Studies of Reinforced Concrete Beams and Slabs Reinforced with Steel Plates

United States Air ForceContract AF 33(600)-3131

Proopiomelanocortin peptide immunocytochemistry in rhesus monkey brain

The immunocytochemical distribution of Proopiomelanocortin (POMC) peptides ([beta]-endorphin, ACTH, [alpha]-MSH, 16K fragment) was studied in the brain of the rhesus monkey (Macaca mulatta). Some animals were administered colchicine intracerebroventricularly prior to sacrifice to enhance the visualization of perikaryal immunoreactivity. Immunoreactive perikarya are localized to hypothalamic infundibular nucleus, giving rise to several distinct projections. Rostral projections extend through midline diencephalic and preoptic areas, and enter the telencephalon. Along this course, immunoreactive fibers are seen in midline hypothalamic and preoptic nuclei, nucleus of the diagonal band, olfactory tubercle, nucleus accumbens, bed nucleus of stria terminalis, septum, and other limbic structures in telencephalon. Caudal to the anterior commissure, some fibers ascend dorsally to enter the midline thalamus, which they innervate. Lateral projections of the infundibular perikarya course through the medial-basal hypothalamus, dorsal to the optic tracts, and enter the amygdala region where they innervate more medially situated amygdaloid nuclei. Caudal projections of the POMC neurons also extend through midline diencephalon, some coursing along a periventricular path to innervate midline hypothalamic and thalamic nuclei. This projection extends into the mesencephalic substantia grisea centralis and may also contribute to the innervation of more dorsally situated nuclei in the pons and medulla, such as the parabrachial nuclei and nucleus tractus solitarius. Other caudal projections originating in the hypothalamus course through the ventral tegmentum of mesencephalon and pons and may contribute to the innervation of midline raphe and other ventrally situated nuclei in the pons and medulla. The distribution of immunoreactive perikarya and fibers in the brain of rhesus monkey is strikingly similar to that found in the rat brain. However, subtle differences appear to exist in the innervation patterns of particular brain regions.Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/24629/1/0000040.pd

Prodynorphin peptide immunocytochemistry in rhesus monkey brain

The present study describes the immunocytochemical distribution of peptides derived from the prodynorphin precursor in the brain of the rhesus monkey (Macaca mulatta). Animals were treated with colchicine (intracerebroventricularly) prior to perfusion to enhance the observation of perikaryal immunoreactivity. Using antisera generated against dynorphin A(1-17), dynorphin B(1-13), and prodynorphin(186-208) (or bridge peptide), the anatomical distribution of dynorphin systems was mapped. The results indicate a widespread neuronal localization of immunoreactivity from the cerebral cortex to the caudal medulla. Anti-dynorphin B and anti-bridge peptide sera proved useful for the demonstration of neuronal perikarya, while the dynorphin A antiserum was best for localizing terminal projection fields. Immunoreactive perikarya are located in numerous brain loci, including the cingulate cortex, caudate nucleus, amygdala, hypothalamus (especially the magnocellular nuclei), thalamus, substantia grisea centralis, parabrachial nucleus, nucleus tractus solitarius, and other nuclei. In addition, fiber and terminal immunoreactivity are seen in varying densities in the striatum and pallidum, substantia innominata, hypothalamus, substantia nigra pars reticulata, parabrachial nucleus, spinal trigeminal nucleus, and other areas. The distribution of prodynorphin peptides in the brain of the monkey is similar to that described for the rat brain; however, significant differences also exist. Other interspecies differences in the anatomy of prodynorphin and proenkephalin neuronal systems in the monkey and human brain are further discussed.Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/25854/1/0000417.pd

Интерференционный множитель Земли

The article is devoted to the pattern propagation factor of the Earth enabling for more precise determination of the radar station visibility range in case there are reflections from underlying surface. The article provides analytical solution in general form taking into account the Earth sphericity. It enables to obtain the results in the wide-band and altitude range of the observed objects by means of computer simulation. The article gives analytical expression for the Earth multiplier under the flat approximation assumption, free of restrictions common for research literature. Besides, the article defines boundaries in which it is permissible to view the Earth as a flat surface. In addition, the article provides examples to illustrate graphical estimate of the error of all approximations both with respect to the general case of the Earth sphericity and relative to each other.Рассмотрена задача учета интерференционного множителя Земли, позволяющего более точно определить зону видимости радиолокационной станции при наличии отражений от подстилающей поверхности. Представлено аналитическое решение этой задачи в общем виде с учетом сферичности Земли, позволяющее получить результат в широком диапазоне дальностей и высот целей с использованием компьютерного моделирования. Получено аналитическое выражение для множителя Земли в условиях “плоского приближения” без ограничений, обычно встречающихся в литературе. Определены границы допустимости “плоского приближения Земли”. На примерах дается графическая оценка погрешности всех приближений как по отношению к общему случаю сферичности Земли, так и относительно друг друга

Mesenteric panniculitis of the sigmoid colon: a case report and review of the literature

<p>Abstract</p> <p>Introduction</p> <p>Mesenteric panniculitis of the sigmoid colon is a rare occurrence in surgical practice. The aim of this article is to present a case of mesenteric panniculitis of the sigmoid colon and a short review of the literature.</p> <p>Case presentation</p> <p>We reviewed the hospital record of a 63-year-old man who presented with a palpable mass in the left abdomen and clinical signs of a partial bowel obstruction. The pre-operative impression was a possible cancer of the sigmoid colon. A laparotomy was performed through a midline incision. The mesentery was found to be markedly thickened, constricted and puckered. The normal architecture of the adipose tissue had been lost and replaced with an irregular nodular mass. The microscopic pathologic sections demonstrated a chronic reactive inflammatory process with an exuberant proliferation of fibroblasts and fibrocytes. The adipose tissue contained scattered areas of steatonecrosis with foci of lipid-laden macrophages, lymphocytes and plasma cells. The sigmoid colon and its mesocolon were resected. The postoperative course was uneventful and the patient was discharged in good condition, and followed up for the next two years.</p> <p>Conclusion</p> <p>Mesenteric panniculitis of sigmoid is an extremely rare entity of unknown origin in which the normal architecture of the mesentery is replaced by fibrosis, necrosis and calcification. On gross examination the alterations may be mistaken for a neoplastic process. A frozen section may be necessary for confirmation of the diagnosis. When the advanced inflammatory changes became irreversible and bowel obstruction occurs, resection may be indicated.</p

The association of circulating amylin with β-amyloid in familial Alzheimer's disease.

INTRODUCTION: This study assessed the hypothesis that circulating human amylin (amyloid-forming) cross-seeds with amyloid beta (Aβ) in early Alzheimer's disease (AD). METHODS: Evidence of amylin-AD pathology interaction was tested in brains of 31 familial AD mutation carriers and 20 cognitively unaffected individuals, in cerebrospinal fluid (CSF) (98 diseased and 117 control samples) and in genetic databases. For functional testing, we genetically manipulated amylin secretion in APP/PS1 and non-APP/PS1 rats. RESULTS: Amylin-Aβ cross-seeding was identified in AD brains. High CSF amylin levels were associated with decreased CSF Aβ42 concentrations. AD risk and amylin gene are not correlated. Suppressed amylin secretion protected APP/PS1 rats against AD-associated effects. In contrast, hypersecretion or intravenous injection of human amylin in APP/PS1 rats exacerbated AD-like pathology through disruption of CSF-brain Aβ exchange and amylin-Aβ cross-seeding. DISCUSSION: These findings strengthened the hypothesis of circulating amylin-AD interaction and suggest that modulation of blood amylin levels may alter Aβ-related pathology/symptoms

A phase-field model for phase transformations in glass-forming alloys

A phase-field model is proposed for phase transformations in glass-forming alloys. The glass transition is introduced as a structural relaxation, and the competition between the glass and crystalline phases is investigated. The simulations are performed for Cu-Zr alloys, employing thermodynamic and kinetic parameters derived from reported thermodynamic modeling and molecular dynamics simulation results,[1–3] respectively. Four distinct phase fields are treated with a multi-phase-field approach, representing the liquid/glass, Cu10Zr7, CuZr, and CuZr2 phases. In addition, a continuum-field method is applied to the liquid to accommodate the liquid–glass transformation. The combined phase-field approach is used to investigate the glass formation tendency, and critical cooling rates are estimated and compared with the reported experimental values

Calcium Ions Promote Formation of Amyloid β-Peptide (1–40) Oligomers Causally Implicated in Neuronal Toxicity of Alzheimer's Disease

Amyloid β-peptide (Aβ) is directly linked to Alzheimer's disease (AD). In its monomeric form, Aβ aggregates to produce fibrils and a range of oligomers, the latter being the most neurotoxic. Dysregulation of Ca2+ homeostasis in aging brains and in neurodegenerative disorders plays a crucial role in numerous processes and contributes to cell dysfunction and death. Here we postulated that calcium may enable or accelerate the aggregation of Aβ. We compared the aggregation pattern of Aβ(1–40) and that of Aβ(1–40)E22G, an amyloid peptide carrying the Arctic mutation that causes early onset of the disease. We found that in the presence of Ca2+, Aβ(1–40) preferentially formed oligomers similar to those formed by Aβ(1–40)E22G with or without added Ca2+, whereas in the absence of added Ca2+ the Aβ(1–40) aggregated to form fibrils. Morphological similarities of the oligomers were confirmed by contact mode atomic force microscopy imaging. The distribution of oligomeric and fibrillar species in different samples was detected by gel electrophoresis and Western blot analysis, the results of which were further supported by thioflavin T fluorescence experiments. In the samples without Ca2+, Fourier transform infrared spectroscopy revealed conversion of oligomers from an anti-parallel β-sheet to the parallel β-sheet conformation characteristic of fibrils. Overall, these results led us to conclude that calcium ions stimulate the formation of oligomers of Aβ(1–40), that have been implicated in the pathogenesis of AD