Presence of α-and β-Integrin Subunits in Rabbit Lacrimal Gland Acinar Cells Cultured on a Laminin-Rich Matrix

Gierow, J. Peter; Andersson, Sofia V.; Sjögren, Elsie C.

doi:10.1007/978-1-4615-0717-8_7

Cited by 6 publications

(2 citation statements)

References 5 publications

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“…Furthermore, Western blotting confirmed that ␣ v integrin, the major receptor for the penton base, is expressed in LGAC at levels comparable to those for HeLa cells (Fig. 3C), consistent with a previous study reporting the expression of ␣ v integrin in intact lacrimal tissue (21).…”

Section: Vol 80 2006 Fiber-mediated Ad5 Uptake In Lacrimal Acini 11837supporting

confidence: 91%

Novel Fiber-Dependent Entry Mechanism for Adenovirus Serotype 5 in LacrimalAcini

Xie

Chiang²,

Contreras³

et al. 2006

J Virol

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The established mechanism for infection of most cells with adenovirus serotype 5 (Ad5) involves fiber capsid protein binding to coxsackievirus-adenovirus receptor (CAR) at the cell surface, followed by penton base capsid protein binding to ␣ v integrins, which triggers clathrin-mediated endocytosis of the virus. Here we determined the identity of the capsid proteins responsible for mediating Ad5 entry into the acinar epithelial cells of the lacrimal gland. Ad5 transduction of primary rabbit lacrimal acinar cells was inhibited by excess Ad5 fiber or knob (terminal region of the fiber) but not excess penton base. Investigation of the interactions of recombinant Ad5 penton base, fiber, and knob with lacrimal acini revealed that the penton base capsid protein remained surface associated, while the knob domain of the fiber capsid protein was rapidly internalized. Introduction of rabbit CAR-specific small interfering RNA (siRNA) into lacrimal acini under conditions that reduced intracellular CAR mRNA significantly inhibited Ad5 transduction, in contrast to a control (nonspecific) siRNA. Preincubation of Ad5 with excess heparin or pretreatment of acini with a heparinase cocktail each inhibited Ad5 transduction by a separate and apparently additive mechanism. Functional and imaging studies revealed that Ad5, fiber, and knob, but not penton base, stimulated macropinocytosis in acini and that inhibition of macropinocytosis significantly reduced Ad5 transduction of acini. However, inhibition of macropinocytosis did not reduce Ad5 uptake. We propose that internalization of Ad5 into lacrimal acini is through a novel fiber-dependent mechanism that includes CAR and heparan sulfate glycosaminoglycans and that the subsequent intracellular trafficking of Ad5 is enhanced by fiber-induced macropinocytosis.

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Section: Vol 80 2006 Fiber-mediated Ad5 Uptake In Lacrimal Acini 11837supporting

confidence: 91%

Novel Fiber-Dependent Entry Mechanism for Adenovirus Serotype 5 in LacrimalAcini

Xie

Chiang²,

Contreras³

et al. 2006

J Virol

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“…Integrins, consisting of an α- and a β-subunit, are cell adhesion glycoprotein transmembrane receptors that play the central role in establishing the orientation of epithelial cell polarity and cell migration. We and others have demonstrated expression of several integrins (including integrin β-1) in the LG (Saarloos et al, 1999; Gierow et al, 2002; Andersson et al, 2006; Umazume et al, 2015). Moreover epithelial β1 integrin has important functions in branching morphogenesis and epithelial cell differentiation (Davies and Fisher, 2002; Zhang et al, 2009; Smeeton et al, 2010; Plosa et al, 2014; Yazlovitskaya et al, 2015).…”

Section: Resultsmentioning

confidence: 80%

FGF Gradient Controls Boundary Position Between Proliferating and Differentiating Cells and Regulates Lacrimal Gland Growth Dynamics

2019

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Fibroblast growth factor (FGF) signaling plays an important role in controlling cell proliferation, survival, and cell movements during branching morphogenesis of many organs. In mammals branching morphogenesis is primarily regulated by members of the FGF7-subfamily (FGF7 and FGF10), which are expressed in the mesenchyme, and signal to the epithelial cells through the “b” isoform of fibroblast growth factor receptor-2 (FGFR2). Our previous work demonstrated that FGF7 and FGF10 form different gradients in the extracellular matrix (ECM) and induce distinct cellular responses and gene expression profiles in the lacrimal and submandibular glands. The last finding was the most surprising since both FGF7 and FGF10 bind signal most strongly through the same fibroblast growth factor receptor-2b isoform (FGFR2b). Here we revisit this question to gain an explanation of how the different FGFs regulate gene expression. For this purpose, we employed our ex vivo epithelial explant migration assay in which isolated epithelial explants are grown near the FGF loaded beads. We demonstrate that the graded distribution of FGF induces activation of ERK1/2 MAP kinases that define the position of the boundary between proliferating “bud” and differentiating “stalk” cells of growing lacrimal gland epithelium. Moreover, we showed that gene expression profiles of the epithelial explants exposed to distinct FGFs strictly depend on the ratio between “bud” and “stalk” area. Our data also suggests that differentiation of “stalk” and “bud” regions within the epithelial explants is necessary for directional and persistent epithelial migration. Gaining a better understanding of FGF functions is important for development of new approaches to enhance tissue regeneration.

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The role of the lacrimal functional unit in the pathophysiology of dry eye

Stern

Gao

Siemasko

et al. 2004

Experimental Eye Research

489

309

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Presence of α-and β-Integrin Subunits in Rabbit Lacrimal Gland Acinar Cells Cultured on a Laminin-Rich Matrix

Cited by 6 publications

References 5 publications

Novel Fiber-Dependent Entry Mechanism for Adenovirus Serotype 5 in LacrimalAcini

Novel Fiber-Dependent Entry Mechanism for Adenovirus Serotype 5 in LacrimalAcini

FGF Gradient Controls Boundary Position Between Proliferating and Differentiating Cells and Regulates Lacrimal Gland Growth Dynamics

The role of the lacrimal functional unit in the pathophysiology of dry eye

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