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Yan C Cheng – One of the best experts on this subject based on the ideXlab platform.

  • biology and regulation of ectoplasmic specialization an atypical Adherens Junction type in the testis
    Biochimica et Biophysica Acta, 2008
    Co-Authors: Elissa W P Wong, Dolores D Mruk, Yan C Cheng

    Abstract:

    Anchoring Junctions are cell adhesion apparatus present in all epithelia and endothelia. They are found at the cell-cell interface (Adherens Junction (AJ) and desmosome) and cell-matrix interface (focal contact and hemidesmosome). In this review, we focus our discussion on AJ in particular the dynamic changes and regulation of this Junction type in normal epithelia using testis as a model. There are extensive restructuring of AJ (e.g., ectoplasmic specialization, ES, a testis-specific AJ) at the Sertoli-Sertoli cell interface (basal ES) and Sertoli-elongating spermatid interface (apical ES) during the seminiferous epithelial cycle of spermatogenesis to facilitate the migration of developing germ cells across the seminiferous epithelium. Furthermore, recent findings have shown that ES also confers cell orientation and polarity in the seminiferous epithelium, illustrating that some of the functions initially ascribed to tight Junctions (TJ), such as conferring cell polarity, are also part of the inherent properties of the AJ (e.g., apical ES) in the testis. The biology and regulation based on recent studies in the testis are of interest to cell biologists in the field, in particular their regulation, which perhaps is applicable to tumorigenesis.

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  • mitogen activated protein kinases Adherens Junction dynamics and spermatogenesis a review of recent data
    Developmental Biology, 2005
    Co-Authors: Chinghang Wong, Yan C Cheng

    Abstract:

    Mitogen-activated protein kinases (MAPKs) are important regulators of many cellular processes. In mammalian testes, these kinases are involved in controlling cell division, differentiation, survival and death, and are therefore critical to spermatogenesis. Recent studies have also illustrated their involvement in Junction restructuring in the seminiferous epithelium, especially at the ectoplasmic specialization (ES), a testis-specific Adherens Junction (AJ) type. ES contributes to the adhesion between Sertoli cells at the blood-testis barrier, as well as between Sertoli and developing spermatids (step 9 and beyond) at the adluminal compartment. MAPKs regulate AJ dynamics in the testis via their effects on the turnover of Junction-associated protein complexes, the production of proteases and protease inhibitors, and the cytoskeleton structure. In this review, roles of the three major MAPK members, namely extracellular signal-regulated kinase (ERK), c-Jun N-terminal kinase (JNK), and p38 MAPK, in ES dynamics are critically discussed. An integrated model of how these three MAPKs regulate adhesion function in the seminiferous epithelium is also presented. This model will serve as the framework for future investigation in the field.

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  • regulation of sertoli germ cell Adherens Junction dynamics via changes in protein protein interactions of the n cadherin β catenin protein complex which are possibly mediated by c src and myotubularin related protein 2 an in vivo study using an andro
    Endocrinology, 2005
    Co-Authors: Jiayi Zhang, Chinghang Wong, Dolores D Mruk, Nikki P Y Lee, Weiliang Xia, Will M Lee, Yan C Cheng

    Abstract:

    Using a well characterized model of cell-cell actin-based Adherens Junction (AJ) disruption by suppressing the intratesticular testosterone level in adult rats with testosterone-estradiol implants, we have confirmed earlier findings that Sertoli-germ cell AJ dynamics are regulated by the activation of kinases via putative signaling pathways but with some unexpected findings as follows. First, the loss of germ cells from the seminiferous epithelium during androgen suppression was associated with a surge in myotubularin-related protein 2 (MTMR2, a lipid phosphatase, in which adult MTMR2−/− mice were recently shown to be azoospermic because of the loss of cell adhesion function between germ and Sertoli cells); kinases: phosphatidylinositol 3-kinase, c-Src, and C-terminal Src kinase; adaptors: α-actinin, vinculin, afadin, and p130 Crk-associated protein; and AJ-integral membrane proteins at the ectoplasmic specialization (ES, a testis-specific cell-cell actin-based AJ type) site: N-cadherin, β-catenin, integr…

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Peter Mundel – One of the best experts on this subject based on the ideXlab platform.

  • the glomerular slit diaphragm is a modified Adherens Junction
    Journal of The American Society of Nephrology, 2000
    Co-Authors: Jochen Reiser, Wilhelm Kriz, Matthias Kretzler, Peter Mundel

    Abstract:

    Abstract . The glomerular slit diaphragm between podocyte foot processes shares typical morphologic features with an Adherens Junction. Differentiated cultured podocytes form cellular structures comparable to filtration slits in vivo . At those sites, zonula occludens-1 (ZO-1) was coexpressed with P-cadherin as well as with α-, β-, and γ-catenin. In situ , P-cadherin was detected at the slit diaphragm in association with ZO-1 as shown by confocal microscopy and immunogold double labeling electron microscopy. P-cadherin expression in vivo and in vitro was confirmed by reverse transcription-PCR. These findings led to the concept that the slit diaphragm represents an Adherens Junction composed of P-cadherin, α-, β-, and γ-catenin, and ZO-1. In contrast to an Adherens Junction of a similar composition recently described in cultured fibroblasts, the slit diaphragm complex does not contain vinculin, which was found in nearby focal contacts. A P-cadherinbased Adherens Junction is well-suited to explain the zipper-like structure of the slit diaphragm. The present study should allow new avenues leading to the identification of additional slit diaphragm-associated proteins conferring specificity to this unique cell Junction.

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  • the glomerular slit diaphragm is a modified Adherens Junction
    Journal of The American Society of Nephrology, 2000
    Co-Authors: Jochen Reiser, Wilhelm Kriz, Matthias Kretzler, Peter Mundel

    Abstract:

    The glomerular slit diaphragm between podocyte foot processes shares typical morphologic features with an Adherens Junction. Differentiated cultured podocytes form cellular structures comparable to filtration slits in vivo. At those sites, zonula occludens-1 (ZO-1) was coexpressed with P-cadherin as well as with alpha-, beta-, and gamma-catenin. In situ, P-cadherin was detected at the slit diaphragm in association with ZO-1 as shown by confocal microscopy and immunogold double labeling electron microscopy. P-cadherin expression in vivo and in vitro was confirmed by reverse transcription-PCR. These findings led to the concept that the slit diaphragm represents an Adherens Junction composed of P-cadherin, alpha-, beta-, and gamma-catenin, and ZO-1. In contrast to an Adherens Junction of a similar composition recently described in cultured fibroblasts, the slit diaphragm complex does not contain vinculin, which was found in nearby focal contacts. A P-cadherin-based Adherens Junction is well-suited to explain the zipper-like structure of the slit diaphragm. The present study should allow new avenues leading to the identification of additional slit diaphragm-associated proteins conferring specificity to this unique cell Junction.

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Haiyan Xu – One of the best experts on this subject based on the ideXlab platform.

  • Comparative study of in vitro effects of different nanoparticles at non-cytotoxic concentration on the Adherens Junction of human vascular endothelial cells
    International Journal of Nanomedicine, 2019
    Co-Authors: Aiyun Yang, Lingyu Piao, Lifan Du, Jie Meng, Haiyan Xu

    Abstract:

    Effects of different nanoparticles (NPs) exposure at acutely non-cytotoxic concentrations are particularly worthy to figure out, compare, and elucidate.
    To investigate and compare the effect of a small library of NPs at non-cytotoxic concentration on the Adherens Junction of human umbilical vein endothelial cells (HUVECs), obtaining new insights of NPs safety evaluation.
    The HUVECs layer was exposed to NPs including gold (Au), platinum (Pt), silica (SiO2), titanium dioxide (TiO2), ferric oxide (Fe2O3), oxidized multi-walled carbon nanotubes, with different surface chemistry and size distribution. Cellular uptake of NPs was observed by transmission electron microscopy. and the cytotoxicity was determined by Cell Counting Kit-8 assay. The NP-induced variation of intracellular reactive oxygen species (ROS) and catalase (CAT) activity was measured using the probe of 2’7′-dichlorodihydr fluorescein diacetate and a CAT analysis kit, respectively. The level of VE-cadherin of HUVECs was analyzed by Western blot, and the loss of Adherens Junction was observed with laser confocal microscopy.
    The acutely non-cytotoxic concentrations of different NPs were determined and applied to HUVECs. The NPs increased the level of intracellular ROS and the activity of CAT to different degrees, depending on the characteristics. At the same time, the HUVECs lost their Adherens Junction protein VE-cadherin and gaps were formed between the cells. The NP-induced oxidative stress and gap formation could be rescued by the supplementary N-acetylcysteine in the incubation.
    The increase of intracellular ROS and CAT activity was one common effect of NPs, even at the non-cytotoxic concentration, and the degree was dependent on the composition, surface chemistry, and size distribution of the NP. The effect led to the gap formation between the cells, while could be rescued by the antioxidant. Therefore, the variation of Adherens Junction between endothelial cells was suggested to evaluate for NPs when used as therapeutics and diagnostics.

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  • comparative study of in vitro effects of different nanoparticles at non cytotoxic concentration on the Adherens Junction of human vascular endothelial cells
    International Journal of Nanomedicine, 2019
    Co-Authors: Aiyun Yang, Lingyu Piao, Lifan Du, Jie Meng, Haiyan Xu

    Abstract:

    Background: Effects of different nanoparticles (NPs) exposure at acutely non-cytotoxic concentrations are particularly worthy to figure out, compare, and elucidate. Objective: To investigate and compare the effect of a small library of NPs at non-cytotoxic concentration on the Adherens Junction of human umbilical vein endothelial cells (HUVECs), obtaining new insights of NPs safety evaluation. Materials and methods: The HUVECs layer was exposed to NPs including gold (Au), platinum (Pt), silica (SiO2), titanium dioxide (TiO2), ferric oxide (Fe2O3), oxidized multi-walled carbon nanotubes, with different surface chemistry and size distribution. Cellular uptake of NPs was observed by transmission electron microscopy. and the cytotoxicity was determined by Cell Counting Kit-8 assay. The NP-induced variation of intracellular reactive oxygen species (ROS) and catalase (CAT) activity was measured using the probe of 2’7′-dichlorodihydr fluorescein diacetate and a CAT analysis kit, respectively. The level of VE-cadherin of HUVECs was analyzed by Western blot, and the loss of Adherens Junction was observed with laser confocal microscopy. Results: The acutely non-cytotoxic concentrations of different NPs were determined and applied to HUVECs. The NPs increased the level of intracellular ROS and the activity of CAT to different degrees, depending on the characteristics. At the same time, the HUVECs lost their Adherens Junction protein VE-cadherin and gaps were formed between the cells. The NP-induced oxidative stress and gap formation could be rescued by the supplementary N-acetylcysteine in the incubation. Conclusion: The increase of intracellular ROS and CAT activity was one common effect of NPs, even at the non-cytotoxic concentration, and the degree was dependent on the composition, surface chemistry, and size distribution of the NP. The effect led to the gap formation between the cells, while could be rescued by the antioxidant. Therefore, the variation of Adherens Junction between endothelial cells was suggested to evaluate for NPs when used as therapeutics and diagnostics.

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