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1.
Eur Rev Med Pharmacol Sci ; 22(20): 6912-6921, 2018 10.
Artigo em Inglês | MEDLINE | ID: mdl-30402857

RESUMO

OBJECTIVE: This study aims to explore whether homeobox A11 antisense RNA (HOXA11-AS) could regulate inflammation induced by diabetic arteriosclerosis (DAA) via PI3K/AKT pathway. PATIENTS AND METHODS: Quantitative Real Time-Polymerase Chain Reaction (qRT-PCR) was used to detect expressions of HOXA11-AS and proinflammatory genes in carotid endarterectomy samples of symptomatic and asymptomatic atherosclerosis (AS) patients, diabetes mellitus (DM), and non-DM patients. The above-mentioned genes in DM animal model and non-DM animal model were also detected. We detected the expression of HOXA11-AS in vascular smooth muscle cells (VSMCs) treated with platelet-derived growth factor (PDGF) or PDGF inhibitor imatinib, respectively. Subsequently, we applied cell transfection technology to interfere with the expression of HOXA11-AS in VSMCs. In vascular endothelial cells (VECs) and VSMCs, we detected the effect of HOXA11-AS on the expressions of genes related to the proliferation, migration, and cell cycle. Then, VSMCs were treated with tumor necrosis factor-α (TNF-α), and the expression of HOXA11-AS was examined in VSMCs. The effect of HOXA11-AS on TNF-α-induced inflammation in VSMCs was detected as well. Finally, we analyzed the effect of HOXA11-AS on PDGF-induced activation of PI3K/AKT pathway in VSMCs and VECs. RESULTS: HOXA11-AS expression was markedly increased in carotid endarterectomy specimens of symptomatic AS patients compared to that of asymptomatic AS patients. Expression levels of HOXA11-AS and pro-inflammatory genes were significantly elevated in carotid endarterectomy specimens of DM patients. Similarly, HOXA11-AS expression was also significantly increased in carotid arteries of DM mice compared with that of non-DM mice. PDGF could upregulate HOXA11-AS expression in VSMCs, which was reversed by PDGF inhibitor imatinib. HOXA11-AS knockdown could reduce the expressions of the proliferation-associated gene (PCNA) and the cycle-related genes (p21, p53), and also inhibited the proliferation and migration of VSMCs induced by PDGF. HOXA11-AS was upregulated by TNF-α. HOXA11-AS knockdown remarkably downregulated expressions of inflammation-related genes in VSMCs induced by TNF-α. In VECs, low expression of HOXA11-AS can inhibit the expression of TNF-α-induced pro-inflammatory genes and PDGF-induced vascular inflammation-related genes. Low expression of HOXA11-AS inhibited PDGF-induced activation of PI3K/AKT pathway in VSMCs and VECs. CONCLUSIONS: HOXA11-AS may participate in DAA by activating the PI3K/AKT pathway to regulate inflammation in VSMCs and VECs.


Assuntos
Arteriosclerose/genética , Angiopatias Diabéticas/etiologia , Proteínas de Homeodomínio/genética , Animais , Ciclo Celular/genética , Proliferação de Células/genética , Células Cultivadas , Regulação para Baixo , Células Endoteliais/metabolismo , Humanos , Inflamação/metabolismo , Camundongos , Miócitos de Músculo Liso/metabolismo , Fosfatidilinositol 3-Quinases/metabolismo , Fator de Crescimento Derivado de Plaquetas/administração & dosagem , Proteínas Proto-Oncogênicas c-akt/metabolismo , Transdução de Sinais/genética , Regulação para Cima
2.
Histol Histopathol ; 11(1): 103-10, 1996 Jan.
Artigo em Inglês | MEDLINE | ID: mdl-8720453

RESUMO

Parenchymal and stromal components of the rat parotid and submandibular glands were examined by conventional and high resolution scanning electron microscopy (HRSEM). Freeze-fractured specimens were subjected to HCl and NaOH extraction procedures to better differentiate connective tissue and cellular components. In addition, the internal three-dimensional morphology of the secretory acinar cells and duct cells was revealed by maceration with a dilute osmium tetroxide solution to selectively remove some of the cytoplasmic components. SEM and HRSEM examination of the HCl-treated samples of both glands revealed a fine filamentous network immediately surrounding each acinus. Coarser bundles of collagen that linked neighboring acini were also observed. NaOH-extracted samples selectively removed the cellular components and showed more clearly the three-dimensional structure of the connective-tissue stroma. A dense-collagenous network surrounded each lobule while more internal regions consisted of a honeycomb-like pattern of evacuated spaces previously occupied by secretory acini. These spaces were smoothened in appearance and often interconnected. Apically-located secretory granules and profiles of the rough endoplasmic reticulum and Golgi apparatus in perinuclear regions were encountered in the acinar and duct cells of macerated samples by HRSEM. In addition, a phenylephrine-induced experimental condition performed in some rats resulted in a significant increase in secretory granule size and density of the serous cells.


Assuntos
Glândula Parótida/ultraestrutura , Ductos Salivares/ultraestrutura , Glândula Submandibular/ultraestrutura , Agonistas alfa-Adrenérgicos/farmacologia , Animais , Corantes , Técnica de Fratura por Congelamento , Masculino , Microscopia Eletrônica , Microscopia Eletrônica de Varredura , Glândula Parótida/citologia , Glândula Parótida/efeitos dos fármacos , Fenilefrina/farmacologia , Ratos , Ratos Sprague-Dawley , Ductos Salivares/citologia , Ductos Salivares/efeitos dos fármacos , Glândula Submandibular/citologia , Glândula Submandibular/efeitos dos fármacos , Inclusão do Tecido
3.
Histol Histopathol ; 10(3): 681-9, 1995 Jul.
Artigo em Inglês | MEDLINE | ID: mdl-7579818

RESUMO

The localization of Trimetaphosphatase (TMPase) activity during the acrosomal formation in the mouse testis was enzyme cytochemically investigated by the cerium-salt method. In addition to the lysosomes of the Sertoli cells and the spermatogenic cells in the seminiferous tubules, positive TMPase activity was detected in the Golgi complex and in the acrosomal vesicles of the spermatids, as well as in the acrosomes of both spermatids and spermatozoa. In the Golgi complex of the spermatids, TMPase activity was observed in the first one or two lamellae of the trans-face and in the small vesicles in the vicinity of the Golgi complex. TMPase positive reaction was also detected in the acrosomes of the spermatozoa in the lumina of both the seminiferous tubules and the epididymal duct. The localization of this enzyme activity was compared with that of acid phosphatase (ACPase), as detected by the cerium-based method, using beta-glycerophosphate as substrate: ACPase activity was completely absent from the Golgi complex, small vesicles, acrosomal vesicle and acrosome throughout the entire process of acrosomal formation. TMPase is thought to become one of the acrosomal components, and may be involved in the acrosomal reaction during fertilization.


Assuntos
Hidrolases Anidrido Ácido/metabolismo , Acrossomo/enzimologia , Acrossomo/ultraestrutura , Testículo/enzimologia , Testículo/ultraestrutura , Fosfatase Ácida/metabolismo , Animais , Histocitoquímica , Lisossomos/enzimologia , Lisossomos/ultraestrutura , Masculino , Camundongos , Camundongos Endogâmicos , Túbulos Seminíferos/enzimologia , Túbulos Seminíferos/ultraestrutura , Células de Sertoli/enzimologia , Células de Sertoli/ultraestrutura , Espermatogênese/fisiologia , Espermatozoides/enzimologia , Espermatozoides/ultraestrutura
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