PubMed Health⌕ Search

PubMed · 10932926

[Nephrolithiasis].

Abstract

The development of efficacious techniques for stone elimination, and in particular of extracorporeal lithotripsy, slackened, in the last two decades, the pharmacological research on nephrolithiasis, with the result that the currently available efficacious drugs are very few. Instead, the recent elucidation of some relevant etiopathogenetic aspects, with special reference to the quantitative and qualitative changes of specific urinary inhibitors of crystallization, could open new therapeutic avenues for many lithiasic forms, now considered idiopathic.

Explore related subjects

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

L Saso, B Silvestrini. [Nephrolithiasis].. https://pubmed.ncbi.nlm.nih.gov/10932926/

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

Solubilization limit of lysozyme into DODMAC reverse micelles.

Dioctyldimethyl ammonium chloride (DODMAC) was used to form reverse micelles and to extract lysozyme from an aqueous solution into an organic phase. The solubilization behavior of lysozyme into a DODMAC reverse micellar phase was examined in terms of the temperature, the type of cations in the aqueous phase, and the surfactant concentration in the organic phase. Complete removal of lysozyme from the aqueous phase was obtained when the pH was set one unit higher than the pI of the protein. However, it was found that there is a solubilization limit of lysozyme in the organic phase. Not all the lysozyme extracted out of the initial aqueous phase was solubilized into the DODMAC reverse micellar phase, resulting in the formation of white precipitate at the aqueous-organic interface. Temperature has a negligible effect on the solubilization limit of lysozyme. The value of the solubilization limit is a strong function of the type of cations present in the aqueous phase, indicating an important role of lysozyme-cation interactions on the extraction process. An increase in the DODMAC concentration from 100-200 mM resulted in little change in the highest concentration of lysozyme obtained in the organic phase.

Calcium↗

Engagement of the inhibitory receptor CD158a interrupts TCR signaling, preventing dynamic membrane reorganization in CTL/tumor cell interaction.

Renal cell carcinoma (RCC) infiltrating lymphocytes (TILs) express killer cell immunoglobulinlike receptors (KIRs) that inhibit the antitumor CD8(+) T-cell lysis. In the present study, to better examine the functional consequences of KIR engagement on cytotoxic T lymphocyte (CTL)/tumor interaction, we have investigated the influence of KIR CD158a on early steps of T-cell activation. We show that coengagement of T-cell receptor (TCR) and CD158a by tumor cells inhibited tyrosine phosphorylation of early signaling proteins ZAP-70 and LAT, lipid raft coalescence, and TCR/CD3 accumulation at the CTL/tumor cell interface. In addition, the guanine exchange factor Vav was not phosphorylated, and no actin cytoskeleton rearrangement was observed. Our data indicate a role of KIR CD158a in the dynamic events induced by TCR triggering, preventing CTL membrane reorganization, and subsequent completion of CTL activation program. Accordingly, the expression of CD158 by TILs may favor tumor cell escape to the immune response.

Calcium↗

A novel regulatory mechanism of the mitochondrial Ca2+ uniporter revealed by the p38 mitogen-activated protein kinase inhibitor SB202190.

It is widely acknowledged that mitochondrial Ca2+ uptake modulates the cytosolic [Ca2+] ([Ca2+]c) acting as a transient Ca2+ buffer. In addition, mitochondrial [Ca2+] ([Ca2+]M) regulates the rate of respiration and may trigger opening of the permeability transition pore and start apoptosis. However, no mechanism for the physiological regulation of mitochondrial Ca2+ uptake has been described. We show here that SB202190, an inhibitor of p38 mitogen-activated protein (MAP) kinase, strongly stimulates ruthenium red-sensitive mitochondrial Ca2+ uptake, both in intact and in permeabilized HeLa cells. The [Ca2+]M peak induced by agonists was increased about fourfold in the presence of the inhibitor, with a concomitant reduction in the [Ca2+]c peak. The stimulation occurred fast and was rapidly reversible. In addition, experiments in permeabilized cells perfused with controlled [Ca2+] showed that SB202190 stimulated mitochondrial Ca2+ uptake by more than 10-fold, but only in the physiological [Ca2+]c range (1-4 mM). Other structurally related p38 MAP kinase inhibitors (SB203580, PD169316, or SB220025) produced little or no effect. Our data suggest that in HeLa cells, a protein kinase sensitive to SB202190 tonically inhibits the mitochondrial Ca2+ uniporter. This novel regulatory mechanism may be of paramount importance to modulate mitochondrial Ca2+ uptake under different physiopathological conditions.

Calcium↗