Organic compounds -- part of the class 532-570 series – Organic compounds – Carbohydrates or derivatives
Patent
1991-05-31
1993-01-26
Lacey, David L.
Organic compounds -- part of the class 532-570 series
Organic compounds
Carbohydrates or derivatives
4353201, 530395, C07K 1300, C07H 2104, C12N 1512
Patent
active
051823756
ABSTRACT:
Two follistatin proteins with inhibin-like activity were isolated from porcine follicular fluid using heparin-Sepharose affinity chromatography, followed by gel filtration on Sephacryl S-200 and then six steps of high-performance liquid chromatography. The larger protein has 315 residues and is believed to be glycosylated. The smaller protein is a 288-residue, C-terminally shortened version thereof. These proteins specifically inhibit basal secretion of FSH, but not of LH, in a rat anterior pituitary monolayer culture system. The half-maximal effective dose for both is 2.5-6.0 ng/ml. Human and rat follistatins exhibit very high homology with the porcine protein, with the human differing from porcine in only 4 residues out of 315 and with the rat differing from porcine in only 8 residues out of 315. Using the porcine amino acid sequence information, cDNA clones encoding these proteins were identified from a porcine ovarian cDNA library. Then, using the porcine cDNA as a probe, the cloning and sequencing of the corresponding human and rat proteins were accomplished.
REFERENCES:
Shimasaki, S. et al., Biochem. Biophys. Research Comm., 152 (2): 717-23, 1988.
Esch, F. S. et al., Miol. Endocrinol., 1 (11): 849-55, 1987, Biosis Abstract No. 6477285.
Shimasaki, S. et al., Proc. Natl. Acad. Sci. USA, 85 (12): 4218-22, 1988, Biosis Abstract No. 6592157.
Robertson, D. M. et al., Biochem. Biophys. Research Comm., 149 (2): 744-49, 1987.
Esch Frederick S.
Guillemin Roger C. L.
Ling Nicholas C. K.
Shimasaki Shunichi
Ueno Naoto
Allen Marianne Porta
Lacey David L.
The Salk Institute for Biological Studies
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