Wnt/β-catenin signaling, which can be a potential therapeutic target for LUAD.

scholarly journals Stimulation of monocyte chemotaxis by human growth hormone and its deactivation by somatostatin

Blood ◽  
1993 ◽  
Vol 82 (3) ◽  
pp. 954-960 ◽  
Author(s):  
CJ Wiedermann ◽  
N Reinisch ◽  
H Braunsteiner
Keyword(s):  
Growth Hormone ◽  
Human Growth Hormone ◽  
Recombinant Human Growth Hormone ◽  
Human Growth ◽  
Inhibitory Effect ◽  
Boyden Chamber ◽  
Recombinant Growth Hormone ◽  
Monocyte Chemotaxis ◽  
Long Acting

Abstract Monocyte infiltration occurs early in the course of inflammation and is a prerequisite for optimal repair of tissue damage. In this study, human recombinant growth hormone was shown to be a potent chemoattractant for human monocytes, inducing migration at picomolar concentrations of recombinant human growth hormone. Chemotaxis of monocytes was measured in vitro by a modified Boyden chamber assay using nitrocellulose micropore filters and measuring microscopically the migration depth of the leading front of monocytes. Somatostatin, which inhibits the release of growth hormone, and its long-acting analogue, octreotide, also stimulated chemotaxis of monocytes; however, the effective peptide concentration was in the micromolar range. When tested for chemotaxis in combination or in experiments using pretreatment with somatostatin and washing of treated cells, somatostatin significantly antagonized the chemotactic responses of monocytes to growth hormone. The inhibitory effect on growth hormone- stimulated chemotaxis was dose dependent and occurred at concentrations severalfold lower than the chemotactically active concentration of somatostatin. Combinations of growth hormone with interferon or substance P also deactivated the chemotactic responses. These observations suggest that human growth hormone may have a regulatory role in monocyte chemotaxis.

scholarly journals K562 cells produce and respond to human erythroid-potentiating activity

Blood ◽  
1988 ◽  
Vol 71 (6) ◽  
pp. 1720-1725 ◽  
Author(s):  
BR Avalos ◽  
SE Kaufman ◽  
M Tomonaga ◽  
RE Williams ◽  
DW Golde ◽  
...  
Keyword(s):  
Colony Formation ◽  
Calf Serum ◽  
K562 Cells ◽  
Biologically Active ◽  
Northern Hybridization ◽  
Erythroid Progenitors ◽  
Surface Receptors ◽  
Erythroleukemia Cell ◽  
Semi Solid

Abstract Human erythroid-potentiating activity (EPA) is a 28,000 mol wt glycoprotein that stimulates the growth of erythroid progenitors in vitro and enhances colony formation by the K562 human erythroleukemia cell line. EPA has potent protease inhibitory activity, and is also referred to as tissue inhibitor of metalloproteinases (TIMP). We observed that colony formation by K562 cells in semi-solid medium containing reduced fetal calf serum (FCS) is not directly proportional to the number of cells plated, suggesting production of autostimulatory factors by K562 cells. Using radioimmunoprecipitation and a bioassay for EPA, medium conditioned by K562 cells was found to contain high levels of biologically active EPA; Northern hybridization analysis confirmed the expression of EPA mRNA. Radiolabeled EPA was used to identify cell surface receptors on K562 cells. Together, these results suggest that EPA may act as an autocrine growth factor for K562 cells.

SENSITIVITY OF THE RAT DIAPHRAGM TO GROWTH HORMONE.

1967 ◽  
Vol 54 (4) ◽  
pp. 645-662 ◽  
Author(s):  
Å. Hjalmarson ◽  
K. Ahrén
Keyword(s):  
Growth Hormone ◽  
Inhibitory Effect ◽  
Rat Diaphragm ◽  
Intracellular Accumulation ◽  
Slight Effect ◽  
Kidney Capsule ◽  
Muscle Tissues ◽  
Hypophysectomized Rats ◽  
Isolated Rat

ABSTRACT The effect of growth hormone (GH) in vitro on the rate of intracellular accumulation of the non-utilizable amino acid α-aminoisobutyric acid (AIB) was studied in the intact rat diaphragm preparation. Bovine or ovine GH (25 μg/ml incubation medium) markedly stimulated the accumulation of AIB-14C by diaphragms from hypophysectomized rats, while there was no or only a very slight effect on diaphragms from normal rats. In diaphragms from rats with the pituitary gland autotransplanted to the kidney capsule GH in vitro stimulated the accumulation of AIB-14C significantly more than in diaphragms from normal rats but significantly less than in diaphragms from hypophysectomized rats. Injections of GH intramuscularly for 4 days to hypophysectomized rats made the diaphragms from these rats less sensitive or completely insensitive to GH in vitro. These results indicate strongly that the relative insensitivity to GH in vitro of diaphragms from normal rats is due to the fact that the muscle tissues from these rats has been exposed to the endogenously secreted GH. The results show that GH can influence the accumulation of AIB-14C in the isolated rat diaphragm in two different ways giving an acute or »stimulatory« effect and a late or »inhibitory« effect, and that it seems to be a time-relationship between these two effects of the hormone.

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