Shell microstructure of <Emphasis Type="Italic">Discinisca suborbicularis</Emphasis> sp. nov. (Brachiopoda,Lingulata) from the Upper Jurassic of Western Siberia

A new species of the phosphatic brachiopod Discinisca suborbicularis (family Discinidae) from the Upper Jurassic of Western Siberia (latitudinal Priob’e) is established. The shell microstructure under protegulum and brephic shell and the microstructure of adult shell (that corresponds to three developmental stages) are described in detail. The shell microstructure of new species considerably differs from Paleozoic discinids and is similar to Recent discinids. D. suborbicularis differs from recent discinids in the presence of protegulum and thicker organophosphatic primary layer.     

Enzyme-linked lectinosorbent assay of <Emphasis Type="Italic">Escherichia coli</Emphasis> and <Emphasis Type="Italic">Staphylococcus aureus</Emphasis>

In this study, we developed a microplate sandwich analysis of Escherichia coli and Staphylococcus aureus bacterial pathogens based on the interaction of their cell wall carbohydrates with natural receptors called lectins. An immobilized lectin-cell-biotinylated lectin complex was formed in this assay. Here, we studied the binding specificity of several plant lectins to E. coli and S. aureus cells, and pairs characterized by high-affinity interactions were selected for the assay. Wheat germ agglutinin and Ricinus communis agglutinin were used to develop enzyme-linked lectinosorbent assays for E. coli and S. aureus cells with the detection limits of 4 × 10⁶ and 5 × 10⁵ cells/mL, respectively. Comparison of the enzyme-linked immonosorbent assay and the enzyme-linked lectinosorbent assay demonstrated no significant differences in detection limit values for E. coli. Due to the accessibility and universality of lectin reagents, the proposed approach is a promising tool for the control of a wide range of bacterial pathogens.     

Implosion dynamics of condensed Z-pinch at the Angara-5-1 facility

The implosion dynamics of a condensed Z-pinch at load currents of up to 3.5 MA and a current rise time of 100 ns was studied experimentally at the Angara-5-1 facility. To increase the energy density, 1- to 3-mm-diameter cylinders made of a deuterated polyethylene?agar-agar mixture or microporous deuterated polyethylene with a mass density of 0.03–0.5 g/cm³ were installed in the central region of the loads. The plasma spatiotemporal characteristics were studied using the diagnostic complex of the Angara-5-1 facility, including electron-optical streak and frame imaging, time-integrated X-ray imaging, soft X-ray (SXR) measurements, and vacuum UV spectroscopy. Most information on the plasma dynamics was obtained using a ten-frame X-ray camera (Е > 100 eV) with an exposure of 4 ns. SXR pulses were recorded using photoemissive vacuum X-ray detectors. The energy characteristics of neutron emission were measured using the time-offlight method with the help of scintillation detectors arranged along and across the pinch axis. The neutron yield was measured by activation detectors. The experimental results indicate that the plasma dynamics depends weakly on the load density. As a rule, two stages of plasma implosion were observed. The formation of hot plasma spots in the initial stage of plasma expansion from the pinch axis was accompanied by short pulses of SXR and neutron emission. The neutron yield reached (0.4–3) × 10¹⁰ neutrons/shot and was almost independent of the load density due to specific features of Z-pinch dynamics.     

Ribosomal leaky scanning through a translated uORF requires eIF4G2

eIF4G2 (DAP5 or Nat1) is a homologue of the canonical translation initiation factor eIF4G1 in higher eukaryotes but its function remains poorly understood. Unlike eIF4G1, eIF4G2 does not interact with the cap-binding protein eIF4E and is believed to drive translation under stress when eIF4E activity is impaired. Here, we show that eIF4G2 operates under normal conditions as well and promotes scanning downstream of the eIF4G1-mediated 40S recruitment and cap-proximal scanning. Specifically, eIF4G2 facilitates leaky scanning for a subset of mRNAs. Apparently, eIF4G2 replaces eIF4G1 during scanning of 5′ UTR and the necessity for eIF4G2 only arises when eIF4G1 dissociates from the scanning complex. In particular, this event can occur when the leaky scanning complexes interfere with initiating or elongating 80S ribosomes within a translated uORF. This mechanism is therefore crucial for higher eukaryotes which are known to have long 5′ UTRs with highly frequent uORFs. We suggest that uORFs are not the only obstacle on the way of scanning complexes towards the main start codon, because certain eIF4G2 mRNA targets lack uORF(s). Thus, higher eukaryotes possess two distinct scanning complexes: the principal one that binds mRNA and initiates scanning, and the accessory one that rescues scanning when the former fails.     

Thrombin is an extracellular signal that activates intracellular death protease pathways inducing apoptosis in model motor neurons

Apoptosis, often also termed “programmed cell death,” occurs in normal development in the brain and spinal cord. Important to concepts of disease and potential intervention is the exciting finding that apoptosis is also found after neurotrauma and in a number of neurodegenerative diseases. Although the precise mechanism of neuronal cell loss remains unknown, much emphasis has been placed recently on the activation of cell death protease cascades within the cell. How these cascades may be activated, especially from extracellular influences, is currently poorly understood. Thrombin, the multifunctional coagulation protease, is an early phase modulator at sites of tissue injury and has been shown to induce cell death in neurons by an apoptotic mechanism by activating its receptor, PAR-1. Using a model motor neuronal cell line, NSC19, which we have shown undergoes apoptosis after treatment with classic apoptosis inducers such as the topoisomerase inhibitors camptothecin and etoposide, we unambiguously found that nanomolar thrombin induced characteristic signs of apoptosis. Strikingly, endonucleolysis was accompanied by an increase in caspase-3-like activity in cellular extracts, which correlated with both detection of caspase-induced signature cleavage of the cortical cytoskeleton component nonerythroid spectrin (α-fodrin) and identification of increased accessibility of a caspase cleavage domain, using an antibody (Ab127) made against a synthetic peptide KGDEVD. Demonstrating that thrombin activation of death proteases was linked to cell death, we were able to inhibit thrombin-induced apoptosis by using a caspase family inhibitor, benzyloxycarbonyl-Asp-(oMe)-flouromethyl ketone (Boc-D-FMK). These novel results demonstrate that thrombin serves as an extracellular “death signal” to activate intracellular protease pathways. These pathways lead to apoptotic cell death and can be modulated by inhibiting caspase activity downstream to PAR-1. Published 1998 John Wiley & Sons, Inc. J Neurobiol 36: 64–80, 1998

1 This is a US Government work and, as such, is in the public domain in the United States of America.