scholarly journals Annexin A2 expression and partners during epithelial cell differentiation

2019 ◽  
Vol 97 (5) ◽  
pp. 612-620 ◽  
Author(s):  
Malik Zibouche ◽  
Françoise Illien ◽  
Jesus Ayala-Sanmartin

The members of the annexin family of calcium- and phospholipid-binding proteins participate in different cellular processes. Annexin A2 binds to S100A10, forming a functional heterotetrameric protein that has been involved in many cellular functions, such as exocytosis, endocytosis, cell junction formation, and actin cytoskeleton dynamics. Herein, we studied annexin A2 cellular movements and looked for its partners during epithelial cell differentiation. By using immunofluorescence, mass spectrometry (MS), and western blot analyses after S100A10 affinity column separation, we identified several annexin A2–S100A10 partner candidates. The association of putative annexin A2–S100A10 partner candidates obtained by MS after column affinity was validated by immunofluorescence and sucrose density gradient separation. The results show that three proteins are clearly associated with annexin A2: E-cadherin, actin, and caveolin 1. Overall, the data show that annexin A2 can associate with molecular complexes containing actin, caveolin 1, and flotillin 2 before epithelial differentiation and with complexes containing E-cadherin, actin, and caveolin 1, but not flotillin 2 after cell differentiation. The results indicate that actin, caveolin 1, and E-cadherin are the principal protein partners of annexin A2 in epithelial cells and that the serine phosphorylation of the N-terminal domain does not play an essential role during epithelial cell differentiation.

2010 ◽  
Vol 299 (6) ◽  
pp. G1252-G1265 ◽  
Author(s):  
Chang Xiao ◽  
Sally A. Ogle ◽  
Michael A. Schumacher ◽  
Neal Schilling ◽  
Robert A. Tokhunts ◽  
...  

In the stomach, strictly regulated cell adherens junctions are crucial in determining epithelial cell differentiation. Sonic Hedgehog (Shh) regulates epithelial cell differentiation in the adult stomach. We sought to identify whether Shh plays a role in regulating adherens junction protein E-cadherin as a mechanism for epithelial cell differentiation. Mouse nontumorigenic gastric epithelial (IMGE-5) cells treated with Hedgehog signaling inhibitor cyclopamine and anti-Shh 5E1 antibody or transduced with short hairpin RNA against Skinny Hedgehog (IMGE-5Ski) were cultured. A mouse model expressing a parietal cell-specific deletion of Shh (HKCre/ShhKO) was used to identify further changes in adherens and tight junctions. Inhibition of Hedgehog signaling in IMGE-5 cells caused loss of E-cadherin expression accompanied by disruption of F-actin cortical expression and relocalization of zonula occludens-1 (ZO-1). Loss of E-cadherin was also associated with increased proliferation in IMGE-5Ski cells and increased expression of the mucous neck cell lineage marker MUC6. Compared with membrane-expressed E-cadherin and ZO-1 protein in controls, dissociation of E-cadherin/β-catenin and ZO-1/occludin protein complexes was observed in HKCre/ShhKO mice. In conclusion, we demonstrate that Hedgehog signaling regulates E-cadherin expression that is required for the maintenance of F-actin cortical expression and stability of tight junction protein ZO-1.


2012 ◽  
Vol 303 (12) ◽  
pp. C1207-C1217 ◽  
Author(s):  
Yi-Chun Yeh ◽  
Hsi-Hui Lin ◽  
Ming-Jer Tang

As increase in collagen deposition is no longer taken as simply a consequence but, rather, an inducer of disease progression; therefore, the understanding of collagen signal transduction is fundamentally important. Cells contain at least two types of collagen receptors: integrins and discoidin domain receptors (DDRs). The integrin heterodimers α1β1, α2β1, α10β1, and α11β1 are recognized as the non-tyrosine kinase collagen receptors. DDR1 and 2, the tyrosine kinase receptors of collagen, are specifically expressed in epithelium and mesenchyme, respectively. While integrin β1 and DDR1 are both required for cell adhesion on collagen, their roles in epithelial cell differentiation during development and disease progression seem to counteract each other, with integrin β1 favoring epithelium mesenchyme transition (EMT) and DDR1 inducing epithelial cell differentiation. The in vitro evidence shows that the integrin β1 and DDR1 exert opposing actions in regulation of membrane stability of E-cadherin, which itself is a critical regulator of epithelial cell differentiation. Here, we review the functional roles of integrin β1 and DDR1 in regulation of epithelial cell differentiation during development and disease progression, and explore the underlining mechanisms regarding to the regulation of membrane stability of E-cadherin.


2017 ◽  
Vol 361 (1) ◽  
pp. 112-125
Author(s):  
Maximilian Niit ◽  
Rozanne Arulanandam ◽  
Jamaica Cass ◽  
Mulu Geletu ◽  
Victoria Hoskin ◽  
...  

2020 ◽  
Author(s):  
Jason J. Gokey ◽  
John Snowball ◽  
Anusha Sridharan ◽  
Parvathi Sudha ◽  
Joseph A. Kitzmiller ◽  
...  

2013 ◽  
Vol 91 (3) ◽  
pp. 1102-1111 ◽  
Author(s):  
M. K. VanKlompenberg ◽  
R. Manjarin ◽  
J. F. Trott ◽  
H. F. McMicking ◽  
R. C. Hovey

2005 ◽  
Vol 31 (5) ◽  
pp. 461-482 ◽  
Author(s):  
Colin E. Olsen ◽  
Brant E. Isakson ◽  
Gregory J. Seedorf ◽  
Richard L. Lubman ◽  
Scott Boitano

Sign in / Sign up

Export Citation Format

Share Document