Alteration of the actin cytoskeleton and localisation of the α6β1 and α3 integrins during regeneration of the rat submandibular gland

Shimizu, Osamu; Shiratsuchi, Hiroshi; Ueda, Kôichiro; Oka, Shogo; Yonehara, Yoshiyuki

doi:10.1016/j.archoralbio.2012.02.018

Cited by 7 publications

(4 citation statements)

References 24 publications

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“…Mice lacking the α6 integrin die shortly after birth because of severe blistering of the skin and other epithelia [Georges‐Labouesse et al, ], a defect that can only be partially compensated by α3 integrin [van der Neut et al, ; De Arcangelis et al, ]. During development and wound healing, both of these integrins show an orchestrated redistribution of their cellular localization that affects their function [Shimizu et al, ]. During cell migration, α3 integrin [Barczyk et al, ] is observed at the tip of the lamellipodia and is involved in the deposition of a provisional extracellular matrix, subsequently utilized by α6 integrin for collective epithelial migration [Margadant et al, ].…”

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confidence: 99%

Characterization of Laminin Binding Integrin Internalization in Prostate Cancer Cells

Das

Anderson

Gard

et al. 2017

J of Cellular Biochemistry

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Laminin binding integrins α6 (CD49f) and α3 (CD49c) are persistently but differentially expressed in prostate cancer (PCa). Integrin internalization is an important determinant of their cell surface expression and function. Using flow cytometry, and first order kinetic modeling, we quantitated the intrinsic internalization rates of integrin subunits in a single cycle of internalization. In PCa cell line DU145, α6 integrin internalized with a rate constant (kactual) of 3.25 min−1, threefold faster than α3 integrin (1.0 min−1), 1.5‐fold faster than the vitronectin binding αv integrin (CD51) (2.2 min−1), and significantly slower than the unrelated transferrin receptor (CD71) (15 min−1). Silencing of α3 integrin protein expression in DU145, PC3, and PC3B1 cells resulted in up to a 1.71‐fold increase in kactual for α6 integrin. The internalized α6 integrin was targeted to early endosomes but not to lamp1 vesicles. Depletion of α3 integrin expression resulted in redistribution of α6β4 integrin to an observed cell–cell staining pattern that is consistent with a suprabasal distribution observed in epidermis and early PIN lesions in PCa. Depletion of α3 integrin increased cell migration by 1.8‐fold, which was dependent on α6β1 integrin. Silencing of α6 integrin expression however, had no significant effect on the kactual of α3 integrin or its distribution in early endosomes. These results indicate that α3 and α6 integrins have significantly different internalization kinetics and that coordination exists between them for internalization. J. Cell. Biochem. 118: 1038–1049, 2017. © 2016 Wiley Periodicals, Inc.

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confidence: 99%

Characterization of Laminin Binding Integrin Internalization in Prostate Cancer Cells

Das

Anderson

Gard

et al. 2017

J of Cellular Biochemistry

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“…To investigate the association between salivary gland atrophy and regeneration, many studies have employed a duct ligation model (16)(17)(18)(19). In this model, ligation causes acinar cells to disappear and increases the amount of connective tissue, while its release induces the appearance of DLSs and the proliferation of acinar cells, after which immature acinar cells appear.…”

Section: Distribution Of Aquaporin-5 Transforming Growth Factor-β 1 mentioning

confidence: 99%

Distribution of aquaporin-5, transforming growth factor-β<sub>1</sub> and laminin during regeneration of atrophic rat submandibular glands after duct ligation

et al. 2018

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The aim of this study was to determine the localization of aquaporin-5 (AQP5), transforming growth factor-β 1 (TGF-β 1) and laminin during regeneration of the rat submandibular gland. After duct ligation for 7 days, the regenerating glands were collected on days 0, 1, 3, 7, and 14 after ligation release to study the process of regeneration. Immunohistochemical staining revealed apical expression of AQP5 in many acinar cells, strong expression in intercalated ducts (ICDs) of the normal submandibular gland at Day 14, and strong expression in duct-like structures (DLSs) during regeneration from Day 0 to 7. However, a few AQP5-negative acinar cells were detected during regeneration. At Day 0, immunopositivity for TGF-β 1 was detected in connective tissue. At Days 3 and 7 during regeneration, TGF-β 1 immunostaining was observed in DLSs, which were surrounded by α-smooth muscle actin-positive thickened myoepithelial cells. Laminin staining was strong in the thickened basement membrane of DLSs at Day 3 during regeneration, but weak around acinar cells at Day 14. These findings suggest that TGF-β 1 is involved in the environment around DLSs, myoepithelial cells and laminin, that DLSs have the same functional properties as ICDs, and that AQP5-negative acinar cells may be mucous cells.

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“…Many studies (Bhaskar et al 1966;Burgess et al 1996;Takahashi et al 2004;Ueda et al 2009) have used a duct ligation model to analyze atrophy and regeneration of the submandibular gland. In this model (Shimizu et al 2012), the ligation causes most acinar cells to disappear and increase the amount of connective tissue, while its release induces the appearance of duct-like structures (DLS) and the proliferation of residual acinar cells, after which immature acinar cells appear.…”

Section: Introductionmentioning

confidence: 99%

Immunolocalization of FGF-2, -7, -8, -10 and FGFR-1–4 during regeneration of the rat submandibular gland

et al. 2015

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Fibroblast growth factors (FGFs) and their receptors (FGFRs) play important roles in the development of the submandibular gland. Although regeneration of submandibular glands follows a similar process to their development, it is unknown how FGFs and FGFRs are distributed during regeneration of submandibular gland. The aim of this study was to determine the localization of FGFs and FGFRs during such regenerative processes. After 7 days' obstruction, the submandibular glands were collected at days 0, 1, 3, 7, 11 and 14 after duct release to study regeneration. The regenerative processes of the submandibular gland were investigated by immunohistochemistry for FGF-2, 7, 8, 10 and FGFR-1-4. Immunohistochemical staining revealed that FGF-2 was moderately expressed in the epithelial cells of duct-like structures (DLS) and newly formed acinar cells (NFAC) at days 0-7, and strongly in intercalated duct (ICD) at control gland and Day 7-14. FGF-7 was localized moderately in NFAC and DLS. FGF-8 was localized moderately in the epithelial cells of DLS during regeneration. Strong positive immunoreactions for FGF-10 were found in NFAC and the epithelial cells of DLS during regeneration, as well as the ICD and lateral surfaces of the maturing acinar cells (MAC). FGFR-1 was expressed moderately in the ICD, and weakly in the NFAC and MAC. Positive immunoreactions for FGFR-2 were not observed during regeneration. Additionally, FGFR-4 was detected strongly in the ICD and slightly in NFAC. These findings suggest that FGF-2, -7, -8 and -10 play important roles in NFAC, MAC, and DLS through FGFR-1 and -4 during regeneration of submandibular gland.

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Alteration of the actin cytoskeleton and localisation of the α6β1 and α3 integrins during regeneration of the rat submandibular gland

Cited by 7 publications

References 24 publications

Characterization of Laminin Binding Integrin Internalization in Prostate Cancer Cells

Characterization of Laminin Binding Integrin Internalization in Prostate Cancer Cells

Distribution of aquaporin-5, transforming growth factor-β<sub>1</sub> and laminin during regeneration of atrophic rat submandibular glands after duct ligation

Immunolocalization of FGF-2, -7, -8, -10 and FGFR-1–4 during regeneration of the rat submandibular gland

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