scholarly journals Studies on the nephrotoxicity of aminoglycoside antibiotics and protection from these effects. (4) Effects of tobramycin alone and in combination with latamoxef on the stability of rat kidney lysosomal membranes.

1987 ◽  
Vol 43 (1) ◽  
pp. 73-80 ◽  
Author(s):  
Ryoji KOJIMA ◽  
Mikio ITO ◽  
Yoshio SUZUKI
Keyword(s):  
Rat Kidney ◽  
Aminoglycoside Antibiotics ◽  
Lysosomal Membranes ◽  
The Stability

scholarly journals Room-temperature stable loop-mediated isothermal amplification (LAMP) reagents to detect leptospiral DNA

2021 ◽  
Vol 15 (4) ◽  
pp. 183-189
Author(s):  
Pui-Yuei Lee ◽  
Yien-Ping Wong ◽  
Shuhaidah Othman ◽  
Hui-Yee Chee
Keyword(s):  
Dna Polymerase ◽  
Cold Storage ◽  
Room Temperature ◽  
Rat Kidney ◽  
Isothermal Amplification ◽  
Storage Requirement ◽  
Loop Mediated Isothermal Amplification ◽  
Modified Method ◽  
Resource Limited ◽  
The Stability

Abstract Background Loop-mediated isothermal amplification (LAMP) is one of the most promising tools for rapidly detecting Leptospira spp. However, LAMP is hampered by cold storage to maintain the enzymatic activity of Bst DNA polymerase. Objective To overcome the drawback of cold storage requirement for LAMP reagents we modified the reagents by adding sucrose as stabilizer. We then sought to determine the stability at room temperature of the premixed LAMP reagents containing sucrose. Method Premixed LAMP reagents with sucrose and without sucrose were prepared. The prepared mixtures were stored at room temperature for up to 60 days, and were subjected to LAMP reactions at various intervals using rat kidney samples to detect leptospiral DNA. Results The premixed LAMP reagents with sucrose remained stable for 45 days while sucrose-free premixed LAMP reagents showed no amplification from day 1 of storage at room temperature up to day 14. Conclusion The LAMP reagent system can be refined by using sucrose as stabilizer, thus allowing their storage at room temperature without the need for cold storage. The modified method enables greater feasibility of LAMP for field surveillance and epidemiology in resource-limited settings.

Adenovirus serotype determines association and localization of the large E1B tumor antigen with cellular tumor antigen p53 in transformed cells

1985 ◽  
Vol 5 (11) ◽  
pp. 3084-3091 ◽  
Author(s):  
A Zantema ◽  
P I Schrier ◽  
A Davis-Olivier ◽  
T van Laar ◽  
R T Vaessen ◽  
...  
Keyword(s):  
Tumor Antigen ◽  
Rat Kidney ◽  
T Antigen ◽  
Transformed Cells ◽  
Kidney Cells ◽  
Primary Cells ◽  
Large T Antigen ◽  
Morphological Transformation ◽  
Cytoplasmic Body ◽  
The Stability

The distribution and stability of the cellular tumor antigen p53 were studied in baby rat kidney cells transformed by region E1 sequences of nononcogenic adenovirus (Ad) type 5 (Ad5) or oncogenic type 12 (Ad12). In transformed cells expressing the large E1B T antigen of Ad5, p53 was associated with this T antigen. The complexed proteins were concentrated in a cytoplasmic body, which has been shown to consist of a cluster of 8-nm filaments (A. Zantema et al., Virology 142:44-58, 1985). In transformed cells expressing the E1B region of Ad12, however, no association between the viral large T antigen and p53 was detectable. In the latter case, both proteins were found almost exclusively in the nucleus. The stability of p53 in both Ad5- and Ad12-transformed cells was increased relative to that in primary cells or cells immortalized by the E1A region only. Thus, the increased stability of p53 in Ad-transformed cells is not caused by association with a viral T antigen, but it correlates with expression of E1B and with morphological transformation.

Effect of Acute Experimental Uremia on the Stability of Liver Lysosomal Membranes

Nephron ◽  
1977 ◽  
Vol 18 (2) ◽  
pp. 88-92 ◽  
Author(s):  
Luiz Erlon A. Rodrigues ◽  
Reinaldo P. Martinelli ◽  
Ivone Cruz ◽  
Heonir Rocha
Keyword(s):  
Lysosomal Membranes ◽  
The Stability

scholarly journals Effects of aminoglycoside antibiotics on lysosomal enzymes of rat kidney.

1983 ◽  
Vol 31 (9) ◽  
pp. 3277-3283 ◽  
Author(s):  
YUKIHIKO ARAMAKI ◽  
ASAICHI INABA ◽  
JUNJI NIIBUCHI ◽  
SEISHI TSUCHIYA
Keyword(s):  
Lysosomal Enzymes ◽  
Rat Kidney ◽  
Aminoglycoside Antibiotics

scholarly journals Adenovirus serotype determines association and localization of the large E1B tumor antigen with cellular tumor antigen p53 in transformed cells.

1985 ◽  
Vol 5 (11) ◽  
pp. 3084-3091 ◽  
Author(s):  
A Zantema ◽  
P I Schrier ◽  
A Davis-Olivier ◽  
T van Laar ◽  
R T Vaessen ◽  
...  
Keyword(s):  
Tumor Antigen ◽  
Rat Kidney ◽  
T Antigen ◽  
Transformed Cells ◽  
Kidney Cells ◽  
Primary Cells ◽  
Large T Antigen ◽  
Morphological Transformation ◽  
Cytoplasmic Body ◽  
The Stability

The distribution and stability of the cellular tumor antigen p53 were studied in baby rat kidney cells transformed by region E1 sequences of nononcogenic adenovirus (Ad) type 5 (Ad5) or oncogenic type 12 (Ad12). In transformed cells expressing the large E1B T antigen of Ad5, p53 was associated with this T antigen. The complexed proteins were concentrated in a cytoplasmic body, which has been shown to consist of a cluster of 8-nm filaments (A. Zantema et al., Virology 142:44-58, 1985). In transformed cells expressing the E1B region of Ad12, however, no association between the viral large T antigen and p53 was detectable. In the latter case, both proteins were found almost exclusively in the nucleus. The stability of p53 in both Ad5- and Ad12-transformed cells was increased relative to that in primary cells or cells immortalized by the E1A region only. Thus, the increased stability of p53 in Ad-transformed cells is not caused by association with a viral T antigen, but it correlates with expression of E1B and with morphological transformation.

The effect of gentamycin and cefuroxime on the stability of rat kidney lysosomes in vivo

1982 ◽  
Vol 10 (6) ◽  
pp. 515-516 ◽  
Author(s):  
IAN G. COWELL ◽  
SAID NOORAZAR ◽  
DAVID T. PLUMMER
Keyword(s):  
Rat Kidney ◽  
The Stability

scholarly journals MAL/VIP17, a New Player in the Regulation of NKCC2 in the Kidney

2010 ◽  
Vol 21 (22) ◽  
pp. 3985-3997 ◽  
Author(s):  
Monica Carmosino ◽  
Federica Rizzo ◽  
Giuseppe Procino ◽  
Davide Basco ◽  
Giovanna Valenti ◽  
...  
Keyword(s):  
Apical Membrane ◽  
Rat Kidney ◽  
Surface Expression ◽  
Salt Transport ◽  
Thick Ascending Limb ◽  
Transport Pathway ◽  
Amino Acid Stretch ◽  
The Stability ◽  
Apical Sorting

The renal-specific Na+-K+-2Cl− cotransporter (NKCC2) is the major salt transport pathway of the apical membrane of the mammalian thick ascending limb of Henle's loop. Here, we analyze the role of the tetraspan protein myelin and lymphocytes-associated protein (MAL)/VIP17 in the regulation of NKCC2. We demonstrated that 1) NKCC2 and MAL/VIP17 colocalize and coimmunoprecipitate in Lilly Laboratories cell porcine kidney cells (LLC-PK1) as well as in rat kidney medullae, 2) a 150-amino acid stretch of NKCC2 C-terminal tail is involved in the interaction with MAL/VIP17, 3) MAL/VIP17 increases the cell surface retention of NKCC2 by attenuating its internalization, and 4) this coincides with an increase in cotransporter phosphorylation. Interestingly, overexpression of MAL/VIP17 in the kidney of transgenic mice results in cysts formation in distal nephron structures consistent with the hypothesis that MAL/VIP17 plays an important role in apical sorting or in maintaining the stability of the apical membrane. The NKCC2 expressed in these mice was highly glycosylated and phosphorylated, suggesting that MAL/VIP17 also is involved in the stabilization of NKCC2 at the apical membrane in vivo. Thus, the involvement of MAL/VIP17 in the activation and surface expression of NKCC2 could play an important role in the regulated absorption of Na+ and Cl− in the kidney.

Sign in / Sign up

Export Citation Format

Share Document