A tale of two collagen receptors, integrin β1 and discoidin domain receptor 1, in epithelial cell differentiation

2012 ◽  
Vol 303 (12) ◽  
pp. C1207-C1217 ◽  
Author(s):  
Yi-Chun Yeh ◽  
Hsi-Hui Lin ◽  
Ming-Jer Tang
Keyword(s):  
Cell Differentiation ◽  
Epithelial Cell ◽  
Tyrosine Kinase ◽  
Disease Progression ◽  
Membrane Stability ◽  
Functional Roles ◽  
Epithelial Cell Differentiation ◽  
Collagen Receptors ◽  
E Cadherin

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.

EXTRACELLULAR MATRIX-DRIVEN ALVEOLAR EPITHELIAL CELL DIFFERENTIATION IN VITRO

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

Localized distribution of alpha 9 integrin in the cornea and changes in expression during corneal epithelial cell differentiation.

1995 ◽  
Vol 43 (4) ◽  
pp. 353-362 ◽  
Author(s):  
M A Stepp ◽  
L Zhu ◽  
D Sheppard ◽  
R L Cranfill
Keyword(s):  
Cell Differentiation ◽  
Epithelial Cell ◽  
Corneal Epithelium ◽  
Corneal Epithelial Cell ◽  
Basal Cells ◽  
Postnatal Maturation ◽  
Central Cornea ◽  
Epithelial Cell Differentiation

A recently characterized integrin alpha-chain, alpha 9, forms heterodimers with the integrin beta 1-chain and is present in the skin with a distribution similar to that of alpha 2 and alpha 3, other beta 1 integrins. To determine whether alpha 9 is expressed in the stratified squamous epithelium of the cornea, we used immunohistochemical techniques to compare the distribution of alpha 9 in the adult mouse cornea with that of alpha 3. Abundant alpha 9 was expressed in the lateral and basal membranes of the basal cells of the conjunctiva and corneal limbus, but very little alpha 9 was present in the basal cells of the central corneal epithelium. In contrast, alpha 3 was present in the membranes of basal cells of the conjunctiva, limbus, and central cornea. To determine when during postnatal maturation of the corneal epithelium alpha 9 becomes restricted to the limbus, we looked at the distribution of alpha 9 and alpha 3 in the developing mouse eye from birth to eyelid opening. At birth, the basal cells of the cornea and developing limbal region did not express alpha 9, but there was abundant alpha 9 expressed in suprabasal cells between the fused lids and in the basal cells of the skin and conjunctiva. In contrast, alpha 3, integrin was expressed uniformly in the basal cells across the surface of the conjunctiva, limbus, and cornea and was present only in the basal cells of the epithelium between the fused eyelids. In the central cornea, alpha 9 expression increased in basal cells up until Day 10 after birth. After Day 10, alpha 9 expression in the central cornea began to decrease; after the lids were open, alpha 9 expression in the central cornea became restricted to the limbus. In the basal and suprabasal cells between the fused eyelids expression of alpha 9 became increasingly restricted over time to the basal cells. Recent data suggest that alpha 9 beta 1 can interact with tenascin. Our dual labeling confocal microscopy studies indicate that localization of alpha 9 and tenascin are not coordinated in the developing mouse cornea. Many recent studies have shown an important role for beta 1 integrins in mediating epithelial cell differentiation in vitro; in vivo, changes in integrin expression have been found in wound healing, psoriasis, and in basal and squamous cell carcinomas.(ABSTRACT TRUNCATED AT 400 WORDS)

In vitro models of intestinal epithelial cell differentiation

2006 ◽  
Vol 23 (4) ◽  
pp. 241-256 ◽  
Author(s):  
P. Simon-Assmann ◽  
N. Turck ◽  
M. Sidhoum-Jenny ◽  
G. Gradwohl ◽  
M. Kedinger
Keyword(s):  
Cell Differentiation ◽  
Epithelial Cell ◽  
Intestinal Epithelial Cell ◽  
In Vitro Models ◽  
Intestinal Epithelial ◽  
Epithelial Cell Differentiation

scholarly journals Hedgehog signaling regulates E-cadherin expression for the maintenance of the actin cytoskeleton and tight junctions

2010 ◽  
Vol 299 (6) ◽  
pp. G1252-G1265 ◽  
Author(s):  
Chang Xiao ◽  
Sally A. Ogle ◽  
Michael A. Schumacher ◽  
Neal Schilling ◽  
Robert A. Tokhunts ◽  
...  
Keyword(s):  
Cell Differentiation ◽  
Epithelial Cell ◽  
Tight Junctions ◽  
Hedgehog Signaling ◽  
Protein Complexes ◽  
Cell Lineage ◽  
Adherens Junction ◽  
Epithelial Cell Differentiation ◽  
Junction Protein ◽  
E Cadherin

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.

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
Keyword(s):  
Cell Differentiation ◽  
Epithelial Cell ◽  
Molecular Complexes ◽  
Annexin A2 ◽  
Serine Phosphorylation ◽  
Cell Junction ◽  
Affinity Column ◽  
Caveolin 1 ◽  
Epithelial Cell Differentiation ◽  
E Cadherin

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.

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