Prescribing Ceftolozane/Tazobactam for Pediatric Patients: Current Status and Future Implications.

Antibiotics are arguably the greatest medical development of the 20th century but these precious resources are being threatened by the continued rise in infections caused by multidrug-resistant bacteria. There is concern that we are on the precipice of a 'post-antibiotic era'. The situation is exacerbated by a stagnation in the pharmaceutical industry in developing new antibiotics, particularly those with activity against some of the most resistant Gram-negative organisms because of significant economic, scientific, and regulatory barriers.

Influence of polyunsaturated fatty acids on urologic inflammation.

Purpose: Studies demonstrate that polyunsaturated fatty acids, fish oils, and alpha-linoleic acid are beneficial anti-inflammatory agents, which suppress inflammatory mediators and their activity.

Methods: This review focuses on the effects of omega-3 fatty acids (O-3FAs) on three primary urologic organs (bladder, kidney, and prostate) and associated conditions such as urolithiasis, kidney transplantation, interstitial cystitis/bladder pain syndrome, bladder cancer, prostate cancer (CaP), and chronic prostatitis/chronic pelvic pain syndrome.

Results: The following themes emerged: the potential influence of O-3FA in suppressing urologic inflammation; the supportive role of O-3FA in therapeutic interventions; pro-inflammatory mechanisms of omega-6 fatty acids (O-6FAs) associated with disease progression; and the importance of the optimal ratio of O-6FAs/O-3FAs.

p38 MAPK plays a role in IL-4 synthesis in jacalin plus CD28-stimulated CD4+ T cells--II.

We have previously shown that jacalin, a CD4+ T cell lectin, induces phosphorylation of intracellular events, moderate levels of interleukin (IL)-2 secretion. We have also shown that in the presence of CD28 costimulation, jacalin induces IL-4 secretion. In the present study, we showed that stimulation of normal CD4+ T cells with jacalin plus CD28 cross-linking (CD28XL) resulted in phosphorylation of signal transducer and activator of transcription (STAT)-6 and expression of Bcl-2 and Bcl-xL, which were inhibited significantly when cells were cultured in the presence of the p38 mitogen-activated protein kinase (MAPK) inhibitor SB203580.

The lectin jacalin plus costimulation with anti-CD28 antibody induces phosphorylation of p38 MAPK and IL-4 synthesis-I.

Costimulatory signals play an important role in the development of T helper cell type 1 (Th1) or Th2 type. Little is known about jacalin plus CD28-mediated signaling and cytokine secretion. In the present study, we analyzed the intracellular signaling events following stimulation of CD4+ T cells with jacalin plus CD28 cross-linking (CD28XL) with anti-CD28 antibody.

IgD-receptor (IgD-R) cross-linking partially protects murine T cells from dexamethasone-induced apoptosis.

Based on our previous findings that immunoglobulin D (IgD) receptor (IgD-R) cross-linking with oligomeric IgD (IgD-R-xL) led to T cell activation, we examined the effect of IgD-R-xL on the expression of Fas antigen and apoptosis induction. In splenic T cells, IgD-R-xL followed by dexamethasone (dex) treatment resulted in a decreased percentage of Fas-positive cells as well as a decreased mean fluorescence intensity (P<0.05) when compared with cells treated with dex alone.

The lectin jacalin induces phosphorylation of ERK and JNK in CD4+ T cells.

The CD4 molecule plays an essential role in mediating the transduction of intracellular signals by functioning as a coreceptor for the complex T cell receptor/CD3 and also acts as the primary receptor for human immunodeficiency virus (HIV). Several authors have shown evidence that jacalin, a plant lectin, binds to CD4 and inhibits in vitro HIV infection. We analyzed jacalin-induced intracellular signaling events in CD4(+) T cells and have shown that cell activation resulted in tyrosine phosphorylation of intracellular substrates p56(lck), p59(fyn), ZAP-70, p95 (vav), phospholipase C-gamma1, and ras activation, as assessed by conversion of ras guanosine 5'-diphosphate to ras guanosine 5'-triphosphate.