The acute influence of amateur boxing on dynamic cerebral autoregulation and cerebrovascular reactivity to carbon dioxide.

Purpose: The purpose of this study was to investigate the acute effect of head impacts, sustained over the course of three rounds of amateur boxing, on indices of cerebrovascular function.

Methods: Eighteen university amateur boxers (six female) completed three experimental trials in a randomised order; (1) three rounds of boxing (BOX), (2) an equivalent bout of pad boxing (where no blows to the head were sustained; PAD), and (3) a time-matched seated control trial (CON). Indices of cerebrovascular function were determined immediately before and 45 min after each trial.

Soluble ephrin a1 is necessary for the growth of HeLa and SK-BR3 cells.

Background: Ephrin A1 (EFNA1) is a member of the A-type ephrin family of cell surface proteins that function as ligands for the A-type Eph receptor tyrosine kinase family. In malignancy, the precise role of EFNA1 and its preferred receptor, EPHA2, is controversial. Several studies have found that EFNA1 may suppress EPHA2-mediated oncogenesis, or enhance it, depending on cell type and context.

Catabolite repression directly affects transcription of the qa-y gene of Neurospora crassa.

The quinic acid (qa) gene cluster of Neurospora crassa is subject to two levels of gene control: a primary system which responds to the presence of quinic acid via the qa-1S repressor protein, and a secondary system which represses transcription of qa genes in the presence of a preferred carbon source, e.g. glucose.

Tissue transglutaminase clusters soluble A-type ephrins into functionally active high molecular weight oligomers.

The Eph receptors and their ligands, the ephrins, are thought to act at points of close cell-cell contact to elicit bi-directional signaling in receptor and ligand expressing cells. However, when cultured in vitro, some A-type ephrins are released from the cell surface and it is unclear if these soluble ephrins participate in Eph receptor activation. We show that soluble ephrin A5 is subject to oligomerization.