ライフサイエンスコーパス: hFSH

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1 hFSH beta V38A and Y39A mutants affected receptor bindin

2 hFSH with mutations of either alpha S85A, alpha T86A, al

3 itary follicle stimulating hormone (eFSH and hFSH) have been characterized in a glycosylation site-sp

4 with the corresponding sequences of hCG and hFSH or alanine cassettes.

5 ons with hLH (human leutinizing hormone) and hFSH (human follicle stimulating hormone) were > 1 micro

6 arge of the seat-belt is similar in hTSH and hFSH but different from hCG.

7 In contrast, an hTSH chimera bearing hFSH seat-belt residues did not possess any follitropic

8 ccharide-containing 20-27aa domain into beta-hFSH subunit was validated in the context of a model sys

9 of a model system, providing protected beta-hFSH subunit functionalized with chitobiose at positions

10 hFSH, hFSHR ECD, and hFSHR ECD-single chain hFSH complex.

11 ctra were recorded for purified single chain hFSH, hFSHR ECD, and hFSHR ECD-single chain hFSH complex

12 ic gonadotropin (hCG) and human follitropin (hFSH), that exhibit activity unique to a third family me

13 internalize agonist (i.e. human follitropin, hFSH) at a rate similar to that of other agonist-G prote

14 omain of human Follicle-Stimulating Hormone (hFSH) are described.

15 hCG) and human follicle-stimulating hormone (hFSH), but determinants of hTSH specificity are unknown.

16 ation of human follicle-stimulating hormone (hFSH).

17 coprotein hormones and corresponds to Q48 in hFSH beta.

18 -651), showed that both of them internalized hFSH at rates that were 2-3 times faster than rFSHR-wild

19 Mutant hFSH beta Q48A was also 8-fold less active than wild-typ

20 After comparison of wild-type and mutant hFSH activities determined in radioreceptor assays (ID50

21 Also, glycoforms at Asn52 of hFSH are all complex type, whereas in eFSH, both complex

22 t for one site in the beta subunit (Asn7) of hFSH all other sites in both species have sulfated glyco

23 ke rFSHR-wt, however, the internalization of hFSH mediated by rFSHR-t649 and rFSHR(Delta642-651) can

24 lar basis of the enhanced internalization of hFSH mediated by these mutants we used an assay that can

25 a loss of receptor binding, yet mutation of hFSH beta 37LVY39 to 37AAA39 was antecendent to a 20-fol

26 Mutation of hFSH beta 48QKTCT52 to 48AAACA52 resulted in a failure o

27 omposite mutation were made of the region of hFSH alpha 74-92, each residue substituted by alanine.

28 ylated 20-27aa domain of the beta-subunit of hFSH under a Lansbury aspartylation protocol.

29 ons were made to pinpoint which of the seven hFSH beta residues in the 37LVY39 to 37AAA39 and the 48Q

30 sylated hFSHbeta associated with four of six hFSH isoform preparations derived by chromatofocusing.

31 The hFSH and mutant hormones were tested in an in vitro bioa

32 n the long loop (between Y33 and F53) of the hFSH beta-subunit which are required for proper subunit

33 alpha S92A only retained 10% or less of the hFSH receptor-binding activity, while compared to these,

34 However, these hFSH mutants were markedly unstable at pH 2.0.

35 n wild-type hFSH when assayed for binding to hFSH receptors.

36 A was also 8-fold less active than wild-type hFSH when assayed for binding to hFSH receptors.

37 Thus, when hFSH bound first, accessibility of antibody binding was

38 as reduced to half of that of wild-type (WT) hFSH.

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