scholarly journals Secreted Phosphoprotein 1 (SPP1, Osteopontin) Binds to Integrin Alphavbeta6 on Porcine Trophectoderm Cells and Integrin Alphavbeta3 on Uterine Luminal Epithelial Cells, and Promotes Trophectoderm Cell Adhesion and Migration1

2009 ◽  
Vol 81 (5) ◽  
pp. 814-825 ◽  
Author(s):  
David W. Erikson ◽  
Robert C. Burghardt ◽  
Kayla J. Bayless ◽  
Greg A. Johnson
Keyword(s):  
Cell Adhesion ◽  
Epithelial Cells ◽  
Integrin Alphavbeta3 ◽  
Trophectoderm Cells ◽  
Secreted Phosphoprotein 1 ◽  
Luminal Epithelial Cells

scholarly journals Highly metastatic claudin-low mammary cancers can originate from luminal epithelial cells

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Patrick D. Rädler ◽  
Barbara L. Wehde ◽  
Aleata A. Triplett ◽  
Hridaya Shrestha ◽  
Jonathan H. Shepherd ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Stem Cell ◽  
Epithelial Cells ◽  
Triple Negative ◽  
Molecular Subtype ◽  
Ras Signaling ◽  
Preneoplastic Lesions ◽  
Independent Manner ◽  
Oncogenic Ras ◽  
Luminal Epithelial Cells

AbstractClaudin-low breast cancer represents an aggressive molecular subtype that is comprised of mostly triple-negative mammary tumor cells that possess stem cell-like and mesenchymal features. Little is known about the cellular origin and oncogenic drivers that promote claudin-low breast cancer. In this study, we show that persistent oncogenic RAS signaling causes highly metastatic triple-negative mammary tumors in mice. More importantly, the activation of endogenous mutant KRAS and expression of exogenous KRAS specifically in luminal epithelial cells in a continuous and differentiation stage-independent manner induces preneoplastic lesions that evolve into basal-like and claudin-low mammary cancers. Further investigations demonstrate that the continuous signaling of oncogenic RAS, as well as regulators of EMT, play a crucial role in the cellular plasticity and maintenance of the mesenchymal and stem cell characteristics of claudin-low mammary cancer cells.

scholarly journals The In Vitro Effect of Steroid Hormones, Arachidonic Acid, and Kinases Inhibitors on Aquaporin 1, 2, 5, and 7 Gene Expression in the Porcine Uterine Luminal Epithelial Cells during the Estrous Cycle

Cells ◽  
2021 ◽  
Vol 10 (4) ◽  
pp. 832
Author(s):  
Damian Tanski ◽  
Agnieszka Skowronska ◽  
Malgorzata Tanska ◽  
Ewa Lepiarczyk ◽  
Mariusz T. Skowronski
Keyword(s):  
Arachidonic Acid ◽  
Epithelial Cells ◽  
Steroid Hormones ◽  
Estrous Cycle ◽  
Kinase Inhibitor ◽  
Mapk Signaling ◽  
Mapk Kinase ◽  
Vitro Effect ◽  
Luminal Epithelial Cells

Aquaporins (AQPs) are integral membrane proteins, which play an important role in water homeostasis in the uterus. According to the literature, the expression of aquaporins in reproductive structures depends on the local hormonal milieu. The current study investigated the effect of selected PKA kinase inhibitor H89 and MAPK kinase inhibitor PD98059, on the expression of AQP1, 2, 5, and 7, and steroid hormones (E2), progesterone (P4), and arachidonic acid (AA) in the porcine endometrium on days 18–20 and 2–4 of the estrous cycle (the follicular phase where estrogen and follicle-stimulating hormone (FSH) are secreted increasingly in preparation for estrus and the luteal phase where the ovarian follicles begin the process of luteinization with the formation of the corpus luteum and progesterone secretion, respectively). The luminal epithelial cells were incubated in vitro in the presence of the aforementioned factors. The expression of mRNA was determined by the quantitative real-time PCR technique. In general, in Experiment 1, steroid hormones significantly increased expression of AQP1, 2, and 5 while arachidonic acid increased expression of AQP2 and AQP7. On the other hand, MAPK kinase inhibitor significantly decreased the expression of AQP1 and 5. In Experiment 2, E2, P4, or AA combined with kinase inhibitors differentially affected on AQPs expression. E2 in combination with PKA inhibitor significantly decreased expression of AQP1 but E2 or P4 combined with this inhibitor increased the expression of AQP5 and 7. On the contrary, E2 with PD98059 significantly increased AQP5 and AQP7 expression. Progesterone in combination with MAPK kinase inhibitor significantly downregulated the expression of AQP5 and upregulated AQP7. Arachidonic acid mixed with H89 or PD98059 caused a decrease in the expression of AQP5 and an increase of AQP7. The obtained results indicate that estradiol, progesterone, and arachidonic acid through PKA and MAPK signaling pathways regulate the expression of AQP1 and AQP5 in the porcine luminal epithelial cells in the periovulatory period.

Redistribution and dysfunction of integrins in cultured renal epithelial cells exposed to oxidative stress

1993 ◽  
Vol 264 (1) ◽  
pp. F149-F157 ◽  
Author(s):  
J. Gailit ◽  
D. Colflesh ◽  
I. Rabiner ◽  
J. Simone ◽  
M. S. Goligorsky
Keyword(s):  
Oxidative Stress ◽  
Cell Adhesion ◽  
Epithelial Cell ◽  
Epithelial Cells ◽  
Cell Surface ◽  
Apical Cell ◽  
Flow Cytometric Analysis ◽  
Adhesion Properties ◽  
Renal Tubular Cells ◽  
Renal Tubular

Tubular obstruction by detached renal tubular epithelial cells is a major cause of oliguria in acute renal failure. Viable renal tubular cells can be recovered from urine of patients with acute tubular necrosis, suggesting a possible defect in cell adhesion to the basement membrane. To study this process of epithelial cell desquamation in vitro, we investigated the effect of nonlethal oxidative stress on the integrin adhesion receptors of the primate kidney epithelial cell line BS-C-1. Morphological and functional studies of cell adhesion properties included the following: interference reflection microscopy, intravital confocal microscopy and immunocytochemistry, flow cytometric analysis of integrin receptor abundance, and cell-matrix attachment assay. High levels of the integrin subunits alpha 3, alpha v, and beta 1 were detected on the cell surface by fluorescence-activated cell sorting (FACS) analysis, as well as lower levels of alpha 1, alpha 2, alpha 4, alpha 5, alpha 6, and beta 3. Exposure of BS-C-1 cells to nonlethal oxidative stress resulted in the disruption of focal contacts, disappearance of talin from the basal cell surface, and in the redistribution of integrin alpha 3-subunits from predominantly basal location to the apical cell surface. As measured in a quantitative cell attachment assay, oxidative stress decreased BS-C-1 cell adhesion to type IV collagen, laminin, fibronectin, and vitronectin. Defective adhesion was not associated with a loss of alpha 3-, alpha 4-, or alpha v-integrin subunits from the cell surface.(ABSTRACT TRUNCATED AT 250 WORDS)

Carboxymethyl β-glucan Binds to Corneal Epithelial Cells and Increases Cell Adhesion to Laminin and Resistance to Oxidative Stress

Cornea ◽  
2007 ◽  
Vol 26 (1) ◽  
pp. 73-79 ◽  
Author(s):  
Marco Porcu ◽  
Francesco Guarna ◽  
Laura Formentini ◽  
Giuseppe Faraco ◽  
Silvia Fossati ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Cell Adhesion ◽  
Epithelial Cells ◽  
Corneal Epithelial Cells ◽  
Corneal Epithelial

scholarly journals Human Blastocysts and Endometrial Epithelial Cells Express Activated Leukocyte Cell Adhesion Molecule (ALCAM/CD166)

2003 ◽  
Vol 88 (7) ◽  
pp. 3437-3443 ◽  
Author(s):  
Hiroshi Fujiwara ◽  
Keiji Tatsumi ◽  
Kenzo Kosaka ◽  
Yukiyasu Sato ◽  
Toshihiro Higuchi ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Epithelial Cells ◽  
Adhesion Molecule ◽  
Cell Adhesion Molecule ◽  
Endometrial Epithelial Cells

Regulation of epithelial and lymphocyte cell adhesion by adenosine deaminase–CD26 interaction

2002 ◽  
Vol 361 (2) ◽  
pp. 203-209 ◽  
Author(s):  
Silvia GINÉS ◽  
Marta MARIÑO ◽  
Josefa MALLOL ◽  
Enric I. CANELA ◽  
Chikao MORIMOTO ◽  
...  
Keyword(s):  
T Cells ◽  
Cell Adhesion ◽  
T Cell ◽  
B Cells ◽  
Epithelial Cell ◽  
Epithelial Cells ◽  
Cell Surface ◽  
Adenosine Deaminase ◽  
Cell To Cell Adhesion ◽  
Lymphocyte Cell

The extra-enzymic function of cell-surface adenosine deaminase (ADA), an enzyme mainly localized in the cytosol but also found on the cell surface of monocytes, B cells and T cells, has lately been the subject of numerous studies. Cell-surface ADA is able to transduce co-stimulatory signals in T cells via its interaction with CD26, an integral membrane protein that acts as ADA-binding protein. The aim of the present study was to explore whether ADA—CD26 interaction plays a role in the adhesion of lymphocyte cells to human epithelial cells. To meet this aim, different lymphocyte cell lines (Jurkat and CEM T) expressing endogenous, or overexpressing human, CD26 protein were tested in adhesion assays to monolayers of colon adenocarcinoma human epithelial cells, Caco-2, which express high levels of cell-surface ADA. Interestingly, the adhesion of Jurkat and CEM T cells to a monolayer of Caco-2 cells was greatly dependent on CD26. An increase by 50% in the cell-to-cell adhesion was found in cells containing higher levels of CD26. Incubation with an anti-CD26 antibody raised against the ADA-binding site or with exogenous ADA resulted in a significant reduction (50–70%) of T-cell adhesion to monolayers of epithelial cells. The role of ADA—CD26 interaction in the lymphocyte—epithelial cell adhesion appears to be mediated by CD26 molecules that are not interacting with endogenous ADA (ADA-free CD26), since SKW6.4 (B cells) that express more cell-surface ADA showed lower adhesion than T cells. Adhesion stimulated by CD26 and ADA is mediated by T cell lymphocyte function-associated antigen. A role for ADA—CD26 interaction in cell-to-cell adhesion was confirmed further in integrin activation assays. FACS analysis revealed a higher expression of activated integrins on T cell lines in the presence of increasing amounts of exogenous ADA. Taken together, these results suggest that the ADA—CD26 interaction on the cell surface has a role in lymphocyte—epithelial cell adhesion.

Involvement of Nestin in the Progression of Canine Mammary Carcinoma

2021 ◽  
pp. 030098582110186
Author(s):  
Hisashi Yoshimura ◽  
Maiko Moriya ◽  
Ayaka Yoshida ◽  
Masami Yamamoto ◽  
Yukino Machida ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Mammary Carcinoma ◽  
Mammary Tumors ◽  
Carcinoma Cells ◽  
Nestin Expression ◽  
Mammary Carcinomas ◽  
Canine Mammary Carcinoma ◽  
Canine Mammary Tumors ◽  
Mammary Carcinoma Cells ◽  
Luminal Epithelial Cells

Nestin, a class VI intermediate filament protein, is known to be expressed in various types of human neoplasms, including breast cancer, and is associated with their progression. However, its expression and role in canine mammary tumors remain unknown. We analyzed nestin expression in canine mammary tumors using in situ hybridization and immunohistochemistry. We also investigated its role in a canine mammary carcinoma cell line using RNA interference. Nestin expression was not observed in luminal epithelial cells of any of the 62 cases of benign mammary lesions examined, although myoepithelial cells showed its expression in most cases. In 16/50 (32%) primary mammary carcinomas and 6/15 (40%) metastases of mammary carcinomas, cytoplasmic nestin expression was detected in luminal epithelial cells. In luminal cells of primary mammary carcinomas, its expression was positively related to several pathological parameters that indicate high-grade malignancy, including histological grading ( P < .01), vascular/lymphatic invasion ( P < .01), Ki-67 index ( P < .01), and metastasis ( P < .05). Immunohistochemistry revealed that nestin expression was related to vimentin expression in mammary carcinomas ( P < .01). This relationship was confirmed using reverse transcription-quantitative polymerase chain reaction using 9 cell lines derived from canine mammary carcinoma ( P < .01). Finally, nestin knockdown in canine mammary carcinoma cells using small interfering RNA inhibited cell proliferation and migration based on WST-8, Boyden chamber, and cell-tracking assays. These findings suggest that nestin may at least partially mediate these behaviors of canine mammary carcinoma cells.

scholarly journals Selectivity in the transport of spermatozoa to oviductal reservoirs in the menstruating fruit bat, Carollia perspicillata

Reproduction ◽  
2010 ◽  
Vol 140 (5) ◽  
pp. 743-757 ◽  
Author(s):  
John J Rasweiler ◽  
Nilima K Badwaik ◽  
Kiranmayi V Mechineni
Keyword(s):  
Epithelial Cells ◽  
Fine Particulate Matter ◽  
Uterine Cavity ◽  
Elastic Fibers ◽  
Carollia Perspicillata ◽  
Fruit Bat ◽  
Fine Particulate ◽  
Uterine Mucosa ◽  
Luminal Epithelial Cells ◽  
Gain Access

To better document the timing of ovulation and fertilization, female reproductive tracts were collected every 12 h from captive-bred fruit bats (Carollia perspicillata) on days 1–3 postcoitum and examined histologically. This also permitted observations on sperm transport, storage, and disposition. As the animals had previously been sexually segregated, most had been cycling and possessed menstrual uteri at the time of collection. Menstruation is periovulatory in this species. A widespread, headfirst orientation of spermatozoa to the uterine mucosa was observed in specimens apparently collected soon after insemination. Thereafter, however, this relationship was limited in most cases to the area around the entrance of each uterotubal junction (UTJ). A small number of spermatozoa also colonized the UTJs, which functioned as temporary sperm reservoirs on days 1–2. AlthoughC. perspicillatais monovular, no consistent differences were observed between the two oviducts in the pattern of sperm storage and release. Very few sperm were ever observed in the isthmus or ampulla (the site of fertilization). Menstrual debris (including fine particulate matter) and leukocytes present in the uterine cavity in most tracts did not gain access to the UTJ with the spermatozoa. Smooth muscle and abundant elastic fibers in the wall of the intramural UTJ, as well as receptors on its luminal epithelial cells, may play roles in the selective transport of spermatozoa to the fertilization site. While some spermatozoa are phagocytosed in the uterine lumen or by epithelial cells in the UTJ, the fate of most is probably expulsion into the vagina.

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