Comment on “Aloe-emodin induces in vitro G2/M arrest and alkaline phosphatase activation in human oral cancer KB cells” [Xiao B, Guo J, Liu D, Zhang S. Oral Oncol 2007;43(9):905–10]

Peroxisome proliferator-activated receptor gamma (PPARg) is a member of the nuclear hormone receptor superfamily and has been shown in vitro to regulate genes involved in lipid metabolism and adipocyte differentiation. By Northern analysis, we and other researchers have shown that expression of this receptor predominates in adipose tissue in adult mice, and appears first in whole-embryo mRNA at 13.5 days postconception. In situ hybridization was used to find out in which developing tissues PPARg is specifically expressed.Digoxigenin-labeled riboprobes were generated using the Genius™ 4 RNA Labeling Kit from Boehringer Mannheim. Full length PPAR gamma, obtained by PCR from mouse liver cDNA, was inserted into pBluescript SK and used as template for the transcription reaction. Probes of average size 200 base pairs were made by partial alkaline hydrolysis of the full length transcripts. The in situ hybridization assays were performed as described previously with some modifications. Frozen sections (10 μm thick) of day 18 mouse embryos were cut, fixed with 4% paraformaldehyde and acetylated with 0.25% acetic anhydride in 1.0M triethanolamine buffer. The sections were incubated for 2 hours at room temperature in pre-hybridization buffer, and were then hybridized with a probe concentration of 200μg per ml at 70° C, overnight in a humidified chamber. Following stringent washes in SSC buffers, the immunological detection steps were performed at room temperature. The alkaline phosphatase labeled, anti-digoxigenin antibody and detection buffers were purchased from Boehringer Mannheim. The sections were treated with a blocking buffer for one hour and incubated with antibody solution at a 1:5000 dilution for 2 hours, both at room temperature. Colored precipitate was formed by exposure to the alkaline phosphatase substrate nitrobluetetrazoliumchloride/ bromo-chloroindlylphosphate.

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Electron microscopic study of the membrane glycoproteins in the rat kidney after cisplatin treatment

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100156547 ◽

1989 ◽

Vol 47 ◽

pp. 912-913

Author(s):

S.K. Aggarwal

Keyword(s):

Alkaline Phosphatase ◽

Rat Kidney ◽

Light And Electron Microscopy ◽

Kidney Tissue ◽

Membrane Glycoproteins ◽

Electron Microscopic ◽

Before And After ◽

Interstrand Cross Links ◽

Cross Links

The proposed primary mechanism of action of the anticancer drug cisplatin (Cis-DDP) is through its interaction with DNA, mostly through DNA intrastrand cross-links or DNA interstrand cross-links. DNA repair mechanisms can circumvent this arrest thus permitting replication and transcription to proceed. Various membrane transport enzymes have also been demonstrated to be effected by cisplatin. Glycoprotein alkaline phosphatase was looked at in the proximal tubule cells before and after cisplatin both in vivo and in vitro for its inactivation or its removal from the membrane using light and electron microscopy.Outbred male Swiss Webster (Crl: (WI) BR) rats weighing 150-250g were given ip injections of cisplatin (7mg/kg). Animals were killed on day 3 and day 5. Thick slices (20-50.um) of kidney tissue from treated and untreated animals were fixed in 1% buffered glutaraldehyde and 1% formaldehyde (0.05 M cacodylate buffer, pH 7.3) for 30 min at 4°C. Alkaline phosphatase activity and carbohydrates were demonstrated according to methods described earlier.

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Proanthocyanidin-enriched extract of Rumex acetosa L. inhibits the in vitro adhesion of Porphyromonas gingivalis to KB cells and decreases the biofilm formation

Planta Medica ◽

10.1055/s-0033-1352245 ◽

2013 ◽

Vol 79 (13) ◽

Author(s):

JM Schmuch ◽

K Köller ◽

S Beckert ◽

A Podbielski ◽

A Hensel

Keyword(s):

Porphyromonas Gingivalis ◽

Biofilm Formation ◽

Kb Cells ◽

Rumex Acetosa ◽

In Vitro Adhesion

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Tissue non-specific alkaline phosphatase activity and mineralization capacity of bi-allelic mutations from severe perinatal and asymptomatic hypophosphatasia phenotypes: Results from an in-vitro mutagenesis model

Bone Abstracts ◽

10.1530/boneabs.7.p62 ◽

2019 ◽

Author(s):

Suma Uday ◽

Tomohiro Matsumara ◽

Vrinda Saraff ◽

Shiho Saito ◽

Hideo Orimo ◽

...

Keyword(s):

Alkaline Phosphatase ◽

Phosphatase Activity ◽

Alkaline Phosphatase Activity ◽

In Vitro Mutagenesis ◽

Specific Alkaline Phosphatase

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Alkaline phosphatase in osteoblasts and fibroblasts cultivated in vitro

Experimental Cell Research ◽

10.1016/0014-4827(56)90196-3 ◽

1956 ◽

Vol 11 (1) ◽

pp. 115-127 ◽

Cited By ~ 17

Author(s):

E. Henrichsen

Keyword(s):

Alkaline Phosphatase

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Downregulation of ceramide synthase 1 promotes oral cancer through endoplasmic reticulum stress

International Journal of Oral Science ◽

10.1038/s41368-021-00118-4 ◽

2021 ◽

Vol 13 (1) ◽

Author(s):

Wen Chen ◽

Chenzhou Wu ◽

Yafei Chen ◽

Yuhao Guo ◽

Ling Qiu ◽

...

Keyword(s):

Squamous Cell Carcinoma ◽

Endoplasmic Reticulum ◽

Oral Cancer ◽

Oral Squamous Cell Carcinoma ◽

Endoplasmic Reticulum Stress ◽

Cell Carcinoma ◽

Squamous Cell ◽

Migration And Invasion ◽

Ceramide Synthase

AbstractC18 ceramide plays an important role in the occurrence and development of oral squamous cell carcinoma. However, the function of ceramide synthase 1, a key enzyme in C18 ceramide synthesis, in oral squamous cell carcinoma is still unclear. The aim of our study was to investigate the relationship between ceramide synthase 1 and oral cancer. In this study, we found that the expression of ceramide synthase 1 was downregulated in oral cancer tissues and cell lines. In a mouse oral squamous cell carcinoma model induced by 4-nitroquinolin-1-oxide, ceramide synthase 1 knockout was associated with the severity of oral malignant transformation. Immunohistochemical studies showed significant upregulation of PCNA, MMP2, MMP9, and BCL2 expression and downregulation of BAX expression in the pathological hyperplastic area. In addition, ceramide synthase 1 knockdown promoted cell proliferation, migration, and invasion in vitro. Overexpression of CERS1 obtained the opposite effect. Ceramide synthase 1 knockdown caused endoplasmic reticulum stress and induced the VEGFA upregulation. Activating transcription factor 4 is responsible for ceramide synthase 1 knockdown caused VEGFA transcriptional upregulation. In addition, mild endoplasmic reticulum stress caused by ceramide synthase 1 knockdown could induce cisplatin resistance. Taken together, our study suggests that ceramide synthase 1 is downregulated in oral cancer and promotes the aggressiveness of oral squamous cell carcinoma and chemotherapeutic drug resistance.

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