Glycoprotein hormone receptors (version 2020.4) in the IUPHAR/BPS Guide to Pharmacology Database

Glycoprotein hormone receptors (provisional nomenclature [45]) are activated by a non-covalent heterodimeric glycoprotein made up of a common α chain (glycoprotein hormone common alpha subunit CGA, P01215), with a unique β chain that confers the biological specificity to FSH, LH, hCG or TSH. There is binding cross-reactivity across the endogenous agonists for each of the glycoprotein hormone receptors. The deglycosylated hormones appear to exhibit reduced efficacy at these receptors [120]

Glycoprotein hormone receptors (version 2019.4) in the IUPHAR/BPS Guide to Pharmacology Database

Glycoprotein hormone receptors (provisional nomenclature [45]) are activated by a non-covalent heterodimeric glycoprotein made up of a common α chain (glycoprotein hormone common alpha subunit CGA, P01215), with a unique β chain that confers the biological specificity to FSH, LH, hCG or TSH. There is binding cross-reactivity across the endogenous agonists for each of the glycoprotein hormone receptors. The deglycosylated hormones appear to exhibit reduced efficacy at these receptors [120]

Glycoprotein hormone receptors in GtoPdb v.2023.1

Glycoprotein hormone receptors (provisional nomenclature [47]) are activated by a non-covalent heterodimeric glycoprotein made up of a common α chain (glycoprotein hormone common alpha subunit CGA, P01215), with a unique β chain that confers the biological specificity to FSH, LH, hCG or TSH. There is binding cross-reactivity across the endogenous agonists for each of the glycoprotein hormone receptors. The deglycosylated hormones appear to exhibit reduced efficacy at these receptors [122, 31]

Anti-Müllerian hormone in men with normal and reduced sperm concentration and men with maldescended testes

Objective: To evaluate serum anti-Müllerian hormone (AMH) in well-characterized men with normal and reduced sperm concentration and in men with a history of or persistent maldescended testes as a possible clinical marker of male factor infertility and/or maldescended testes. Design: Retrospective analysis of 199 men selected from our database (Androbase). Setting: The university-based Institute of Reproductive Medicine. Patient(s): One hundred eight men with normal and 60 men with reduced sperm concentration without known cause of infertility and additionally 31 infertile men with current or former maldescended testes were evaluated. Intervention(s): Serum AMH was analyzed by an in-house ELISA. Main Outcome Measure(s): Hormone and semen parameters were compared and correlated with AMH. Result(s): No significant differences were found in AMH levels. Only in men with maldescended testes did AMH correlate negatively with FSH and positively with testicular volume and sperm concentration. No correlations between AMH and LH or testosterone (T) were found. Conclusion(s): Anti-Müllerian hormone serum levels are not significantly affected by impaired spermatogenesis in general but are correlated with spermatogenic parameters in men with current or former maldescended testes. Therefore, AMH measurement does not improve clinical routine diagnostics but should be evaluated further in patients with maldescended testes. Anti-Müllerian hormone might serve as a marker of Sertoli cell number, function, and/or maturation in these men

Structure and Chromosomal Localization of the Human Anti-Müllerian Hormone Type II Receptor Gene

Using the rat anti-müllerian hormone type II receptor (AMHRII) cDNA as a probe, two overlapping lambda phage clones containing the AMHRII gene were isolated from a human genomic library. Sequence analysis of the exons was performed and the exon/intron boundaries were determined. The coding region was found to consist of 11 exons, divided over 8 kb. The genomic structure resembles that of the related activin type II receptor gene. The AMHRII gene was mapped to human chromosome 12q12-q13. The results reported are essential for identification of AMHRII gene alterations in patients with persistent müllerian duct syndrome.</p

Structure and Chromosomal Localization of the Human Anti-Müllerian Hormone Type II Receptor Gene

Using the rat anti-müllerian hormone type II receptor (AMHRII) cDNA as a probe, two overlapping lambda phage clones containing the AMHRII gene were isolated from a human genomic library. Sequence analysis of the exons was performed and the exon/intron boundaries were determined. The coding region was found to consist of 11 exons, divided over 8 kb. The genomic structure resembles that of the related activin type II receptor gene. The AMHRII gene was mapped to human chromosome 12q12-q13. The results reported are essential for identification of AMHRII gene alterations in patients with persistent müllerian duct syndrome.</p

Women have more potential to induce browning of perirenal adipose tissue than men

Objective Brown adipose tissue (BAT) can generate heat by burning fatty acids, a process mediated by uncoupling protein 1 (UCP1). White adipose tissue (WAT) depots can gain BAT-like properties, and various studies have suggested that females have more active BAT or BAT-like WAT. We studied sex differences in BAT-like properties of human perirenal adipose tissue. Methods Perirenal and subcutaneous adipose tissue was obtained from 20 male and 24 female healthy live kidney donors. Mesenchymal stem cells (MSCs), adipocyte precursor cells, were isolated from these depots to study whether intrinsic factors control BAT-like properties of the adipose tissue depots. Results When average outside temperature a week before harvesting was below 11C, brown-like adipocytes expressing UCP1 were present in perirenal adipose tissue of women, but not of men. MSCs derived from perirenal adipose tissue expressed significantly more UCP1 when from female origin compared to male origin (P = 0.009). However, UCP1 protein content and oxygen consumption rate did not differ between adipocytes derived from male and female perirenal MSCs. Conclusions Female perirenal adipose tissue has a higher potency to gain BAT-like properties than male perirenal adipose tissue. The degree of gaining BAT-like properties depends on sex-specific intrinsic factors and environmental triggers such as temperature