Regulation of immunity in rats by lactogenic and growth hormones

1983 ◽  
Vol 102 (3) ◽  
pp. 351-357 ◽  
Author(s):  
Eva Nagy ◽  
Istvan Berczi ◽  
Henry G. Friesen
Keyword(s):  
Growth Hormone ◽  
Contact Dermatitis ◽  
Blood Cells ◽  
Antibody Formation ◽  
Human Growth ◽  
Growth Hormones ◽  
Placental Lactogen ◽  
Bovine Growth Hormone ◽  
Human Placental Lactogen ◽  
Rat Growth

Abstract. Antibody formation to sheep red blood cells and the development of contact dermatitis in response to dinitrochlorobenzene are impaired in hypophysectomized (Hypo-X) rats. Rat prolactin, rat growth hormone, bovine prolactin, bovine growth hormone, human placental lactogen and human growth hormone all restored the immunological competence of Hypo-X animals. The possible mechanism of action of these hormones on immune reactions is discussed.

scholarly journals Recombinant hormones from fragments of human growth hormone and human placental lactogen.

1981 ◽  
Vol 256 (1) ◽  
pp. 296-300
Author(s):  
J. Russell ◽  
L.M. Sherwood ◽  
K. Kowalski ◽  
A.B. Schneider
Keyword(s):  
Growth Hormone ◽  
Human Growth Hormone ◽  
Human Growth ◽  
Placental Lactogen ◽  
Human Placental Lactogen

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.

Participation of JAK, STAT and unknown proteins in human placental lactogen-induced signaling: a unique signaling pathway different from prolactin and growth hormone

1997 ◽  
Vol 153 (1) ◽  
pp. R1-R3 ◽  
Author(s):  
Takashi Takeda ◽  
Hirohisa Kurachi ◽  
Toshiya Yamamoto ◽  
Hiroaki Homma ◽  
Kenichirou Morishige ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Growth Hormone ◽  
Signal Transduction Pathway ◽  
Human Growth ◽  
Placental Lactogen ◽  
Human Placental Lactogen ◽  
Signal Transducer ◽  
Stat Proteins ◽  
Unique Signal ◽  
Stat Pathway

Abstract The signal transduction mechanism involved in human placental lactogen (hPL) was studied. We have identified that hPL rapidly stimulated the tyrosine phosphorylation of at least 7 proteins including Janus Kinases (JAK1 and JAK2) and a signal transducer and activator of transcription protein (Stat3). This is the first evidence that the JAK-STAT pathway is involved in the hPL signaling. Moreover, two unknown proteins which were different from STAT proteins (Stat1, 3 and 5) in sizes were predominantly tyrosine-phosphorylated. Because human growth hormone (hGH) activates Stat1, 3, 5 and human prolactin (hPRL) activates Stat5, these results show that hPL uses a unique signal transduction pathway which is different from hGH and hPRL.

RESPONSE OF CHONDROCYTES ISOLATED FROM HUMAN FOETAL CARTILAGE TO PLASMA SOMATOMEDIN ACTIVITY

1978 ◽  
Vol 76 (3) ◽  
pp. 473-477 ◽  
Author(s):  
I. K. ASHTON ◽  
M. J. O. FRANCIS
Keyword(s):  
Growth Hormone ◽  
Human Growth Hormone ◽  
Thymidine Incorporation ◽  
Human Growth ◽  
Placental Lactogen ◽  
Human Placental Lactogen ◽  
Direct Effects

Plasma somatomedin activity enhanced the incorporation of [3H]thymidine into chondrocytes isolated from human foetal cartilage during weeks 13–21 of gestation. Human growth hormone (0·1–20 μu./ml), human placental lactogen (0·1–5 μg/ml) and insulin (0·25– 10 μu./ml) had no direct effects on the synthesis of DNA in these chondrocytes, although insulin at concentrations of 2·5–100 mu./ml increased [3H]thymidine incorporation by up to 400%.

Human and rat growth hormones enhance guanylate cyclase activity

1981 ◽  
Vol 240 (2) ◽  
pp. E79-E82
Author(s):  
D. L. Vesely
Keyword(s):  
Growth Hormone ◽  
Guanylate Cyclase ◽  
Soluble Guanylate Cyclase ◽  
Human Growth ◽  
Growth Hormones ◽  
Cyclase Activity ◽  
Kidney Cortex ◽  
Guanylate Cyclase Activity ◽  
Rat Growth ◽  
Stimulation Of

The objective of this investigation was to determine whether physiological levels of growth hormone have part of their mechanism of action through stimulation of guanylate cyclase (EC 4.6.1.2.). Rat and human growth hormones enhanced the activity of soluble guanylate cyclase two- to fourfold in rat gracilis anticus skeletal muscle, liver, lung, heart, pancreas, and kidney cortex at a concentration of 10 nM. Dose-response relationships revealed that more than half-maximal stimulation of guanylate cyclase activity was seen at a concentration as low as 10 nM and nonstimulation of guanylate cyclase activity was seen when the concentration was decreased to 1 nM. Maximal enhancement was seen at 100 nM of growth hormone, and there was no further enhancement when the concentration was increased to the micromolar or millimolar range. Thus, the data in this investigation indicate that at concentrations at which growth hormone is known to cause its growth-promoting effects, growth hormone does cause an enhancement of the activity of the guanylate cyclase-cyclic GMP system.

Measurement of Human Growth Hormone in Pregnancy and Correlation with Human Placental Lactogen

1971 ◽  
Vol 32 (3) ◽  
pp. 328-332 ◽  
Author(s):  
SURENDRA K. VARMA ◽  
PETER H. SONKSEN ◽  
KAMLESH VARMA ◽  
J. STUART SOELDNER ◽  
HERBERT A. SELENKOW ◽  
...  
Keyword(s):  
Growth Hormone ◽  
Human Growth Hormone ◽  
Human Growth ◽  
Placental Lactogen ◽  
Human Placental Lactogen ◽  
In Pregnancy
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