Growth hormone secretion:: Molecular and cellular mechanisms and in vivo approaches

被引:54
作者
Anderson, LL
Jeftinija, S
Scanes, CG
机构
[1] Iowa State Univ, Dept Anim Sci, Ames, IA 50011 USA
[2] Iowa State Univ, Dept Biomed Sci, Ames, IA 50011 USA
关键词
growth hormone; growth hormones secretagogues; cellular mechanisms; signal transduction systems;
D O I
10.1177/153537020422900403
中图分类号
R-3 [医学研究方法]; R3 [基础医学];
学科分类号
1001 ;
摘要
Growth hormone (GH) release is under the direct control of hypothalamic releasing hormones, some being also produced peripherally. The role of these hypothalamic factors has been understood by in vitro studies together with such in vivo approaches as stalk sectioning. Secretion of GH is stimulated by GH-releasing hormone (GHRH) and ghrelin (acting via the GH secretagogue [GHS] receptor [GHSR]), and inhibited by somatostatin (SRIF). Other peptides/proteins influence GH secretion, at least in some species. The cellular mechanism by which the releasing hormones affect GH secretion from the somatotrope requires specific signal transduction systems (cAMP and/or calcium influx and/or mobilization of intracellular calcium) and/or tyrosine kinase(s) and/or nitric oxide (NO)/cGMP. At the subcellular level, GH release (at least in response to GHS) is accomplished by the following. The GH-containing secretory granules are moved close to the cell surface. There is then transient fusion of the secretory granules with the fusion pores in the multiple secretory pits in the somatotrope cell surface.
引用
收藏
页码:291 / 302
页数:12
相关论文
共 116 条
  • [51] Localization of leptin receptor-like immunoreactivity in the corticotropes, somatotropes, and gonadotropes in the ovine anterior pituitary
    Iqbal, J
    Pompolo, S
    Considine, RV
    Clarke, IJ
    [J]. ENDOCRINOLOGY, 2000, 141 (04) : 1515 - 1520
  • [52] G(i) regulation of secretory vesicle swelling examined by atomic force microscopy
    Jena, BP
    Schneider, SW
    Geibel, JP
    Webster, P
    Oberleithner, H
    Sritharan, KC
    [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1997, 94 (24) : 13317 - 13322
  • [53] Structure and composition of the fusion pore
    Jena, BP
    Cho, SJ
    Jeremic, A
    Stromer, MH
    Abu-Hamdah, R
    [J]. BIOPHYSICAL JOURNAL, 2003, 84 (02) : 1337 - 1343
  • [54] Reconstituted fusion pore
    Jeremic, A
    Kelly, M
    Cho, SJ
    Stromer, MH
    Jena, BP
    [J]. BIOPHYSICAL JOURNAL, 2003, 85 (03) : 2035 - 2043
  • [55] JOHKE T, 1978, ENDOCRINOL JAPON, V25, P19
  • [56] Kennedy SR, 2002, J ANIM SCI, V80, P744
  • [57] KLINDT J, 1983, P SOC EXP BIOL MED, V172, P508, DOI 10.3181/00379727-172-41596
  • [58] A novel amphibian hypothalamic neuropeptide: Isolation, localization, and biological activity
    Koda, A
    Ukena, K
    Teranishi, H
    Ohta, S
    Yamamoto, K
    Kikuyama, S
    Tsutsui, K
    [J]. ENDOCRINOLOGY, 2002, 143 (02) : 411 - 419
  • [59] Ghrelin is a growth-hormone-releasing acylated peptide from stomach
    Kojima, M
    Hosoda, H
    Date, Y
    Nakazato, M
    Matsuo, H
    Kangawa, K
    [J]. NATURE, 1999, 402 (6762) : 656 - 660
  • [60] Spontaneous and receptor-controlled soluble guanylyl cyclase activity in anterior pituitary cells
    Kostic, TS
    Andric, SA
    Stojilkovic, SS
    [J]. MOLECULAR ENDOCRINOLOGY, 2001, 15 (06) : 1010 - 1022