Commentary on Section 264 of ITAA 1936: commissioner may require information and evidence
Dabner, Justin
2007-01-01
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55 records were found.
Faculty Sponsor: George Bousfield; Office of Research Administration, Fairmount College of Liberal Arts and Sciences, College of Education,
College of Engineering, College of Fine Arts, University Libraries, Emory Lindquist Honors Program
Human FSH exists as two major glycoforms, tetra-glycosylated and di-glycosylated hFSH. Tetra-glycosylated FSH possesses both α and β subunit carbohydrates while di-glycosylated hFSH possesses only α subunit carbohydrates. Western blotting differentiated the glycosylated, 24 kDa hFSHβ band from the non-glycosylated 21kDa FSHβ band. As part of the laboratory-wide effort to define glycoform abundance in individual humans, FSH was isolated from pituitaries. The findings from this assay were combined with previous data from individual human pituitaries showing the highest abundance of di-glycosylated hFSH in the youngest individuals, intermediate variation in perimenopausal individuals, and low abundance in post menopausal women.
Heterodimeric pituitary gonadotropins, luteinizing hormone (LH) and follicle-stimulating
hormone (FSH), play significant roles in follicular development and maintenance of the female
reproductive cycle. FSH functions in the ovary include: stimulation of follicle growth, estradiol
synthesis and selection of dominant follicles. FSH exists as two glycoforms, designated di- and
tetra-glycosylated FSH. Di-glycosylated FSH contains 2 carbohydrates located only on the α
subunit, while tetra-glycosylated FSH has 4 carbohydrates, 2 each on the α and β subunits.
Individual pituitary FSH analysis shows that in young, reproductive-age women, di-glycosylated
FSH is more abundant than tetra-glycosylated FSH, whereas in postmenopausal women there is
more pituitary tetra-glycosylated FSH. In vitro bioassay of di-glycosylated FSH shows that it ...
Follicle-stimulating hormone (FSH) is a gonadotropic hormone produced by the ante-rior pituitary, which plays a major role in follicular development leading up to ovulation and spermatogenesis. FSH possesses two dissimilar subunits, α and β, like other members of the glycoprotein hormone family. Human FSH exists as a heterogeneous mixture of glycoforms, differing in the number and location of two β subunit N-glycans. FSH acts through its cog-nate receptor to initiate a series of physiological events required for granulosa cell prolifera-tion and differentiation in the ovary, as well as Sertoli cell function in the testis. Preliminary studies have documented thiazolidinone derivatives activate FSH receptors expressed in Chi-nese hamster ovarian (CHO) cells and rat granulosa cells, however, the mechanism of action for this compound is no...
Follicle stimulating hormone (FSH) is a glycoprotein hormone with subunits α and β, and is required for gamete development. Differential glycosylation may produce diglycosylated FSH with higher biological activity, and is suspected to be generated via the action of oligosaccharyltransferase(OST) isoforms. Signal peptide hydrophobicity of α and β maycontribute to selective usage of OST, and hence modulate N-glycosylation. We hypothesize that N-glycosylation of FSH subunits is regulated via differential interactions between OST isoforms and subunit signal peptides and modulated by estrogen. To test our hypothesis, we will engineer chimeric hFSH subunits by swapping the signal peptide sequences of α and β. Constructs with the chimeric sequences will be transfected into cell lines, and expressed FSH will be examined.
Follicle-stimulating hormone (FSH) is a glycoprotein hormone with two subunits, alpha and beta, and is required for gamete development. FSH is now known to exist as a ratio of two glycoforms that varies during the menstrual cycle and in premenopausal periods in women. A newly identified glycoform, referred to as diglycosylated FSH, is characterized by the presence of two glycans attached to the alpha subunit while none are attached to the beta subunit. Preliminary data suggest that estrogen is responsible for reducing the glycosylation of FSHbeta in reproductive-age women, thus yielding higher concentrations of diglycosylated FSH than is found in older women. This selective reduction of glycosylation of the FSHbeta subunit is suspected to be due to activity of different oligosaccharyltransferase (OST) subunit isoforms. To investigate h...
Graduate School, Academic Affairs, University Libraries
Research completed at the Department of Biological Sciences, College of Liberal Arts and Sciences, Wichita State University.
