Missed Ischemic Stroke Diagnosis in the Emergency Department by Emergency Medicine and Neurology Services.

Background And Purpose: The failure to recognize an ischemic stroke in the emergency department is a missed opportunity for acute interventions and for prompt treatment with secondary prevention therapy. Our study examined the diagnosis of acute ischemic stroke in the emergency department of an academic teaching hospital and a large community hospital.

Methods: A retrospective chart review was performed from February 2013 to February 2014.

Malignant cerebral edema after large anterior circulation infarction: a review.

Malignant infarction implies a large middle cerebral artery (MCA) stroke that leads to rapid clinical deterioration and edema formation, and can be associated with hemorrhagic transformation, herniation, and poor functional outcomes, including death. Malignant edema is brain edema formation that occurs in the setting of large territory infarction. This review discusses the most recent efforts in diagnosis, prevention, and management of malignant edema in acute ischemic strokes.

Intracellular domain of the IFNaR2 interferon receptor subunit mediates transcription via Stat2.

We recently demonstrated that IFNaR2, a subunit of the interferon receptor, can be proteolytically cleaved in response to interferon-alpha and other activators of protein kinase C. Cleavage occurs at multiple sites, via a mechanism similar to that employed by Notch and the Alzheimer's precursor protein, and releases the intracellular domain (ICD). In this study, we demonstrate that the IFNaR2 ICD, when fused to the yeast Gal4 DNA binding domain (Gal4DBD) selectively modulates transcription of four different promoters under the control of Gal4 upstream activating sequences.

Regulated proteolysis of the IFNaR2 subunit of the interferon-alpha receptor.

The type I interferons (IFNs) bind surface receptors, induce JAK kinases and activate STAT transcription factors to stimulate the transcription of genes downstream of IFN-stimulated response elements (ISREs). In this study, we demonstrate that IFNaR2, a subunit of the type I IFN receptor, is proteolytically cleaved in a regulated manner. Immunoblotting shows that multi-step cleavage occurs in response to phorbol ester (PMA) and IFN-alpha, generating both a transmembrane 'stub' and the intracellular domain (ICD), similar to Notch proteolysis.

Stat2 binding to the interferon-alpha receptor 2 subunit is not required for interferon-alpha signaling.

The interferon-alpha (IFNalpha) receptor consists of two subunits, the IFNalpha receptor 1 (IFNaR1) and 2 (IFNaR2) chains. Following ligand binding, IFNaR1 is phosphorylated on tyrosine 466, and this site recruits Stat2 via its SH2 domain. In contrast, IFNaR2 binds Stat2 constitutively.