794 research outputs found

    From: Stephan Bilak

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    The Law of the Land Rural Debt and Private Land Transfer in Upper Canada, 1841-1867

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    In mid-nineteenth century Upper Canada, installment contracts or "bargain and sale agreements" were the pre-eminent mode of land-transfer in rural areas. In contrast, mortgages were generally limited to facilitating capital investment in commercial and manufacturing centers. Case reports indicate that these two different schemes of land transfer and finance resulted from settlement policies, population growth, economic conditions and social pressures. Dans le Haut-Canada du milieu du XIXe siècle, les contrats de paiement à tempérament ou le simple marchandage étaient les principaux modes de transmission de terrain dans les régions rurales. Aussi, le rôle des hypothèques se limitait généralement à faciliter l’investissement des capitaux dans les milieux commerciaux et manufacturiers. Des études de cas indiquent que les deux modes distincts de transmission de terrain et de fonds étaient les résultats des politiques de colonisation, de la croissance démographique, des conditions économiques et des pressions sociales

    Identification of intermediate filaments and their proteins in mature mammalian striated muscle

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    The major purposes of this study were to: (1) clearly identify intermediate filaments (IFs) and elucidate their structural arrangement at the myofibrillar Z-lines in non-diseased, mature mammalian striated muscle cells, and (2) determine the localization of constituent proteins of the IFs by immunogold localization. IFs running transversely to the long axis of the cell and connecting Z-lines of adjacent myofibrils were identified by high resolution transmission electron microscopy (TEM) of plastic-embedded porcine semitendinosus muscle, especially in areas of cells where myofibrils were less tightly packed. When the plane of section included the periphery of myofibrils at their Z-lines, examination indicated that IFs surround, rather than significantly penetrate, myofibrils. IFs also were identified that connect myofibrils (especially at their Z-lines) to nuclei, mitochondria, and the sarcolemma;In order to examine the three-dimensional structural relationship of IFs and myofibrils, micrographs were taken after tilting the specimen to obtain stereo pairs. The results suggest that IFs primarily surround myofibrils at their Z-lines and that a few IFs are arranged in a longitudinal fashion along the periphery of the myofibrils;Results from TEM-immunogold labeling studies indicate that desmin is located primarily at the periphery of Z-lines and nearby I-band regions in both cardiac and skeletal muscle. A lower level of desmin labeling was observed along the periphery of the long axis of the myofibrils, which suggested the presence of some longitudinal IFs. The immunogold labeling pattern observed with anti-synemin was very similar to that obtained with anti-desmin. However, the intensity of the synemin labeling was generally lower than that observed with anti-desmin. Intense labeling with anti-desmin was observed in some areas near the sarcolemma and nuclei in samples examined after pre-embedding labeling. The linear pattern of the labeling suggests that IFs attach myofibrils to those membranous structures;These results support a cytoskeletal concept that IFs link adjacent myofibrils together at their Z-lines, and myofibrils to membranous structures. The IFs are attached to myofibrils primarily in a lateral rather than end-on fashion. The IFs identified by TEM contain desmin. Synemin is either part of, or attached to, desmin IFs

    Interview of Epi Stephen Bilak

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    Shackelford interviews Bilak on his experiences in the mission field in Switzerland. The interview was conducted in Searcy, AR

    Selected properties of the cytoskeletal protein synemin and its interactions with proteins at the muscle Z-line

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    The primary purposes of this study were to: (1) examine selected properties of the intermediate filament-associated protein (IFAP), synemin, (2) identify synemin (or a synemin homolog) in adult mammalian muscle, and (3) examine synemin\u27s ability to interact with proteins located at the myofibrillar Z-line. An integrated biochemical, immunological, and ultrastructural approach was used;Synemin (230 kD) was solubilized from an actomyosin-extracted avian smooth muscle residue and purified by chromatography on two hydroxyapatite columns and one DEAE-Sephacel column in the presence of 6 M urea. Renatured, soluble synemin was obtained by removal of the urea by dialysis against 10 mM Tris-HCl, pH 8.5. Electron microscopy of negatively stained specimens revealed that synemin in 10 mM Tris-HCl, pH 8.5, is spherical in nature (diameter ~11 nm), and chemical crosslinking experiments showed that synemin molecules exist primarily as dimers. Synemin and desmin have similar pH- and ionic strength-dependent solubility properties, but desmin forms intermediate filaments (IFs) and synemin forms complex aggregates under physiological-like conditions. Synemin\u27s wide distribution in adult avian and mammalian skeletal, cardiac, and smooth muscles was shown by Western blot analysis and by immunofluorescence labeling of isolated myofibrils and of muscle cryosections. Double-labeling experiments with conventional immunofluorescence, confocal scanning laser microscopy, and computer-assisted image analysis showed that desmin and synemin colocalize at the myofibrillar Z-lines in a punctate pattern;Synemin\u27s ability to interact with desmin was examined by negative staining and immunogold electron microscopy as well as by immunoblot overlay assays. Purified desmin self-assembles into long (\u3e1 [mu]m) IFs when dialyzed against physiological-like buffers; however, desmin\u27s ability to assemble into these long IFs decreases as the relative amount of synemin to desmin increases. The smallest, full width (~10 nm) IF assembly intermediate formed in the presence of synemin was ~50-70 nm long. Immunogold labeling experiments indicated that synemin binds along the desmin IFs, or at points of filament intersection. Solid-phase binding assays indicated that synemin can bind to desmin and to [alpha]-actinin;These results, taken in toto, indicate that synemin (or a homolog) exists in mammalian muscles, that synemin copolymerizes with, or binds along the length of, desmin IFs, and suggest that synemin may serve as a cytoskeletal crosslinking component between IFs and myofibrils in muscle cells

    El desplazamiento interno más allá de 2018: el camino a seguir

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    Las estadísticas y los desafíos en torno al desplazamiento interno son abrumadores. Sin embargo, se ha aprendido mucho desde la publicación de los Principios Rectores de los Desplazamientos Internos en 1998. Lo que se necesita ahora es un esfuerzo conjunto y un impulso sostenido para aprovechar esa conciencia y afrontar los desafíos cambiante
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