Molecular cloning of cDNAs for precursors of porcine pituitary glycoprotein hormone common α-subunit and of thyroid stimulating hormone β-subunit

1989 ◽  
Vol 63 (1-2) ◽  
pp. 209-217 ◽  
Author(s):  
Hirai Toshiaki ◽  
Takikawa Hiroo ◽  
Kato Yukio
1995 ◽  
Vol 4 (3) ◽  
pp. 163-177 ◽  
Author(s):  
Manuela Simoni ◽  
Eberhard Nieschlag

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.


2001 ◽  
Vol 12 (3) ◽  
pp. 191-208 ◽  
Author(s):  
H S Randeva ◽  
A Jackson ◽  
E Karteris ◽  
E W Hillhouse

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.


1995 ◽  
Vol 4 (3) ◽  
pp. 163-177 ◽  
Author(s):  
Manuela Simoni ◽  
Eberhard Nieschlag

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.


Endocrinology ◽  
2007 ◽  
Vol 148 (7) ◽  
pp. 3468-3476 ◽  
Author(s):  
Kee K. Kim ◽  
Seok B. Song ◽  
Kwang I. Kang ◽  
Myungchull Rhee ◽  
Kyoon Eon Kim

Although there is evidence that the LIM homeodomain transcription factor, Lhx2, can stimulate transcription of the glycoprotein hormone α-subunit gene, the role of Lhx2 in regulating TSH β-subunit has not been established. In the present studies, the ability of Lhx2 to regulate transcription of the TSH β-subunit gene was examined. In the thyrotrope-derived TαT1 cell line, Lhx2 expression was found to be induced by treatment with either TRH or cAMP, consistent with the possibility that Lhx2 may play a role in mediating the ability of this signaling pathway to stimulate TSH gene expression. Transient, forced overexpression of Lhx2 stimulated activity of a TSH β-subunit reporter gene. Deletion studies provided evidence that the −177 to −79 region of the TSH β-subunit promoter was necessary for stimulation of reporter gene activity by Lhx2. A gel mobility shift assay provided the evidence that Lhx2 can bind to this region of DNA. DNase I footprinting studies demonstrated that two distinct regions of the TSHβ promoter, −118 to −108 and −86 to −68, are protected by Lhx2 from nuclease digestion. These regions contain repeats of the sequence, 5′-(G/T)CAAT(T/A)-3′. Mutation of this sequence, especially in the −86 to −68 region, substantially decreased Lhx2 responsiveness of the TSH β-subunit reporter gene. In addition, a DNA fragment containing the −177 to −79 region of the TSHβ promoter was found to confer Lhx2 responsiveness to a minimal promoter. These results provide multiple lines of evidence consistent with a role for Lhx2 in modulating expression of the TSH β-subunit gene.


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