The Human Placental Lactogen and Growth Hormone Multi-Gene Family

1988 ◽  
pp. 33-57
Author(s):  
Hugo A. Barrera-Saldanña ◽  
Ramiro Ramírez-Solís ◽  
William H. Walker ◽  
Susan L. Fitzpatrick ◽  
Diana Reséndez-Pérez ◽  
...  
1981 ◽  
Vol 256 (1) ◽  
pp. 296-300
Author(s):  
J. Russell ◽  
L.M. Sherwood ◽  
K. Kowalski ◽  
A.B. Schneider

1972 ◽  
Vol 50 (10) ◽  
pp. 1014-1017
Author(s):  
Catherine L. Tanser ◽  
Nannie K. M. de Leeuw

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.


1983 ◽  
Vol 102 (3) ◽  
pp. 351-357 ◽  
Author(s):  
Eva Nagy ◽  
Istvan Berczi ◽  
Henry G. Friesen

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.


1997 ◽  
Vol 153 (1) ◽  
pp. R1-R3 ◽  
Author(s):  
Takashi Takeda ◽  
Hirohisa Kurachi ◽  
Toshiya Yamamoto ◽  
Hiroaki Homma ◽  
Kenichirou Morishige ◽  
...  

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.


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