Root distribution in a Norway spruce (Picea abies (L.) Karst.) stand subjected to drought and ammonium-sulphate application

Results of the spatial distribution of fine roots are reported from a Norway spruce (Picea abies (L.) Karst.) in SW Sweden stand subjected to drought (D) and ammonium-sulphate application (NS). The sampling was carried out by excavating monoliths in segments of 0.5 × 0.5 × 0.1 m to a depth of one meter. Root data also included in the study were obtained by excavating whole trees and soil coring.The data suggest a fairly deep distribution pattern of fine roots (< 1 mm in diameter) in the study area compared with other forest sites in SW Sweden. The weight fraction of living fine roots in the LFH-horizon amounted to 53, 36 and 55% of the total fine-root biomass and 12, 30 and 32% of the total fine-root necromass (dead fine roots) in the control, D and NS-treatment areas respectively. Drought seemed to result in a redistribution of fine roots to deeper mineral soil horizons. Ammonium sulphate application led to the reverse, viz, a concentration of fine roots to the LFH-horizon. A significantly smaller fine-root necromass was indicated in the LFH-horizon of the control areas compared with both the D and NS-treatment areas, suggesting a high mortality of fine roots in these areas. A heavy dry matter fraction accumulates in roots > 1 mm in diameter and in stumps. These root fraction, were frequently found between the trees, although the stump constitutes an important fraction in terms of dry weight.     

METTL14 Inhibits Hematopoietic Stem/Progenitor Differentiation and Promotes Leukemogenesis via mRNA m6A Modification

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A prudent hoarder: effects of long-term hoarding in the European nuthatch, Sitta europaea

Although hoarding has been studied intensively for many decades,few studies have attempted to measure its actual fitness consequences.To fill this gap, we used ptilochronology, the growth of replacementfeathers as a measure of nutritional status, and thus a reflectionof starvation risk, of individual European nuthatches (Sittaeuropaea) during winter. We found that nuthatches are long-termhoarders, retrieving stored food up to at least 98 days afterstoring it. Long-term hoarding enhanced the nutritional statusof individual birds significantly because those individualsexperimentally given an opportunity to store seeds during autumnregrew plucked rectrices faster and larger than did controlbirds. Nuthatches used their stored seeds prudently by adjustingthe amounts they ate to meet their requirements, as determinedby ambient temperatures. Nuthatches refrained from using storedfood during periods of relatively benign conditions so theycould use the food during periods of more severe conditions.     

Increased Intra- and Extracellular Concentrations of γ-Glutamylglutamate and Related Dipeptides in the Ischemic Rat Striatum: Involvement of γ-Glutamyl Transpeptidase

Abstract: The present work relates to the possibility that the ATP-independent enzyme γ-glutamyl transpeptidase (EC 2.3.2.2), which has been postulated to be part of an amino acid uptake system, is active during cerebral ischemia. This was evaluated in the ischemic rat striatum by determination of intra- and extracellular concentrations of γ-glutamyl dipeptides (the products of the transpeptidation) and glutathione (the physiological γ-glutamyl donor). An ischemic period (0–30 and 31–60 min) resulted in prominent increases in the respective concentration of extracellular γ-glutamylglutamate (24- and 67-fold), γ-glutamyltaurine + γ-glutamylglycine (5.8- and 19-fold), and γ-glutamylglutamine (2.6- and 6.8-fold) as revealed using in vivo microdialysis. The changes coincided with increased respective extracellular concentrations of glutamate (83- and 115-fold), taurine (17- and 25-fold), glycine (4.6- and 6.1-fold), and glutamine (1.7- and 2.1-fold). Furthermore, under anoxic conditions in vitro (0–30 and 0–60 min), respective striatal tissue concentrations were increased for γ-glutamylglutamate (20- and 17-fold), γ-glutamyltaurine (6.7- and 11-fold), γ-glutamylglutamine (1.7- and 1.2-fold), and γ-glutamylglycine (14- and 18-fold), whereas glutathione levels were, on an average, decreased by ∼350 µ M . In summary, γ-glutamyl transpeptidase is involved in de novo dipeptide synthesis in the mammalian brain during anoxic conditions, indicating transport of amino acids such as glutamate.     

Alpha2A-adrenoceptors strengthen working memory networks by inhibiting cAMP-HCN channel signaling in prefrontal cortex

Spatial working memory (WM; i.e., "scratchpad" memory) is constantly updated to guide behavior based on representational knowledge of spatial position. It is maintained by spatially tuned, recurrent excitation within networks of prefrontal cortical (PFC) neurons, evident during delay periods in WM tasks. Stimulation of postsynaptic alpha2A adrenoceptors (alpha2A-ARs) is critical for WM. We report that alpha2A-AR stimulation strengthens WM through inhibition of cAMP, closing Hyperpolarization-activated Cyclic Nucleotide-gated (HCN) channels and strengthening the functional connectivity of PFC networks. Ultrastructurally, HCN channels and alpha2A-ARs were colocalized in dendritic spines in PFC. In electrophysiological studies, either alpha2A-AR stimulation, cAMP inhibition or HCN channel blockade enhanced spatially tuned delay-related firing of PFC neurons. Conversely, delay-related network firing collapsed under conditions of excessive cAMP. In behavioral studies, either blockade or knockdown of HCN1 channels in PFC improved WM performance. These data reveal a powerful mechanism for rapidly altering the strength of WM networks in PFC.     

Changes in Extracellular Amino Acids and Spontaneous Neuronal Activity During Ischemia and Extended Reflow in the CA1 of the Rat Hippocampus

This study addresses the possible involvement of an agonist-induced postischemic hyperactivity in the delayed neuronal death of the CA1 hippocampus in the rat. In two sets of experiments, dialytrodes were implanted into the CA1 either acutely or chronically (24 h of recovery). During 20 min of cerebral ischemia (four-vessel occlusion model) and 8 h of reflow, we followed extracellular amino acids and multiple-unit activity. Multiple-unit activity ceased within 20 sec of ischemia and remained zero during the ischemic insult and for the following 1 h of reflow. During ischemia, extracellular aspartate, glutamate, taurine, and gamma-aminobutyric acid increased in both acute and chronic experiments (seven- to 26-fold). Multiple-unit activity recovered to preischemic levels following 4-6 h of reflow. In the group with dialytrodes implanted acutely, the continuous increase in multiple-unit activity reached 110% of basal at 8 h of reflow. In the group with dialytrodes implanted chronically, multiple-unit activity recovered faster and reached 140% of control at 8 h, paralleled by an increase in extracellular aspartate (5.5-fold) and glutamate (twofold). In conclusion, the postischemic increase of excitatory amino acids and the recovery of the neuronal activity may stress the CA1 pyramidal cells, which could be detrimental in combination with, e.g., postsynaptic impairments.     

Radicicol-sensitive peptide binding to the N-terminal portion of GRP94

GRP94 is a molecular chaperone that carries immunologically relevant peptides from cell to cell, transferring them to major histocompatibility proteins for presentation to T cells. Here we examine the binding of several peptides to recombinant GRP94 and study the regulation and site of peptide binding. We show that GRP94 contains a peptide-binding site in its N-terminal 355 amino acids. A number of peptides bind to this site with low on- and off-rates and with specificity that is distinct from that of another endoplasmic reticulum chaperone, BiP/GRP78. Binding to the N-terminal fragment is sufficient to account for the peptide binding activity of the entire molecule. Peptide binding is inhibited by radicicol, a known inhibitor of the chaperone activities of HSP90-family proteins. However, the peptide-binding site is distinct from the radicicol-binding pocket, because both can bind to the N-terminal fragment simultaneously. Furthermore, peptide binding does not cause the same conformational change as does binding of radicicol. When the latter binds to the N-terminal domain, it induces a conformational change in the downstream, acidic domain of GRP94, as measured by altered gel mobility and loss of an antibody epitope. These results relate the peptide-binding activity of GRP94 to its other function as a chaperone.