Altered Arrangement Research Articles

Histopathological Study on Induced Eeffects of Cadmium on Liver, Gizzard and Kidney of Larus argentatus

The study was carried out on the effects of cadmium (Cd) on liver, gizzard and kidney of Larus argentatus. Significant alterations were observed after the treatment of high and low dose of cadmium chloride injected to Larus argentatus. Investigation of the effects of Cd on body tissues was done by sectioning of fixed tissue by paraffin section techniques. Major changes were noted at high dose of cadmium chloride in liver, kidney and gizzard. While, under low dose of cadmium chloride, mild to moderate changes in hepatocytes around blood vessels in liver; reduction in thickness of epithelium and muscular layer in gizzard; and slight alterations in arrangement of tubules of loop of henle in the kidney of proximal convoluted tubules with granular cytoplasm were observed. No lesions were found in the mentioned body tissues of Larus argentatus of control group.

Cell death and lumen formation in spheroids of MCF‐7 cells

3D (three-dimensional) cell culture permits a more integrated analysis of the relationship between cells, inserting them into a structure more closely resembling the cellular microenvironment in vivo. The development of in vitro parameters to approximate in vivo 3D cellular environments makes a less reductionist interpretation of cell biology possible. For breast cells, in vitro 3D culture has proven to be an important tool for the analysis of luminal morphogenesis. A greater understanding of this process is necessary because alterations in the lumen arrangement are associated with carcinogenesis. Following lumen formation in 3D cell culture using laser scanning confocal microscopy, we observed alterations in the arrangement of cytoskeletal components (F-actin and microtubules) and increasing levels of cell death associated with lumen formation. The formation of a polarized monolayer facing the lumen was characterized through 3D reconstructions and the use of TEM (transmission electron microscopy), and this process was found to occur through the gradual clearing of cells from the medullary region of the spheroids. This process was associated with different types of cell death, such as apoptosis, autophagy and entosis. The present study showed that changes in the extracellular matrix associated with long periods of time in 3D cell culture lead to the formation of a lumen in MCF-7 cell spheroids and that features of differentiation such as lumen and budding formation occur after long periods in 3D culture, even in the absence of exogenous extracellular compounds.

CMS: an adapter molecule involved in cytoskeletal rearrangements.

Cas ligand with multiple Src homology (SH) 3 domains (CMS) is an ubiquitously expressed signal transduction molecule that interacts with the focal adhesion protein p130(Cas). CMS contains three SH3 in its NH2 terminus and proline-rich sequences in its center region. The latter sequences mediate the binding to the SH3 domains of p130(Cas), Src-family kinases, p85 subunit of phosphatidylinositol 3-kinase, and Grb2. The COOH-terminal region contains putative actin binding sites and a coiled-coil domain that mediates homodimerization of CMS. CMS is a cytoplasmic protein that colocalizes with F-actin and p130(Cas) to membrane ruffles and leading edges of cells. Ectopic expression of CMS in COS-7 cells resulted in alteration in arrangement of the actin cytoskeleton. We observed a diffuse distribution of actin in small dots and less actin fiber formation. Altogether, these features suggest that CMS functions as a scaffolding molecule with a specialized role in regulation of the actin cytoskeleton.

Comparison of acute response to polychlorinated biphenyl in liver of rat and channel catfish: A biochemical and morphological study

The acute response of liver of channel catfish and rat to polychlorinated biphenyl was compared on a structural and functional basis. Both the rat and the fish had elevated microsomal enzyme activities. However, in the rat the response was quantitatively greater in all respects. Morphologically, rats responded with lipid accumulation and marked increases in smooth endoplasmic reticulum. Fish liver showed lipid accumulation and increased profiles of rough endoplasmic reticulum with alterations in arrangement that appeared as vesicles and parallel cisternae. Minimal changes were seen in smooth endoplasmic reticulum, which appeared to be increased as discrete foci.

Tremorogenesis: Effects of reserpine on the substantia nigra

A study of the parkinsonism-like state in the dog was made by means of moderate dosages of reserpine. Light-microscope studies of the substantia nigra and autospectral analysis of the accelerometrically determined tremor were performed. Tremor measurements and histological studies were performed 4 hr after a single injection of reserpine and 4 hr after the last of four daily injections of reserpine. Some animals were allowed to survive for observation of additional signs of parkinsonism. The drug-induced tremor in the dog was compared with autospectrally analyzed tremor measurements on clinically evaluated Parkinson's disease patients. The administration of reserpine did not evoke a parkinsonian tremor frequency. Instead, a high-frequency tremor was produced. Alterations in arrangement of the Nissl substance, cytoplasmic vacuolization, and nuclear lobulation were produced by all dosages of reserpine, and could not be correlated with the occurrence of experimental tremor. It is hypothesized that such cellular alterations may briefly disrupt neuronal metabolic processes which are then reflected as a transitory nigral dysfunction related to gamma-alpha imbalance at spinal levels. Such an imbalance may contribute to the genesis of tremor.

Alteration of Arrangements in Respect of the Part I. Examination

Alteration of Arrangements in Respect of the Part I. Examination

Chemie der Eiweisskörper

ALTHOUGH only four years have elapsed since the first edition of this work appeared, the great advances made in our knowledge of the chemistry of the proteids have necessitated a considerable revision of the book. The author, however, has found it possible to avoid any enlargement of the work by altering the order of subjects treated, and by stating the facts more concisely than in the previous edition. Some of the alterations in arrangement appear somewhat difficult to justify. Thus, for example, in the earlier edition the physical characters were dealt with prior to the consideration of the more purely chemical properties of the proteids, while in this edition the order is reversed. As the first edition has been already reviewed in NATURE, only a brief account of the chief additions to the second will be necessary.