scholarly journals Cloning of the Genes for the Pituitary Glycoprotein Hormone α and Follicle-Stimulating Hormone β Subunits in the Japanese Crested Ibis, Nipponia nippon

2003 ◽  
Vol 20 (4) ◽  
pp. 449-459 ◽  
Author(s):  
Daisuke Kawasaki ◽  
Tadashi Aotsuka ◽  
Toru Higashinakagawa ◽  
Susumu Ishii
Keyword(s):  
Follicle Stimulating Hormone ◽  
Glycoprotein Hormone ◽  
Nipponia Nippon ◽  
Crested Ibis ◽  
Stimulating Hormone

scholarly journals Advances in the Regulation of Mammalian Follicle-Stimulating Hormone Secretion

Animals ◽  
2021 ◽  
Vol 11 (4) ◽  
pp. 1134
Author(s):  
Hao-Qi Wang ◽  
Wei-Di Zhang ◽  
Bao Yuan ◽  
Jia-Bao Zhang
Keyword(s):  
Molecular Mechanisms ◽  
Current Knowledge ◽  
Follicle Stimulating Hormone ◽  
Hormone Secretion ◽  
Β Subunit ◽  
Glycoprotein Hormone ◽  
Livestock Breeding ◽  
Biological Specificity ◽  
Therapeutic Development ◽  
Stimulating Hormone

Mammalian reproduction is mainly driven and regulated by the hypothalamic-pituitary-gonadal (HPG) axis. Follicle-stimulating hormone (FSH), which is synthesized and secreted by the anterior pituitary gland, is a key regulator that ultimately affects animal fertility. As a dimeric glycoprotein hormone, the biological specificity of FSH is mainly determined by the β subunit. As research techniques are being continuously innovated, studies are exploring the underlying molecular mechanism regulating the secretion of mammalian FSH. This article will review the current knowledge on the molecular mechanisms and signaling pathways systematically regulating FSH synthesis and will present the latest hypothesis about the nuclear cross-talk among the various endocrine-induced pathways for transcriptional regulation of the FSH β subunit. This article will provide novel ideas and potential targets for the improved use of FSH in livestock breeding and therapeutic development.

FSH in therapy: physiological basis, new preparations and clinical use

1995 ◽  
Vol 4 (3) ◽  
pp. 163-177 ◽  
Author(s):  
Manuela Simoni ◽  
Eberhard Nieschlag
Keyword(s):  
Follicle Stimulating Hormone ◽  
Thyroid Stimulating Hormone ◽  
Clinical Use ◽  
Β Subunit ◽  
Glycoprotein Hormone ◽  
Physiological Basis ◽  
Α Subunit ◽  
And Function ◽  
Polypeptide Chains ◽  
Stimulating Hormone

Follicle stimulating hormone (FSH) is a glycoprotein hormone secreted by the pituitary gland that, together with luteinizing hormone (LH), controls development, maturation and function of the gonad. Like the related hormones, LH, thyroid stimulating hormone (TSH) and human chorionic gonadotropin (hCG), FSH consists of two polypeptide chains, α and β, bearing carbohydrate moietiesN-linked to asparagine (Asn) residues. The α subunit is common to all members of the glycoprotein hormone family, whereas the β subunit, although structurally very similar, differs in each hormone and confers specificity of action.

scholarly journals Allosteric Regulation of the Follicle-Stimulating Hormone Receptor

Endocrinology ◽  
2018 ◽  
Vol 159 (7) ◽  
pp. 2704-2716 ◽  
Author(s):  
Selvaraj Nataraja ◽  
Venkataraman Sriraman ◽  
Stephen Palmer
Keyword(s):  
Small Molecule ◽  
Hormone Receptor ◽  
Follicle Stimulating Hormone ◽  
Receptor Activation ◽  
Luteinizing Hormone Receptor ◽  
Receptor Interaction ◽  
Surface Binding ◽  
Glycoprotein Hormone ◽  
Small Molecule Modulators ◽  
Stimulating Hormone

Abstract Follicle-stimulating hormone receptor (FSHR) belongs to the leucine-rich repeat family of the G protein–coupled receptor (LGR), which includes the glycoprotein hormone receptors luteinizing hormone receptor, thyrotropin receptor, and other LGRs 4, 5, 6, and 7. FSH is the key regulator of folliculogenesis in females and spermatogenesis in males. FSH elicits its physiological response through its cognate receptor on the cell surface. Binding of the hormone FSH to its receptor FSHR brings about conformational changes in the receptor that are transduced through the transmembrane domain to the intracellular region, where the downstream effector interaction takes place, leading to activation of the downstream signaling cascade. Identification of small molecules that could activate or antagonize FSHR provided interesting tools to study the signal transduction mechanism of the receptor. However, because of the nature of the ligand-receptor interaction of FSH-FSHR, which contains multiple sites in the extracellular binding domain, most of the small-molecule modulators of FSHR are unable to bind to the orthosteric site of the receptors. Rather they modulate receptor activation through allosteric sites in the transmembrane region. This review will discuss allosteric modulation of FSHR primarily through the discovery of small-molecule modulators, focusing on current data on the status of development and the utility of these as tools to better understand signaling mechanisms.

hCG production and activity during pregnancy

2001 ◽  
Vol 12 (3) ◽  
pp. 191-208 ◽  
Author(s):  
H S Randeva ◽  
A Jackson ◽  
E Karteris ◽  
E W Hillhouse
Keyword(s):  
Luteinizing Hormone ◽  
Chorionic Gonadotropin ◽  
Essential Role ◽  
Follicle Stimulating Hormone ◽  
Thyroid Stimulating Hormone ◽  
Β Subunit ◽  
Glycoprotein Hormone ◽  
Α Subunit ◽  
Hormone Specificity ◽  
Stimulating Hormone

Human chorionic gonadotropin (hCG) has an essential role in early pregnancy. It is a member of the glycoprotein hormone family also comprising the pituitary derived follicle stimulating hormone (FSH), luteinizing hormone (LH) and thyroid stimulating hormone (TSH). Each hormone consists of a non-covalently bound α and β subunit. Within a species the α subunit is identical and hormone specificity is determined by the unique β subunit.

FSH in therapy: physiological basis, new preparations and clinical use

1995 ◽  
Vol 4 (3) ◽  
pp. 163-177 ◽  
Author(s):  
Manuela Simoni ◽  
Eberhard Nieschlag
Keyword(s):  
Follicle Stimulating Hormone ◽  
Thyroid Stimulating Hormone ◽  
Clinical Use ◽  
Β Subunit ◽  
Glycoprotein Hormone ◽  
Physiological Basis ◽  
Α Subunit ◽  
And Function ◽  
Polypeptide Chains ◽  
Stimulating Hormone

Follicle stimulating hormone (FSH) is a glycoprotein hormone secreted by the pituitary gland that, together with luteinizing hormone (LH), controls development, maturation and function of the gonad. Like the related hormones, LH, thyroid stimulating hormone (TSH) and human chorionic gonadotropin (hCG), FSH consists of two polypeptide chains, α and β, bearing carbohydrate moietiesN-linked to asparagine (Asn) residues. The α subunit is common to all members of the glycoprotein hormone family, whereas the β subunit, although structurally very similar, differs in each hormone and confers specificity of action.

scholarly journals Glycoprotein G-protein Coupled Receptors in Disease: Luteinizing Hormone Receptors and Follicle Stimulating Hormone Receptors

Diseases ◽  
2020 ◽  
Vol 8 (3) ◽  
pp. 35
Author(s):  
Duaa Althumairy ◽  
Xiaoping Zhang ◽  
Nicholas Baez ◽  
George Barisas ◽  
Deborah A. Roess ◽  
...  
Keyword(s):  
Luteinizing Hormone ◽  
G Protein ◽  
Hormone Receptors ◽  
Follicle Stimulating Hormone ◽  
G Protein Coupled Receptors ◽  
Human Beings ◽  
Glycoprotein Hormone ◽  
Luteinizing Hormone Receptors ◽  
G Protein Coupled ◽  
Stimulating Hormone

Signal transduction by luteinizing hormone receptors (LHRs) and follicle-stimulating hormone receptors (FSHRs) is essential for the successful reproduction of human beings. Both receptors and the thyroid-stimulating hormone receptor are members of a subset of G-protein coupled receptors (GPCRs) described as the glycoprotein hormone receptors. Their ligands, follicle-stimulating hormone (FSH) and luteinizing hormone (LH) and a structurally related hormone produced in pregnancy, human chorionic gonadotropin (hCG), are large protein hormones that are extensively glycosylated. Although the primary physiologic functions of these receptors are in ovarian function and maintenance of pregnancy in human females and spermatogenesis in males, there are reports of LHRs or FSHRs involvement in disease processes both in the reproductive system and elsewhere. In this review, we evaluate the aggregation state of the structure of actively signaling LHRs or FSHRs, their functions in reproduction as well as summarizing disease processes related to receptor mutations affecting receptor function or expression in reproductive and non-reproductive tissues. We will also present novel strategies for either increasing or reducing the activity of LHRs signaling. Such approaches to modify signaling by glycoprotein receptors may prove advantageous in treating diseases relating to LHRs or FSHRs function in addition to furthering the identification of new strategies for modulating GPCR signaling.

scholarly journals Actions and Roles of FSH in Germinative Cells

2021 ◽  
Vol 22 (18) ◽  
pp. 10110
Author(s):  
Kaiana Recchia ◽  
Amanda Soares Jorge ◽  
Laís Vicari de Figueiredo Pessôa ◽  
Ramon Cesar Botigelli ◽  
Vanessa Cristiane Zugaib ◽  
...  
Keyword(s):  
Germ Cell ◽  
Germ Cells ◽  
Primordial Germ Cells ◽  
Follicle Stimulating Hormone ◽  
Adult Life ◽  
Target Cells ◽  
Β Subunit ◽  
Glycoprotein Hormone ◽  
Stimulating Hormone

Follicle stimulating hormone (FSH) is produced by the pituitary gland in a coordinated hypothalamic–pituitary–gonadal (HPG) axis event, plays important roles in reproduction and germ cell development during different phases of reproductive development (fetal, neonatal, puberty, and adult life), and is consequently essential for fertility. FSH is a heterodimeric glycoprotein hormone of two dissociable subunits, α and β. The FSH β-subunit (FSHβ) function starts upon coupling to its specific receptor: follicle-stimulating hormone receptor (FSHR). FSHRs are localized mainly on the surface of target cells on the testis and ovary (granulosa and Sertoli cells) and have recently been found in testicular stem cells and extra-gonadal tissue. Several reproduction disorders are associated with absent or low FSH secretion, with mutation of the FSH β-subunit or the FSH receptor, and/or its signaling pathways. However, the influence of FSH on germ cells is still poorly understood; some studies have suggested that this hormone also plays a determinant role in the self-renewal of germinative cells and acts to increase undifferentiated spermatogonia proliferation. In addition, in vitro, together with other factors, it assists the process of differentiation of primordial germ cells (PGCLCs) into gametes (oocyte-like and SSCLCs). In this review, we describe relevant research on the influence of FSH on spermatogenesis and folliculogenesis, mainly in the germ cell of humans and other species. The possible roles of FSH in germ cell generation in vitro are also presented.

Glycoprotein hormone alpha-subunit production and plurihormonality in human corticotroph tumours—an in vitro and immunohistochemical study

1995 ◽  
Vol 133 (1) ◽  
pp. 25-32 ◽  
Author(s):  
Bhaloo Desai ◽  
Jacqueline M Burrin ◽  
Catherine A Nott ◽  
Jennian F Geddes ◽  
Edmund J Lamb ◽  
...  
Keyword(s):  
Growth Hormone ◽  
Luteinizing Hormone ◽  
Immunohistochemical Study ◽  
Follicle Stimulating Hormone ◽  
Alpha Subunit ◽  
Bronchial Carcinoid ◽  
Glycoprotein Hormone ◽  
Nelson’S Syndrome ◽  
Stimulating Hormone

Desai B, Burrin JM, Nott CA, Geddes JF, Lamb EJ, Aylwin SJB, Wood DF, Thakkar C, Monson JP. Glycoprotein hormone alpha-subunit production and plurihormonality in human corticotroph tumours—an in vitro and immunohistochemical study. Eur J Endocrinol 1995;133:25–32. ISSN 0804–4643 Glycoprotein hormone alpha-subunit (αSU) is a recognized product of clinically non-functioning, glycoprotein hormone-secreting and somatotroph adenomas but has not been studied systematically in corticotroph tumours. We have performed immunohistochemistry for αSU in a consecutive series of four corticotroph tumours causing Nelson's syndrome, three corticotroph macroadenomas, 12 corticotroph microadenomas and one adrenocorticotrophin-secreting bronchial carcinoid tumour. In addition we have assessed αSU secretion in vitro in corticotroph adenomas from two subjects with Cushing's disease and two subjects with Nelson's syndrome. Immunohistochemistry, performed after microwave treatment of sections to enhance antigen retrieval, demonstrated αSU positivity in 3/4 Nelson's tumours, 2/3 corticotroph macroadenomas, 7/12 microadenomas and one bronchial carcinoid. Eight of the 13 tumours positive for αSU were also immunostained after microwave pretreatment of sections for thyrotrophin (six positive), follicle-stimulating hormone (four positive), luteinizing hormone (three positive), β-chorionic gonadotrophin (five positive), growth hormone (three positive) and prolactin (two positive) immunoreactivity. In vitro cell cultures of all four tumours studied secreted adrenocorticotrophin and three secreted αSU, with the variable presence of luteinizing hormone, follicle-stimulating hormone, thyrotrophin, growth hormone and prolactin, in basal culture. The αSU secretion was augmented by phorbol ester (160 ± 15%, sem, n = 3 wells; p < 0.01) and 8-bromo-cAMP (138 ± 8%; p < 0.05) in one tumour. These data indicate that plurihormonality and, in particular, αSU elaboration and secretion by corticotroph tumours is more common than hitherto recognized. Possible mechanisms include abnormal or deregulated gene expression, autocrine or paracrine effects or a stem cell origin of tumour. The possible relationship of αSU production to corticotroph tumour behaviour and prognosis remains to be established. John P Monson, Dept of Endocrinology, Royal London Hospital, Whitechapel, London El 1BB, UK

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