Noctuidae of North America, by Augustus R. Grote. E. W. Classey Limited, London, 1971. 85 pages with 4 coloured plates. Price U.S. $16.95, (£7, 2s. ster1ing)plus postage, handling and applicable sales taxes. Distributed in North America by Entomological Reprint Specialists, P.O. Box 77971, Dockweiler Station, Los Angeles, California, 90007.

0007. Seeing the appearance of this desirable reprint of Noctuidae of North America by Augustus R. Grote is like finding a long-lost friend on a country collecting trip. It is full of valuable lore relating to the pursuit and description of many new noctuid species of yesteryear. The four coloured plates depicting 45 species are reproduced with remarkable fidelity when compared with the originals

First Records of the White People Shoot Border, Eucosma Gloriola (Lepidoptera: Olethreutidae) in Michigan

Excerpt: During late June and early July, 1965, it was apparent that plantations of Scotch and Austrian pines in various Michigan counties were being damaged by lepidopterous larvae mining in the pith of newly developed lateral and terminal branches. Infested samples were examined by Dr. William Wallner, Department of Entomology, Michigan State University, and an attempt was made to rear the extracted larvae. Although as many as two larvae were present in some of the shoots, none survived and no adult moths were secured. A series of larvae was preserved for future study

Moth Species New to Michigan

This is a compilation of moth species previously unrecorded from Michigan. Moore\u27s (1955) publication has been critically examined necessitating some specific changes. All questionable material has been determined by present day specialists in their particular fields. The McDunnough (1938) checklist is followed in the arrangement of the new data together with most of the recent changes in nomenclature as presented by Forbes (1948, 1954, 1960), Hardwick (1970), Hodges (1971), and Covell (1970, 1971). With the advent of more sophisticated collecting equipment and the easier access to Michigan\u27s Upper Peninsula a total of 154 species has been added. Many institutional and private collections have been examined including the large collection at Michigan State University which was not considered in the Moore publication

The Genus Phragmatobia in North America, with the Description of a New Species (Lepidoptera: Arctiidae)

Excerpt: This paper, based on the examination of 1,879 specimens, serves to resolve the taxonomic problems involving the three North American species of Phragmatobia. The genus Phragmatobia, the ruby tiger moths, has had a checkered history since it was described by Stephens in 1829 (type, by monotypy, Noctua j\u27uliginosa Linnaeus, 1758). Although many species have been described in or transferred to this genus, in both the Old and New Worlds, most of them have been removed to other genera. By 1902 Dyar recognized only two North American species, a status since then unchanged (McDunnough, 1938; Forbes, 1960). Despite the recent stability of the names, there has been much confusion as to which names to apply to particular specimens. This problem is resolved below, with the description of a third North American species, long confused with the two named species

Resveratrol given intraperitoneally does not inhibit the growth of high-risk t(4;11) acute lymphoblastic leukemia cells in a NOD/SCID mouse model.

The efficacy of resveratrol as a preventive agent against the growth of t(4;11) acute lymphoblastic leukemia (ALL) was evaluated in NOD.CB17-Prkdcscid/J mice engrafted with the human t(4;11) ALL SEM cell line. SEM cells were injected into the tail vein and engraftment was monitored by flow cytometry. Once engraftment was observed, mice were injected intraperitoneally with resveratrol (10 mg/kg body weight) dissolved in dimethylsulfoxide (DMSO) or DMSO alone (control) every other day, or vincristine (0.5 mg/kg body weight) 3 times per week for 4 weeks (n=16 per group). Comparisons of the percent of human leukemia cells in blood and survival curves showed resveratrol did not inhibit progression of the disease. Liquid chromatography-tandem mass spectrometry analyses of mouse sera showed resveratrol was rapidly metabolized to glucuronidated and sulfated forms 1 h post-injection, with low to no resveratrol or metabolites observed in sera by 24-48 h. These data indicate that in contrast to findings in in vitro models, parenterally administered resveratrol does not have potential as a preventive agent against high risk t(4;11) ALL

Acute Hypercapnia/Ischemia Alters the Esterification of Arachidonic Acid and Docosahexaenoic Acid Epoxide Metabolites in Rat Brain Neutral Lipids.

In the brain, approximately 90% of oxylipins are esterified to lipids. However, the significance of this esterification process is not known. In the present study, we (1) validated an aminopropyl solid phase extraction (SPE) method for separating esterified lipids using 100 and 500 mg columns and (2) applied the method to quantify the distribution of esterified oxylipins within phospholipids (PL) and neutral lipids (NL) (i.e. triacylglycerol and cholesteryl ester) in rats subjected to head-focused microwave fixation (controls) or CO2 -induced hypercapnia/ischemia. We hypothesized that oxylipin esterification into these lipid pools will be altered following CO2 -induced hypercapnia/ischemia. Lipids were extracted from control (n = 8) and CO2 -asphyxiated (n = 8) rat brains and separated on aminopropyl cartridges to yield PL and NL. The separated lipid fractions were hydrolyzed, purified with hydrophobic-lipophilic-balanced SPE columns, and analyzed with ultra-high-pressure liquid chromatography coupled to tandem mass spectrometry. Method validation showed that the 500 mg (vs 100 mg) aminopropyl columns yielded acceptable separation and recovery of esterified fatty acid epoxides but not other oxylipins. Two epoxides of arachidonic acid (ARA) were significantly increased, and three epoxides of docosahexaenoic acid (DHA) were significantly decreased in brain NL of CO2 -asphyxiated rats compared to controls subjected to head-focused microwave fixation. PL-bound fatty acid epoxides were highly variable and did not differ significantly between the groups. This study demonstrates that hypercapnia/ischemia alters the concentration of ARA and DHA epoxides within NL, reflecting an active turnover process regulating brain fatty acid epoxide concentrations

20S human proteasomes bind with a specific orientation to lipid monolayers in vitro

Abstract20S Proteasomes are non-lysosomal, high molecular weight proteinases implicated in the degradation of misfolded proteins and several short-lived regulatory proteins. They have a well established role, as the core of the 26S proteasome complex, in the ubiquitin-dependent proteolytic pathway and in antigen processing. While correctly folded proteins are not degraded by the 20S proteasome, unfolding, for example by oxidation, may render them degradable. The 20S proteasome is a 700-kDa cylindrical particle, composed of 14 subunits of molecular masses 20–35 kDa. There is evidence that 20S proteasomes are in close proximity to or associate with the endoplasmic reticulum and nuclear and plasma membranes in vivo. To better understand the lipid association of 20S proteasomes in vitro, we used a lipid monolayer system as a simple model system for biological membranes. The structure and orientation of the monolayer lipid bound 20S proteasomes has been determined by electron microscopy. 20S proteasomes associated in an ‘end-on’ configuration specifically on PI lipid monolayers forming large arrays, with their channels opposite the lipid headgroups. On ER and Golgi lipid films 20S proteasones were oriented in the same way as on the PI lipid film but were monodisperse. Protein molecules were randomly oriented in the presence of PA, PG, PS, PC and mitochondrial lipid monolayers. We show that 20S proteasomes bind to phospholipids in vitro in a preferred orientation which places the proteasome channel perpendicular to the membrane

Method for repairing cracks in structures

A first material with a known maximum temperature of operation is coated with a second material on at least one surface of the first material. The coating has a melting temperature that is greater than the maximum temperature of operation of the first material. The coating is heated to its melting temperature until the coating flows into any cracks in the first material's surface

Bioactivity and structural properties of chimeric analogs of the starfish SALMFamide neuropeptides S1 and S2

The starfish SALMFamide neuropeptides S1 (GFNSALMFamide) and S2 (SGPYSFNSGLTFamide) are the prototypical members of a family of neuropeptides that act as muscle relaxants in echinoderms. Comparison of the bioactivity of S1 and S2 as muscle relaxants has revealed that S2 is ten times more potent than S1. Here we investigated a structural basis for this difference in potency by comparing the bioactivity and solution conformations (using NMR and CD spectroscopy) of S1 and S2 with three chimeric analogs of these peptides. A peptide comprising S1 with the addition of S2's N-terminal tetrapeptide (Long S1 or LS1; SGPYGFNSALMFamide) was not significantly different to S1 in its bioactivity and did not exhibit concentration-dependent structuring seen with S2. An analog of S1with its penultimate residue substituted from S2 (S1(T); GFNSALTFamide) exhibited S1-like bioactivity and structure. However, an analog of S2 with its penultimate residue substituted from S1 (S2(M); SGPYSFNSGLMFamide) exhibited loss of S2-type bioactivity and structural properties. Collectively, our data indicate that the C-terminal regions of S1 and S2 are the key determinants of their differing bioactivity. However, the N-terminal region of S2 may influence its bioactivity by conferring structural stability in solution. Thus, analysis of chimeric SALMFamides has revealed how neuropeptide bioactivity is determined by a complex interplay of sequence and conformation

Structural analysis of the starfish SALMFamide neuropeptides S1 and S2: The N-terminal region of S2 facilitates self-association

The neuropeptides S1 (GFNSALMFamide) and S2 (SGPYSFNSGLTFamide), which share sequence similarity, were discovered in the starfish Asterias rubens and are prototypical members of the SALMFamide family of neuropeptides in echinoderms. SALMFamide neuropeptides act as muscle relaxants and both S1 and S2 cause relaxation of cardiac stomach and tube foot preparations in vitro but S2 is an order of magnitude more potent than S1. Here we investigated a structural basis for this difference in potency using spectroscopic techniques. Circular dichroism spectroscopy showed that S1 does not have a defined structure in aqueous solution and this was supported by 2D nuclear magnetic resonance experiments. In contrast, we found that S2 has a well-defined conformation in aqueous solution. However, the conformation of S2 was concentration dependent, with increasing concentration inducing a transition from an unstructured to a structured conformation. Interestingly, this property of S2 was not observed in an N-terminally truncated analogue of S2 (short S2 or SS2; SFNSGLTFamide). Collectively, the data obtained indicate that the N-terminal region of S2 facilitates peptide self-association at high concentrations, which may have relevance to the biosynthesis and/or bioactivity of S2 in vivo