scholarly journals Effects of retinoic acid on growth hormone-releasing hormone receptor, growth hormone secretagogue receptor gene expression and growth hormone secretion in rat anterior pituitary cells

2016 ◽  
Vol 63 (6) ◽  
pp. 555-561 ◽  
Author(s):  
Rita Maliza ◽  
Ken Fujiwara ◽  
Takehiro Tsukada ◽  
Morio Azuma ◽  
Motoshi Kikuchi ◽  
...  
1987 ◽  
Vol 253 (5) ◽  
pp. E591-E594
Author(s):  
C. Schofl ◽  
J. Sandow ◽  
W. Knepel

The effect of human growth hormone-releasing factor (GRF) on intracellular free calcium concentration ([Ca2+]i) was examined in rat anterior pituitary cells. The [Ca2+]i was monitored directly by means of the intracellularly trapped fluorescent indicator, fura-2. GRF rapidly elevated [Ca2+]i, reaching a new plateau within approximately 30 s. The half-maximally effective concentration of GRF was approximately 130 pM. GRF produced a maximal increase in [Ca2+]i by approximately 120 nM. The GRF (2 nM)-induced elevation of [Ca2+]i was abolished by removal of extracellular calcium (Ca2+ omitted, 2 mM EGTA). The GRF (2 nM)-caused rise in [Ca2+]i was largely reduced in the presence of the calcium channel blockers Mg2+ (31.2 mM) or nifedipine (1 microM). An increase in [Ca2+]i by approximately 60 nM was elicited by the addition of prostaglandin E2 (1 microM), which can stimulate growth hormone secretion independent of GRF receptors. These data indicate that GRF elevates the [Ca2+]i, possibly in somatotrophs; this GRF-induced increase in [Ca2+]i may depend on an influx of extracellular Ca2+, largely through Mg2+- and nifedipine-sensitive calcium channels.


2002 ◽  
Vol 14 (2) ◽  
pp. 156-162 ◽  
Author(s):  
M. Yamazaki ◽  
K. Nakamura ◽  
H. Kobayashi ◽  
M. Matsubara ◽  
Y. Hayashi ◽  
...  

2009 ◽  
Vol 52 (1) ◽  
pp. 79-84 ◽  
Author(s):  
F. G. Colinet ◽  
D. Portetelle ◽  
R. Renaville

Abstract. Bovine ghrelin, a 27 amino acid peptide, has been identified in oxyntic glands of the abomasum. It is an endogenous ligand for growth hormone secretagogue receptor and stimulates food intake and growth hormone secretion. The bovine GHRL gene was completely sequenced and consists of five exons and four introns. Like mouse and human GHRL genes, we found that the bovine GHRL gene also contains a first non-coding exon of 21 bp. The bovine GHRL gene codes for 116 amino acid peptide named preproghrelin which contains the ghrelin peptide and another peptide similar to obestatin. Sequence analysis revealed eight polymorphisms, which are located in the non-coding sequence of the gene.


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