A role for glycosylation of the alpha subunit in transduction of biological signal in glycoprotein hormones.
The biological properties of recombinants of glycoprotein hormones in which the alpha and beta subunits were differentially deglycosylated have been investigated. Specific deglycosylation of the alpha subunit generated a recombinant that had more receptor-binding activity but did not produce hormone response in the target cells. The deglycosylated alpha + beta recombinant was also an antagonist of the action of the native hormone. Thus, the carbohydrates in the alpha subunit play a dominant role in the transduction of the hormone signal into the cell.
Sairam
M R
MR
Bhargavi
G N
GN
D000818:Animals; D000242:Cyclic AMP / Q000378:metabolism; D005260:Female; D005640:Follicle Stimulating Hormone / Q000502:physiology*; D006023:Glycoproteins / Q000502:physiology*; D007985:Leydig Cells / Q000502:physiology; D007986:Luteinizing Hormone / Q000502:physiology*; D008297:Male; D010053:Ovary / Q000502:physiology; D051381:Rats; D011956:Receptors, Cell Surface / Q000502:physiology*; D011962:Receptors, FSH; D011974:Receptors, LH; D012671:Seminiferous Tubules / Q000502:physiology; D012756:Sheep; D013329:Structure-Activity Relationship; D013552:Swine
D006023:Glycoproteins; D011956:Receptors, Cell Surface; D011962:Receptors, FSH; D011974:Receptors, LH; D007986:Luteinizing Hormone; D005640:Follicle Stimulating Hormone; D000242:Cyclic AMP