Drip,Ship, and On-Demand Endovascular Therapy for Acute Ischemic Stroke

Background

The “drip and ship” approach can facilitate an early initiation of intravenous thrombolysis (IVT) for acute ischemic stroke (AIS) at community hospitals. New endovascular treatment modalities, such as stent retrieval, have further improved the rate of safe and successful recanalization. We assessed the clinical outcomes of on-demand endovascular therapy in patients with AIS who were transported to a comprehensive stroke center under the “drip and ship” paradigm.

Methods

This retrospective study evaluated prospectively registered patients with acute large vessel occlusions in the anterior circulation who underwent endovascular recanalization after IVT at our regional comprehensive stroke center between January 2011 and April 2014. Clinical outcomes and neuroradiological findings were compared between patients who received IVT at the center (direct visit, DV) and at a community hospital (drip and ship, DS).

Results

Baseline characteristics such as age, initial National Institutes of Health Stroke Scale (NIHSS) score, and risk factors for stroke were similar, and most patients underwent endovascular therapy with a Solitaire stent (81.9% vs. 89.3% for DV and DS, respectively, P = 0.55). The average initial NIHSS score was 12.15±4.1 (12.06 vs. 12.39 for DV and DS, respectively, P = 0.719). The proportions of long-term favorable outcomes (modified Rankin Scale score ≤2 at 90 days) and successful recanalization (Thrombolysis in Cerebral Ischemia score ≥2b) were not significantly different (P = 0.828 and 0.158, respectively). The mortality rates and occurrences of symptomatic intracerebral hemorrhage were not significantly different (P = 0.999 and 0.267, respectively).

Conclusions

The “drip and ship” approach with subsequent endovascular therapy is a feasible treatment concept for patients with acute large vessel occlusion in the anterior circulation that could help improve clinical outcomes in patients with AIS.     

Isolation and characterization of a cDNA coding for human myeloperoxidase

A cDNA encoding the carboxyl-terminal fragment of the human myeloperoxidase heavy chain was isolated and characterized. It was then used to determine the locations of the myeloperoxidase light and heavy chains in the polypeptide precursor. A cDNA library from poly(A)+ RNA from human leukemia HL-60 cells was constructed in pBR322 and screened by differential hybridization with enriched and depleted cDNA probes and then by hybridization with an oligonucleotide probe. A cDNA clone containing 1278 bp with an open reading frame of 474 bp and a 3' noncoding region of 804 bp was isolated. The amino acid sequence deduced from the nucleotide sequence consisted of 158 residues including a sequence of 14 amino acids known to be present in the heavy chain of the molecule. The cDNA also included a stop codon of TAG followed by a noncoding sequence that included a potential recognition site for polyadenylylation and a poly(A) tail. RNA transfer blot analysis with the cDNA probe indicated that myeloperoxidase mRNA was approximately 3.3 kb in length. In vitro translation of the mRNA selected by cDNA hybridization revealed preferential synthesis of a 74,000-Da polypeptide precursor that could be precipitated with anti-myeloperoxidase IgG. Antibodies specific for the heavy and light chains of myeloperoxidase were isolated from antiserum by affinity chromatography employing Sepharose columns covalently bound to the heavy or light chains. Antibodies specific for the light chain or the heavy chain readily precipitated the 74,000-Da precursor polypeptide. These results indicated that myeloperoxidase is synthesized as a single chain which undergoes processing into a light and heavy chain. Furthermore, the heavy chain of myeloperoxidase originates from the carboxyl terminus of the precursor polypeptide.     

Effects of Atmospheric NO2 on Azolla-Anabaena Symbiosis

Cultures of the water fern Azolla pinnata R, Br. exposed for1 week to atmospheric NO₂ (50, 100 or 200 nl l^-1) induced additionallevels of nitrate reductase (NaR) protein and nitrite reductase(NiR) activity. At low concentrations of NO₂ (50 nl l^-1), nitratederived from NO₂ provides an alternative N source for Azollabut does not affect rates of acetylene reduction. However, thesymbiotic relationship between Azolla and its endosymbiont,Anabaena azollae is only affected adversely by high concentrations(100 and 200 nl l^-1) of atmospheric NO₂. The resultant decreasesin rate of growth, nitrogen fixation, heterocyst formation,and overall nitrogen cycling are probably due to the additionalaccumulation of N products derived from higher levels of atmosphericNO₂. Parallel increases in levels of polyamines suggest thatAzolla partially alleviates these harmful effects by incorporatingsome of the extra NO₂-induced N into polyamines.Copyright 1994,1999 Academic Press Azolla-Anabaena symbiosis, nitrogen dioxide pollution, nitrogen metabolism, polyamines     

Sterilization effects of a TiO<Subscript>2</Subscript> photocatalytic film against a<Emphasis Type="Italic">Streptococcus mutans</Emphasis> culture

Streptococcus mutans is one of the more significant pathogens involved in the development of dental caries in humans. The purpose of this research was to design a TiO₂-coated dental instrument and to determine the bactericidal effects of the instrument onS. mutants. TiO₂ photocatalytic films were prepared by the low-pressure metal-organic chemical vapor deposition (LPMOCVD) method using titanium tetraisopropoxide (TTIP) as precursor. The photocatalytic reaction was carried out on a TiO₂-coated pyrex petri dish with an ultraviolet (UV) light emitting diode (LED) illuminator or a fluorescent lamp light source. Our data indicates that the relative survival ratio ofS. mutans when plated onto TiO₂ photocatalytic films and under exposure to UV-A light for 15 min was 0.01%. In addition, a fluorescent lamp light source also had bactericidal effects on theS. mutans plated TiO₂ photocatalytic films. These results indicate that TiO₂-coated dental materials or devices may be useful in dental treatments for the prevention of carious or enamel demineralization.     

Intracellular K(+) inhibits apoptosis by suppressing the Apaf-1 apoptosome formation and subsequent downstream pathways but not cytochrome c release

Cellular ionic homeostasis, fundamentally K(+) homeostasis, has been implicated as a critical regulator of apoptosis. The intracellular K(+) efflux on apoptotic insult and suppression of apoptosis by high concentration of extracellular K(+) or after inhibition of this efflux by K(+) channel blockers have established the crucial role of K(+) in turning on the apoptotic machinery. Several contrasting observations have reported the antiapoptotic effect of intracellular K(+) concentration to be the result of inhibition of cytochrome c release from mitochondria, but the exact inhibitory mechanism remains obscure. However, here we show the blockage of K(+) efflux during apoptosis did not affect cytochrome c release from the mitochondria, still completely inhibited the formation of the apoptosome comprising Apaf-1, cytochrome c, caspase-9 and other accessories. As a consequence of this event, procaspase-9, -3, -8 and other death-related proteins were not processed. Furthermore, physiological concentrations of K(+) also inhibited the processing of procaspase-3 by purified caspase-8 or -9, the nucleosomal DNA fragmentation by purified DFF40/CAD and the nuclear fragmentation to varying extents. Altogether, these findings suggest that the efflux of K(+) is prerequisite not only for the formation of the apoptosome but also for the downstream apoptotic signal-transduction pathways.     

Modifications of membrane lipids in response to wounding of Arabidopsis thaliana leaves

Mechanical wounding of Arabidopsis thaliana leaves results in modifications of most membrane lipids within 6 hours. Here, we discuss the lipid changes, their underlying biochemistry, and possible relationships among activated pathways. New evidence is presented supporting the role of the processive galactosylating enzyme SENSITIVE TO FREEZING2 in the wounding response.