Na+-dependent, active nucleoside transport in mouse spleen lymphocytes, leukemia cells, fibroblasts and macrophages, but not in equivalent human or pig cells; dipyridamole enhances nucleoside salvage by cells with both active and facilitated transport

1990 ◽  
Vol 1025 (1) ◽  
pp. 32-42 ◽  
Author(s):  
Peter G.W. Plagemann ◽  
Josep M. Aran
Keyword(s):  
Facilitated Transport ◽  
Nucleoside Transport ◽  
Leukemia Cells ◽  
Mouse Spleen ◽  
Nucleoside Salvage ◽  
Spleen Lymphocytes

Heterogeneous uptake of 9-β-D-arabinofuranosyladenine by mouse spleen lymphocytes

1985 ◽  
Vol 63 (9) ◽  
pp. 1175-1181
Author(s):  
Anthony F. Almeida
Keyword(s):  
Nucleoside Transport ◽  
Mouse Spleen ◽  
Uptake Capacity ◽  
Simple Diffusion ◽  
Spleen Lymphocytes ◽  
Dose Dependent ◽  
Mouse Lymphocytes

Spleens of mice treated with 9-β-D-[2,8-3H]arabinofuranosyladenine (araA), 0.5–30.0 mg/kg showed rapid dose-dependent accumulation of 3H, which peaked at 2.5 mg/kg. Lymphocytes from spleens showed linear uptake when incubated with 0.68, 1.36, and 5.03 μM araA over 120 s. With 1.0 mM araA, uptake was reduced in rate but was not saturated. Tritiated metabolites identified from these lymphocytes were araA which predominated after brief incubations, its deaminated form (araH), and some phosphorylated product in small amount. Inhibition of deaminase increased intracellular araA. Although potent inhibitors of nucleoside transport inhibited araA uptake marginally, adenosine competed with araA for about 50% of the uptake capacity. The data suggest that the uptake of araA by mouse lymphocytes, which is not simple diffusion, occurs by a mechanism distinct from typical nucleoside transport.

UVC-induced damage in mouse spleen lymphocytes and anti-radiation effect of exogenous nucleotides

2014 ◽  
Author(s):  
Cuilin Cheng ◽  
Zhenyu Wang ◽  
Haitian Zhao ◽  
Aiju Hou ◽  
Rongchun Wang ◽  
...  
Keyword(s):  
Radiation Effect ◽  
Mouse Spleen ◽  
Spleen Lymphocytes

Density Gradient Electrophoresis of Mouse Spleen Lymphocytes

1980 ◽  
Vol 63 (3) ◽  
pp. 258-265 ◽  
Author(s):  
C.D. Platsoucas ◽  
S.G. Robbins ◽  
N. Catsimpoolas
Keyword(s):  
Density Gradient ◽  
Mouse Spleen ◽  
Gradient Electrophoresis ◽  
Spleen Lymphocytes

Inhibition of proliferative responses of mouse spleen lymphocytes and rabbit Peyer's patch cells by bovine milk caseins and their digests

1995 ◽  
Vol 62 (2) ◽  
pp. 339-348 ◽  
Author(s):  
Hajime Otani ◽  
Isao Hata
Keyword(s):  
Colorimetric Assay ◽  
Bovine Milk ◽  
Inhibitory Effect ◽  
Mouse Spleen ◽  
Pokeweed Mitogen ◽  
Peyer’S Patch ◽  
Peyer's Patch ◽  
Diphenyltetrazolium Bromide ◽  
Spleen Lymphocytes ◽  
Milk Casein

SUMMARYThe modulating effect of bovine milk casein components and their digests on the proliferative responses of mouse spleen lymphocytes and rabbit Peyer's patch cells induced or not induced by mitogens has been studied with a colorimetric assay using 3-(4, 5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide. All the casein components and their digests tested had little mitogenic effect on the proliferative responses of mouse spleen lymphocytes and rabbit Peyer's patch cells. Intact κ-casein significantly inhibited the proliferative responses of mouse spleen lymphocytes and Peyer's patch cells induced by mitogens such as lipopolysaccharide fromSalmonella typhimurium, concanavalin A, phytohaemagglutinin and pokeweed mitogen. In contrast, intact αsl-casein and β-casein had little effect. κ-Casein had an inhibitory effect after digesti on by pancreatin or trypsin, but not after pepsin or chymotrypsin digestion. Both pancreatin and trypsin digests of αsl-casein and -casein significantly inhibited the proliferative responses of mouse spleen lymphocytes and rabbit Peyer's patch cells induced by mitogens, whereas pepsin and chymotrypsin digests of both caseins were without effect. Moreover, the trypsin digest of each casein component had an inhibitory effect on mouse spleen lymphocyte proliferation in the absence of mitogen. Since trypsin is a major proteinase in pancreatin, the substrate specificity of trypsin seems to be important for the formation of the inhibitory peptides from casein components. These observations suggest that intact κ-casein and some peptides formed from milk casein components by the action of trypsin may suppress the immune responsiveness of neonates.

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