Serial position functions in general knowledge

Serial position functions with marked primacy and recency effects are ubiquitous in episodic memory tasks. The demonstrations reported here explored whether bow-shaped serial position functions would be observed when people ordered exemplars from various categories along a specified dimension. The categories and dimensions were: actors and age; animals and weight; basketball players and height; countries and area; and planets and diameter. In all cases, a serial position function was observed: People were more accurate to order the youngest and oldest actors, the lightest and heaviest animals, the shortest and tallest basketball players, the smallest and largest countries, and the smallest and largest planets, relative to intermediate items. The results support an explanation of serial position functions based on relative distinctiveness, which predicts that serial position functions will be observed whenever a set of items can be sensibly ordered along a particular dimension. The serial position function arises because the first and last items enjoy a benefit of having no competitors on 1 side and therefore have enhanced distinctiveness relative to mid-dimension items, which suffer by having many competitors on both sides

Increased susceptibility to proactive interference in adults with dyslexia?

Recent findings show that people with dyslexia have an impairment in serial-order memory. Based on these findings, the present study aimed to test the hypothesis that people with dyslexia have difficulties dealing with proactive interference (PI) in recognition memory. A group of 25 adults with dyslexia and a group of matched controls were subjected to a 2-back recognition task, which required participants to indicate whether an item (mis)matched the item that had been presented 2 trials before. PI was elicited using lure trials in which the item matched the item in the 3-back position instead of the targeted 2-back position. Our results demonstrate that the introduction of lure trials affected 2-back recognition performance more severely in the dyslexic group than in the control group, suggesting greater difficulty in resisting PI in dyslexia.Peer reviewedFinal Accepted Versio

Reanalysis of P2X(7) receptor expression in rodent brain

P2X receptors are cationic-selective ion channels gated by extracellular ATP. There are seven subunits (P2X1-7), the first six of which are expressed throughout the peripheral and central nervous systems. P2X7 receptors are rapidly upregulated and activated as a result of inflammatory stimuli in immune cells, where they act not only as cationic channels but uniquely couple with rapid release of proinflammatory cytokines, cytoskeletal rearrangements, and apoptosis or necrotic cell death. The P2X7 receptor has been termed the cytolytic non-neuronal P2X receptor because it had not been detected in neurons until recently when it has been immunolocalized to several brain regions, particularly the hippocampus, and has been suggested to be involved in presynaptic modulation of transmitter release. Because its expression in brain neurons may have substantial functional implications, we have performed detailed immunocytochemical, immunoblot, and immunoprecipitation studies on brain and non-neuronal tissue using all currently available antibodies. We first examined rats, but staining patterns were inconsistent among antibodies; we therefore studied mice for which there are two P2X7 knock-out mice constructs available, one expressing the LacZ transgene. We found that P2X7 receptor protein is strongly and reliably detected in the submandibular gland and lung of wild-type mice but not in either of the P2X7-/- mice. However, we failed to find evidence for P2X7 receptor protein in hippocampal neurons or their input-output projections. Either the P2X7 protein in the hippocampus is below the limits of detection by the currently available methods or it is not present

Cesium and strontium isotopes in the northwestern North Atlantic and Arctic Ocean, 1981-1985

This report is a follow-up to Woods Hole Oceanographic Institution Technical Report WHOI-84-40. It contains 137cs and 90sr data from seawater samples collected on four cruises in the northwestern North Atlantic, Arctic Ocean, and Barents Sea during 1981 to 1985, and radionuclide data from samples collected on a cruise to the Norwegian-Greenland Seas in 1979. Also included are data from four ice stations in the Arctic from 1979 to 1985. The sample collections were made possible through collaborative efforts with several laboratories. The radionuclide analyses were done at WHOI.Funding was provided by the National Science Foundation under grant Number OCE-840284

The Second Transmembrane Domain of P2X7 Contributes to Dilated Pore Formation

Activation of the purinergic receptor P2X7 leads to the cellular permeability of low molecular weight cations. To determine which domains of P2X7 are necessary for this permeability, we exchanged either the C-terminus or portions of the second transmembrane domain (TM2) with those in P2X1 or P2X4. Replacement of the C-terminus of P2X7 with either P2X1 or P2X4 prevented surface expression of the chimeric receptor. Similarly, chimeric P2X7 containing TM2 from P2X1 or P2X4 had reduced surface expression and no permeability to cationic dyes. Exchanging the N-terminal 10 residues or C-terminal 14 residues of the P2X7 TM2 with the corresponding region of P2X1 TM2 partially restored surface expression and limited pore permeability. To further probe TM2 structure, we replaced single residues in P2X7 TM2 with those in P2X1 or P2X4. We identified multiple substitutions that drastically changed pore permeability without altering surface expression. Three substitutions (Q332P, Y336T, and Y343L) individually reduced pore formation as indicated by decreased dye uptake and also reduced membrane blebbing in response to ATP exposure. Three others substitutions, V335T, S342G, and S342A each enhanced dye uptake, membrane blebbing and cell death. Our results demonstrate a critical role for the TM2 domain of P2X7 in receptor function, and provide a structural basis for differences between purinergic receptors. © 2013 Sun et al

Activation kinetics of single P2X receptors

After the primary structure of P2X receptors had been identified, their function had to be characterized on the molecular level. Since these ligand-gated ion channels become activated very quickly after binding of ATP, methods with adequate time resolution have to be applied to investigate the early events induced by the agonist. Single-channel recordings were performed to describe conformational changes on P2X2, P2X4, and P2X7 receptors induced by ATP and also by allosteric receptor modifiers. The main results of these studies and the models of P2X receptor kinetics derived from these observations are reviewed here. The investigation of purinoceptors by means of the patch clamp technique following site-directed mutagenesis will probably reveal more details of P2X receptor function at the molecular level

Long-term (trophic) purinergic signalling: purinoceptors control cell proliferation, differentiation and death

The purinergic signalling system, which uses purines and pyrimidines as chemical transmitters, and purinoceptors as effectors, is deeply rooted in evolution and development and is a pivotal factor in cell communication. The ATP and its derivatives function as a 'danger signal' in the most primitive forms of life. Purinoceptors are extraordinarily widely distributed in all cell types and tissues and they are involved in the regulation of an even more extraordinary number of biological processes. In addition to fast purinergic signalling in neurotransmission, neuromodulation and secretion, there is long-term (trophic) purinergic signalling involving cell proliferation, differentiation, motility and death in the development and regeneration of most systems of the body. In this article, we focus on the latter in the immune/defence system, in stratified epithelia in visceral organs and skin, embryological development, bone formation and resorption, as well as in cancer. Cell Death and Disease (2010) 1, e9; doi:10.1038/cddis.2009.11; published online 14 January 201