RT Journal Article
SR Electronic
T1 Serum albumin maintains Wnt water-solubility and activity
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 2023.01.22.525087
DO 10.1101/2023.01.22.525087
A1 Joo Hye Yeo
A1 Soon Sung Kwon
A1 Jiyeon Chae
A1 Ines Kusen
A1 Jaeeun Han
A1 Ju Yeon Lim
A1 Jae-Ho Cheong
A1 Taeil Kim
A1 Yang Ouk Jung
A1 Chul Hoon Kim
A1 Jinu Lee
YR 2023
UL http://biorxiv.org/content/early/2023/01/23/2023.01.22.525087.abstract
AB Wnt proteins regulate adult tissue homeostasis and repair by driving stem cell self-renewal and differentiation. High-performance Wnt preparations have enormous therapeutic potential, especially alongside various stem cell technologies. Currently, most of these Wnt preparations contain FBS or the detergent CHAPS to maintain Wnt solubility and activity. Recently, afamin was identified as a serum factor that solubilizes Wnt3a in conditioned media (CM), obviating the requirement for animal sera. Here, we report serum albumin (SA) is required for afamin-mediated solubilization of Wnt3a in CM. Moreover, SA-mediated solubilization of purified Wnt3a in tubes does not require afamin. This means conventional CHAPS-Wnt3a preparations can be modified into SA-purified Wnt3a (SA-pWnt3a) preparations by exchanging CHAPS for SA through dialysis. SA-pWnt3a preparations effectively promote the growth of human stem cell organoids. These data suggest SA as a physiological factor for maintaining Wnt3a activity in therapeutic applications.Competing Interest StatementC.H.K. is supported in part by a collaborative research grant from Interpark Bio Convergence Corp.