Analysis of Differential Glycosylation Patterns of Human FSH

نویسندگان

  • Carrie Chambers
  • Bin Shuai
  • George Bousfield
چکیده

Follicle stimulating hormone (FSH) is a glycoprotein hormone with subunitsαandβ, 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.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

The Relationship of Secretion and Activity of Recombinant Factor IX with N-Glycosylation

Background:  Human coagulation factor IX (hFIX) is a glycoprotein with two N-glycosylation sites at the activation peptide. Since the activation peptide is removed in mature hFIX, the exact role of N-glycosylation is unclear. To investigate the role of N-glycosylation in the secretion and activity of hFIX, we inhibited N-glycosylation by tunicamycin in the stable Human Embryonic Kidney (HEK)- c...

متن کامل

Glycosylation Effects on FSH-FSHR Interaction Dynamics: A Case Study of Different FSH Glycoforms by Molecular Dynamics Simulations

The gonadotropin known as follicle-stimulating hormone (FSH) plays a key role in regulating reproductive processes. Physiologically active FSH is a glycoprotein that can accommodate glycans on up to four asparagine residues, including two sites in the FSHα subunit that are critical for biochemical function, plus two sites in the β subunit, whose differential glycosylation states appear to corre...

متن کامل

Dynamic changes in glycosylation and glycan composition of serum FSH and LH during natural ovarian stimulation

BACKGROUND Glycosylation and glycan composition are of fundamental importance for the biological properties of FSH and LH. The aim of this study was to determine the glycosylation, sialylation, and sulfonation of serum FSH and LH throughout the normal menstrual cycle. METHODS Serum samples were collected from 79 healthy women with regular menstrual cycles. The mean numbers of anionic monosacc...

متن کامل

Naturally Occurring Follicle-Stimulating Hormone Glycosylation Variants

Follicle-stimulating hormone (FSH) is a member of the glycoprotein hormone family, which is a subfamily of the cystine knot growth factor superfamily [1,2]. The glycoprotein hormones are composed of heterodimeric glycoprotein subunits, a common α-subunit, and a hormone-specific β-subunit. While the α-subunit primary structure is identical for all glycoprotein hormones within the same species, t...

متن کامل

Changes in Glycosylation of Alpha-1-Protease Inhibitor in Inflammation (Rheumatoid Arthritis and Crohn\'s Disease)

Alpha-1-proteinase inhibitor (API) is one of the acute phase proteins. Following an inflammatory stimuli the concentration of API increased up to four folds. Accompanying these quantitative changes, there is qualitative alterations in the structure of carbohydrate moiety (glycosylation). To determine the alterations in the glycosylation of API in inflammation, API was isolated from the sera of...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:

دوره   شماره 

صفحات  -

تاریخ انتشار 2009