Incorporation of tyrosine phosphate into tetraphenylethylene affords an amphiphilic molecule for alkaline phosphatase detection, hydrogelation and calcium mineralization

Huan Liu; Zhonglin Lv; Kaiguo Ding; Xiaoli Liu; Lin Yuan; Hong Chen; Xinming Li

doi:10.1039/c3tb21024c

Incorporation of tyrosine phosphate into tetraphenylethylene affords an amphiphilic molecule for alkaline phosphatase detection, hydrogelation and calcium mineralization

Journal of Materials Chemistry B ◽

10.1039/c3tb21024c ◽

2013 ◽

Vol 1 (41) ◽

pp. 5550 ◽

Cited By ~ 36

Author(s):

Huan Liu ◽

Zhonglin Lv ◽

Kaiguo Ding ◽

Xiaoli Liu ◽

Lin Yuan ◽

...

Keyword(s):

Alkaline Phosphatase ◽

Tyrosine Phosphate

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Interrelationship of the cellular distribution and secretion of regular structure (RS) protein in Bacillus licheniformis nm 105

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100123969 ◽

1992 ◽

Vol 50 (1) ◽

pp. 712-713

Author(s):

Xiaorong Zhu ◽

Richard McVeigh ◽

Bijan K. Ghosh

Keyword(s):

Alkaline Phosphatase ◽

Bacillus Licheniformis ◽

Self Assembly ◽

Gel Electrophoresis ◽

Culture Supernatant ◽

Regular Structure ◽

The Self ◽

Cellular Distribution ◽

Structural Protein ◽

Laboratory Cultures

A mutant of Bacillus licheniformis 749/C, NM 105 exhibits some notable properties, e.g., arrest of alkaline phosphatase secretion and overexpression and hypersecretion of RS protein. Although RS is known to be widely distributed in many microbes, it is rarely found, with a few exceptions, in laboratory cultures of microorganisms. RS protein is a structural protein and has the unusual properties to form aggregate. This characteristic may have been responsible for the self assembly of RS into regular tetragonal structures. Another uncommon characteristic of RS is that enhanced synthesis and secretion which occurs when the cells cease to grow. Assembled RS protein with a tetragonal structure is not seen inside cells at any stage of cell growth including cells in the stationary phase of growth. Gel electrophoresis of the culture supernatant shows a very large amount of RS protein in the stationary culture of the B. licheniformis. It seems, Therefore, that the RS protein is cotranslationally secreted and self assembled on the envelope surface.

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In Situ Localization of PPAR Gamma and Uncoupling Protein in Mouse Embryo Sections Using Digoxigenin-Labeled Riboprobes

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100162624 ◽

1996 ◽

Vol 54 ◽

pp. 32-33

Author(s):

C. Jennermann ◽

S. A. Kliewer ◽

D. C. Morris

Keyword(s):

Alkaline Phosphatase ◽

Room Temperature ◽

Uncoupling Protein ◽

Ppar Gamma ◽

Nuclear Hormone Receptor ◽

Full Length ◽

Northern Analysis ◽

Peroxisome Proliferator

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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