The New Classes of Synthetic Illicit Drugs Can Significantly Harm the Brain: A Neuro Imaging Perspective with Full Review of MRI Findings.

Synthetic drugs contain substances that are pharmacologically similar to those found in traditional illicit drugs. Some of the most commonly abused synthetic drugs include synthetic marijuana, bath salts, ecstasy, N-bomb, methamphetamine and anabolic steroids. Many of them share the same chemical properties and physiologic responses with the drugs they mimic and may exaggerate the pathologic response in the brain leading to addiction. These drugs have detrimental (and often irreversible) effects on the brain and primarily affect the central nervous system by two mechanisms: 1) Neural hyper stimulation via increasing activation of certain neurotransmitters (norepinephrine, dopamine, and serotonin), 2) Cause significant reduction in CNS neural connectivity affecting various brain regions such as the basal ganglia, hippocampus, cerebellum, parietal lobe, and globus pallidus. Furthermore these drugs sometimes have severe, life-threatening adverse effects on the human body. A few structural MRI studies have been conducted in synthetic drug abusers to reveal the effects of these drugs on the brain parenchyma. This review article will describe the potential brain imaging findings in synthetic drug abusers as demonstrated by several case reports and the primary literature.

Interpretive criteria for mupirocin susceptibility testing of Staphylococcus spp. using CLSI guidelines.

Mupirocin is an antimicrobial agent commonly used to treat staphylococcal infection or to eliminate persistent carriage. To date, interpretive criteria have not been established to define susceptibility or resistance when performing mupirocin susceptibility testing. In this evaluation, using CLSI guidelines, a total of 502 staphylococci comprising 219 methicillin-sensitive Staphylococcus aureus, 222 methicillin-resistant S. aureus and 61 coagulase-negative staphylococci are tested by broth microdilution, disc diffusion and E-test. Disc diffusion using 5 microg mupirocin discs was found to be a reliable method to distinguish susceptible and resistant strains. Minimum inhibitory concentration (MIC) determination was required to differentiate low-level and high-level resistance to mupirocin. E-test was found to be an accurate alternative to broth microdilution for the routine determination of MIC values of staphylococci to mupirocin. Broth microdilution and disc-diffusion results were plotted on a scattergram, and error rates were calculated. No errors were found using susceptibility criteria of < 4 microg/mL (MIC) and > 19 mm (zone diameter).

Multiple protein kinase activities required for activation of sperm flagellar motility.

A specific peptide inhibitor of the cyclic AMP (cAMP)-dependent protein kinase (PKI-peptide) is a very effective inhibitor of the cAMP-dependent activation of motility of Ciona spermatozoa, when PKI-peptide is present at the beginning of incubation of demembranated spermatozoa with cAMP and ATP. Under conditions where approximately 120 sec is required for full activation of motility, the window of sensitivity to the PKI-peptide lasts for only 25-30 sec. Examination of sperm pellet proteins labeled with 32P ATP during activation reveals a major 25 kDa phosphoprotein and 2 minor phosphoproteins whose phosphorylation is highly sensitive to to inhibition by the PKI-peptide and essentially complete during this early phase. These sperm proteins appear to be immediate substrates for cAMP-dependent protein kinase, and phosphorylation of one or more of these appears to be requires, but not sufficient, for activation of motility. The phosphorylation of other proteins is reduced or eliminated when PKI-peptide is present at the beginning of incubation, but is unaffected by later addition of PKI-peptide. Some of these substrates appear to be likely candidates for axonemal proteins that must be phosphorylated during the later stages of incubation in order to complete the activation process. This selection is based upon a high degree of inhibition by inclusion of PKI-peptide or other inhibitors at the start of the incubation process, on near-completion of their phosphorylation by the end of the 2 min incubation period required for the activation of motility, and evidence that these proteins are phosphorylated during in vivo activation of motility. Although these observations suggest the presence of a second kinase activity that is upregulated by the initial activation of the cAMP-dependent protein kinase, assays using exogenous substrates have not yet been able to identify such a kinase activity.