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KMID : 0900920020260040395
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Korean journal of Animal Reproduction
2002 Volume.26 No. 4 p.395 ~ p.399
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COOH-Terminal Animo Acids of Tethered-Buman Glycoprotein Bormone alpha-Subunit Play an Important Role for Secretion
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Min K.-S.
Yoon J.-K.
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Abstract
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Human chorionic gonadotropin (hCG) is a member of the glycoprotein hormone family which includes FSH. hCG TSH. These hormone family is characterized by a heterodimeric structure composed a common alpha-subunit noncovalently linked to a hormone specific beta-subunit. To determine u and beta -subunits can be synthesized as a single polypeptide chain (tethered-hCG) and also display biological activity, the tethered-hCC and -FSH molecule by fusing the carboxyl terminus of the hCG beta-subunit to the amino terminus of the alpha-subunit was constructed. To determine the importance of alpha COOH -terminal amino acid, we also deleted the alpha COOH-terminal amino acids. The expressing vectors were transfected into CHO-K 1 cells. The tethered-wthCG and -wtFSH was efficiently secreted. The alpha Δ83hCG and alpha Δ 83FSH mutants had no secretion. These results are the first conclusive evidence that COOH-terminal amino acids are very important for secretion in human glycoprotein hormone alpha-subunit. These results demonstrated that the alpha Δ83hCG and alpha Δ 83FSH mutants could be play a pivotal role in the secretion of tethered-molecule.
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KEYWORD
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Tethered-hCG/FSH, C-terminal deletion mutant, Recombinant, CHO cells
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