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Difference between follistatin isoforms in the inhibition of activin signalling: activin neutralizing activity of follistatin isoforms is dependent on their affinity for activin.

Abstract：

:We demonstrate the difference between the follistatin isoforms (FS-288 and FS-315), two activin-binding proteins, in the neutralizing activity for activin signalling. Transcriptional reporter assay using 3TP-Lux, an activin-responsive reporter construct, showed that the inhibitory effect of FS-288 on activin-induced transcriptional response is more potent than that of FS-315. The potency was not influenced by the presence of heparan sulfates, by which FS, in particular FS-288, associates with cell surfaces at a high affinity. Furthermore, FS-288 inhibited the binding of activin to its type II receptor more markedly than did FS-315, as evidenced by surface plasmon resonance and affinity cross-linking experiments. Moreover, the Kd of FS-288 and FS-315 for activin A was estimated to be 46.5+/-0.37 pM and 432+/-26 pM, respectively, by surface plasmon resonance experiments. These results indicate that the different potency between the two FS isoforms in the inhibition of activin activities depends on their affinity for activin A.

journal_name

Cell Signal

journal_title

Cellular signalling

authors

Hashimoto O,Kawasaki N,Tsuchida K,Shimasaki S,Hayakawa T,Sugino H

doi

10.1016/s0898-6568(00)00099-1

subject

Has Abstract

pub_date

2000-08-01 00:00:00

pages

565-71

issue

8

eissn

0898-6568

issn

1873-3913

pii

S0898-6568(00)00099-1

journal_volume

12

pub_type

杂志文章

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