Characterization and nucleotide sequence of the gene for the common α subunit of the bovine pituitary glycoprotein hormones

ABSTRACT Recombinant cDNA clones that encode the α subunit of the chicken pituitary glycoprotein hormones were isolated from a pituitary library. The longer of the two cDNA clones that were sequenced was 754bp in length. It contained 81 nucleotides of the 5′-untranslated region (UTR), an open-reading frame of 360bp that encoded a 24 amino acid leader polypeptide sequence as well as the 96 amino acid mature α subunit, and 268 nucleotides of the 3′-UTR, followed by a 45 bp poly(A) tract. There was 69–79% homology between the nucleotide sequence of the coding region for the chicken and mammalian α-subunit cDNAs. Northern blot analysis revealed that the steady-state levels of an approximately 800 bp α-subunit specific transcript increased quantitatively when dispersed chicken pituitary glands were treated in culture with chicken gonadotrophin-releasing hormone-I.

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Nucleotide sequence of a cDNA for the common alpha subunit of the bovine pituitary glycoprotein hormones. Conservation of nucleotides in the 3'-untranslated region of bovine and human pre-alpha subunit mRNAs.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)32472-4 ◽

1983 ◽

Vol 258 (8) ◽

pp. 4679-4682

Author(s):

J H Nilson ◽

A R Thomason ◽

M T Cserbak ◽

C L Moncman ◽

R P Woychik

Keyword(s):

Nucleotide Sequence ◽

Untranslated Region ◽

Alpha Subunit ◽

Glycoprotein Hormones ◽

The Common

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COMPARISON OF CIRCULATING GLYCOPROTEIN HORMONES AND THEIR SUBUNITS IN PATIENTS WITH OAT CELL CARCINOMA OF THE LUNG AND URAEMIC PATIENTS ON CHRONIC DIALYSIS

Acta Endocrinologica ◽

10.1530/acta.0.0830026 ◽

1976 ◽

Vol 83 (1) ◽

pp. 26-35 ◽

Cited By ~ 20

Author(s):

C. Hagen ◽

E. D. Gilby ◽

A. S. McNeilly ◽

K. Ølgaard ◽

P. K. Bondy ◽

...

Keyword(s):

Renal Failure ◽

Chronic Renal Failure ◽

Cell Carcinoma ◽

Normal Subjects ◽

Glycoprotein Hormones ◽

Α Subunit ◽

Female Patients ◽

Disease States ◽

Oat Cell Carcinoma ◽

The Common

ABSTRACT It has recently been suggested that the measurement of the glycoprotein hormones and their subunits in human serum may serve as biochemical markers of non-endocrine tumours. Using radioimmunoassays for LH, FSH, HCGβ-, LHβ- and the common α-subunit, significant differences in the levels of these substances could not be detected between patients with oat cell lung tumours and patients with chronic renal failure. However, compared to normal subjects the α-subunit levels in serum were elevated in 12% of the male and 30% of the female patients with oat cell carcinoma of the lung and in 80 and 50% of the male and female patients, respectively, with chronic renal failure. The LHβ-subunit concentration was normal in all tumour patients and none of these patients had detectable (< 4 ng/ml) levels of HCGβ-subunit. While such measurements may be of value in relationship to particular neoplasms, it appears that raised levels of glycoproteins and their subunits may be found in other disease states.

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Pars tuberalis-specific cells in the ovine pituitary do express the common α-chain of glycoprotein hormones: an in situ hybridization and immunocytochemical study

Acta Endocrinologica ◽

10.1530/eje.0.1310540 ◽

1994 ◽

Vol 131 (5) ◽

pp. 540-546 ◽

Cited By ~ 11

Author(s):

TM Böckers ◽

J Bockmann ◽

J-D Fauteck ◽

MR Kreutz ◽

R Bock ◽

...

Keyword(s):

In Situ Hybridization ◽

Secretory Activity ◽

Immunocytochemical Staining ◽

Pars Tuberalis ◽

Glycoprotein Hormones ◽

Immunocytochemical Study ◽

Α Subunit ◽

The Common ◽

Α Chain

Böckers TM, Bockmann J, Fauteck J-D, Kreutz MR, Bock R, Wittkowski W. Pars tuberalis-specific cells in the ovine pituitary do express the common α-chain of glycoprotein hormones: an in situ hybridization and immunocytochemical study. Eur J Endocrinol 1994;131:540–6. ISSN 0804–4643 The ovine pituitary pars tuberalis was investigated by electron microscopy, immunocytochemistry and non-radioactive in situ hybridization in order to characterize further the pars tuberalis-specific cells, whose functional role within the endocrine system is still enigmatic. Ultrastructural analysis revealed that, besides gonadotropic cells, the vast majority of cells in the ovine pars tuberalis show the typical characteristics of pars tuberalis-specific cells with clear signs of secretory activity. Immunocytochemical staining with a polyclonal antibody directed against the α-subunit of ovine glycoprotein hormones and in situ hybridization with an antisense oligonucleotide complementary to the α-subunit mRNA showed that the common α-chain of glycoprotein hormones is expressed in pars tuberalis-specific cells. Antibodies against the β-subunits failed to detect any of the known β-chains of pituitary glycoprotein hormones in these cells. The demonstration of the glycoprotein α-subunit in pars tuberalis-specific cells of the adult sheep supports previously existing evidence that these cells do secrete one or more glycoprotein hormones. With respect to the thyrotropin-β-like immunoreactivity in rats and hamsters, one might speculate that pars tuberalis-specific cells are a pluripotent cell type with a low secretory activity under basal conditions. Further studies should prove the hypothesis that a pre-existing mRNA pool in these cells can be used for sustained translation of glycoprotein hormones after physiological or pharmacological stimulation. W Wittkowski, Institute of Anatomy, University of Münster, Vesaliusweg 2–4, 48 129 Münster, Germany

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