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1.
J Gastrointest Surg ; 26(11): 2351-2353, 2022 11.
Artículo en Inglés | MEDLINE | ID: mdl-35641813

RESUMEN

BACKGROUND: Metastasis is the worst prognostic variable of patients with colorectal cancer (CRC). For the development of metastases, it is necessary that cancer cells detach from the primary tumor, migrate into the angiolymphatic system, and invade the tissue where they will develop. The breakdown of the tight junctions (TJs) plays an important role in colorectal metastatic tumors. Claudin-3 and occludin are the main component proteins of TJs. AIM: To analyze the expression and tissue content of claudin-3 and occludin in normal and neoplastic tissues of patients with metastatic CRC. METHODS: Fifty-seven consecutive patients with stage III and IV CRC were included. Fragments of neoplastic tissue were collected from the tumor margins, and samples of the normal tissue were collected from the same patient in a standardized distance of 10 cm from the cranial margin of the tumor. Immunohistochemistry technique was used to identify the tissue staining of claudin-3 and occludin. To measure the content of both proteins in cellular membranes of normal and cancer cells, a validated immunoscore was used. RESULTS: Claudin-3 and occludin in normal tissues are in the apical and lateral membranes of cells, while in the neoplastic, in cytoplasm. The mean of the tissue content of claudin-3 in the normal tissue was 2.57 ± 0.16, while in the neoplastic tissue was 1.03 ± 0.13. The contents of occludin were 2.77 ± 0.1 in normal tissue, while in the neoplastic were 1.08 ± 0.14. CONCLUSION: There is a reduction in the content of the claudin-3 and occludin in the cell membranes of the neoplastic tissue in patients with CRC.


Asunto(s)
Neoplasias Colorrectales , Uniones Estrechas , Humanos , Ocludina/análisis , Ocludina/metabolismo , Claudina-3/análisis , Claudina-3/metabolismo , Claudina-1/análisis , Claudina-1/metabolismo , Uniones Estrechas/química , Uniones Estrechas/metabolismo , Uniones Estrechas/patología , Neoplasias Colorrectales/patología
2.
Biochim Biophys Acta Mol Cell Res ; 1866(3): 418-429, 2019 03.
Artículo en Inglés | MEDLINE | ID: mdl-30296500

RESUMEN

Colorectal cancer (CRC) is frequently a lethal disease because of metastasis. Actin cytoskeletal rearrangement is an essential step in cell migration during activation of the epithelial-mesenchymal transition (EMT) program, which is associated with metastatic properties of cancer cells. Cofilin-1 protein modulates actin dynamics by promoting actin treadmilling, thereby driving membrane protrusion and cell migration and invasion. However, the role of cofilin-1 during EMT in CRC is unknown. Here, we show that cofilin-1 and p-cofilin-1 have distinct subcellular distribution in EMT cells, as determined by super-resolution microscopy images, indicating distinct roles in different areas of cells. Silenced cofilin-1 cells treated with TGF-ß (siCofilin-1/TGF-ß) evaded p-LIMK2-p-cofilin-1 status, leading to recovery of E-cadherin and claudin-3 at the cell-cell contact and their respective protein levels, actin reorganization, and decreased mesenchymal protein level. Furthermore, siCofilin-1/TGF-ß cells exhibited decreased migration and invasion rates as well as MMP-2 and -9 activity and augmented focal adhesion size. The expression of an inactive phospho-cofilin-1 mimetic (S3E) reduced E-cadherin and claudin-3 in cell-cell contacts, reduced their protein levels, and increased vimentin protein. Based on our findings, we suggest that cofilin-1 is crucial to switching from epithelial to mesenchymal-like morphology and cell migration and invasion by regulating actin cytoskeleton organization through activation of RhoA-LIMK2-cofilin-1 signaling, impacting the cell-cell adhesion organization of colon cancer cells in EMT.


Asunto(s)
Citoesqueleto de Actina/metabolismo , Cofilina 1/metabolismo , Neoplasias Colorrectales/metabolismo , Actinas/metabolismo , Antígenos CD/metabolismo , Cadherinas/metabolismo , Adhesión Celular/fisiología , Línea Celular Tumoral , Movimiento Celular/fisiología , Claudina-3/metabolismo , Neoplasias Colorrectales/patología , Citoesqueleto/metabolismo , Transición Epitelial-Mesenquimal/fisiología , Humanos , Quinasas Lim/metabolismo , Invasividad Neoplásica , Transducción de Señal , Factor de Crecimiento Transformador beta/metabolismo , Vimentina/metabolismo , Proteína de Unión al GTP rhoA/metabolismo
3.
Life Sci ; 188: 149-157, 2017 Nov 01.
Artículo en Inglés | MEDLINE | ID: mdl-28882647

RESUMEN

AIMS: Type 2 diabetes mellitus (T2DM) is one of the most prevalent diseases worldwide. Diabetic nephropathy (DN) is a complication of diabetes and the mechanisms underlying onset and progression of this disease are not fully understood. It has been shown that hyperglycemia is an independent factor to predict the development of DN in individuals with T2DM, however, a link between high plasma glucose levels and renal tubular injuries in DN remains unknown. In this study, we investigated the effect of high levels of glucose (i.e. 180 or 360mg/dL) for up to 24h (acute) or over 72h (chronic) upon tight junction (TJ)-mediated epithelial barrier integrity of the kidney tubular cell line, MDCK. METHODS/KEY FINDINGS: High levels of glucose (180 and 360mg/dL) induced a decrease in transepithelial electrical resistance associated with an increase in TJ cation selectivity at 24h or in TJ permeability to a paracellular marker, Lucifer Yellow, at 72h-exposure when compared to control group (exposed to 100mg/dL glucose). Immunofluorescence analyses showed that glucose treatment induced a significant decrease in the tight junctional content of claudins-1 and -3 as well as a significant increase in claudin-2 (particularly at 24h-exposure) and a time-dependent change in occludin/ZO-1 junctional content. The analyses of total cell content of these junctional proteins by Western blot did not reveal significant changes, except in claudin-2 expression. SIGNIFICANCE: Our data suggest that high levels of glucose induce time-dependence changes in TJ structure in MDCK monolayers, suggesting a possible link between hyperglycemia-induced tubular epithelial barrier disruption and diabetic nephropathy.


Asunto(s)
Células Epiteliales/efectos de los fármacos , Células Epiteliales/fisiología , Glucosa/efectos adversos , Túbulos Renales/citología , Uniones Estrechas/efectos de los fármacos , Uniones Estrechas/fisiología , Animales , Células Cultivadas , Claudina-1/metabolismo , Claudina-2/metabolismo , Claudina-3/metabolismo , Perros , Células de Riñón Canino Madin Darby , Potenciales de la Membrana/efectos de los fármacos , Potenciales de la Membrana/fisiología , Ocludina/metabolismo , Uniones Estrechas/metabolismo
4.
Anaerobe ; 39: 143-9, 2016 Jun.
Artículo en Inglés | MEDLINE | ID: mdl-27063897

RESUMEN

Clostridium perfringens type C strains produce severe disease in humans and animals including enterotoxaemia and hemorrhagic diarrhea. Type C disease is mediated by production of toxins that damage the site of infection inducing loss of bloody fluids. Production of type C toxins, such as CPA, PFO, and, CPB is regulated by the C. perfringens Agr-like (CpAL) quorum sensing (QS) system. The CpAL system is also required to recapitulate, in vivo, intestinal signs of C. perfringens type C-induced disease, including hemorrhagic diarrhea and accumulation of fluids. The intestinal epithelium forms a physical barrier, made up of a series of intercellular junctions including tight junctions (TJs), adherens junctions (AJs) and desmosomes (DMs). This selective barrier regulates important physiological processes, including paracellular movement of ions and solutes, which, if altered, results in loss of fluids into the intestinal lumen. In this work, the effects of C. perfringens infection on the barrier function of intestinal epithelial cells was evaluated by measuring trans-epithelial resistance (TEER). Our studies demonstrate that infection of human enterocytes with C. perfringens type C strain CN3685 induced a significant drop on TEER. Changes in TEER were mediated by the CpAL system as a CN3685ΔagrB mutant did not induce such a drop. Physical contact between bacteria and enterocytes produced more pronounced changes in TEER and this phenomenon appeared also to be mediated by the CpAL system. Finally, immunofluorescence studies demonstrate that C. perfringens type C infection redistribute TJs protein occludin, and Claudin-3, and DMs protein desmoglein-2, but did not affect the AJs protein E-cadherin.


Asunto(s)
Clostridium perfringens/metabolismo , Enterocitos/metabolismo , Regulación Bacteriana de la Expresión Génica , Interacciones Huésped-Patógeno , Percepción de Quorum , Uniones Estrechas/metabolismo , Animales , Proteínas Bacterianas , Células CACO-2 , Línea Celular Tumoral , Claudina-3/genética , Claudina-3/metabolismo , Clostridium perfringens/genética , Desmogleína 2/genética , Desmogleína 2/metabolismo , Impedancia Eléctrica , Enterocitos/microbiología , Técnica del Anticuerpo Fluorescente , Expresión Génica , Humanos , Ocludina/genética , Ocludina/metabolismo , Transporte de Proteínas , Uniones Estrechas/microbiología
5.
PLoS One ; 8(9): e74994, 2013.
Artículo en Inglés | MEDLINE | ID: mdl-24069372

RESUMEN

The altered expressions of claudin proteins have been reported during the tumorigenesis of colorectal cancer. However, the molecular mechanisms that regulate these events in this cancer type are poorly understood. Here, we report that epidermal growth factor (EGF) increases the expression of claudin-3 in human colorectal adenocarcinoma HT-29 cells. This increase was related to increased cell migration and the formation of anchorage-dependent and anchorage-independent colonies. We further showed that the ERK1/2 and PI3K-Akt pathways were involved in the regulation of these effects because specific pharmacological inhibition blocked these events. Genetic manipulation of claudin-1 and claudin-3 in HT-29 cells showed that the overexpression of claudin-1 resulted in decreased cell migration; however, migration was not altered in cells that overexpressed claudin-3. Furthermore, the overexpression of claudin-3, but not that of claudin-1, increased the tight junction-related paracellular flux of macromolecules. Additionally, an increased formation of anchorage-dependent and anchorage-independent colonies were observed in cells that overexpressed claudin-3, while no such changes were observed when claudin-1 was overexpressed. Finally, claudin-3 silencing alone despite induce increase proliferation, and the formation of anchoragedependent and -independent colonies, it was able to prevent the EGF-induced increased malignant potential. In conclusion, our results show a novel role for claudin-3 overexpression in promoting the malignant potential of colorectal cancer cells, which is potentially regulated by the EGF-activated ERK1/2 and PI3K-Akt pathways.


Asunto(s)
Claudina-3/genética , Neoplasias Colorrectales/genética , Expresión Génica , Línea Celular Tumoral , Movimiento Celular/efectos de los fármacos , Proliferación Celular/efectos de los fármacos , Transformación Celular Neoplásica/efectos de los fármacos , Transformación Celular Neoplásica/genética , Claudina-1/genética , Claudina-1/metabolismo , Claudina-3/metabolismo , Neoplasias Colorrectales/metabolismo , Factor de Crecimiento Epidérmico/farmacología , Receptores ErbB/metabolismo , Regulación Neoplásica de la Expresión Génica/efectos de los fármacos , Silenciador del Gen , Humanos , Proteína Quinasa 1 Activada por Mitógenos/metabolismo , Proteína Quinasa 3 Activada por Mitógenos/metabolismo , Fosfatidilinositol 3-Quinasas/metabolismo , Transporte de Proteínas/efectos de los fármacos , Proteínas Proto-Oncogénicas c-akt/metabolismo , Transducción de Señal/efectos de los fármacos , Ensayo de Tumor de Célula Madre
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