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In order to understand the initiation behavior of microstructurally small cracks in a stress corrosion cracking condition, it is important to know the tensile normal stress acting on the grain boundary (normal GB stress). The local stress in a polycrystalline body is enhanced by the inhomogeneity which stems from the shape and orientation of each grain. The stress in a three-dimensional polycrystalline body consisting of 100 grains with random orientation, under a remote uniform tensile stress condition, is evaluated by the finite element method. It was revealed that the local stress on the polycrystalline body is inhomogeneous under uniform applied stress and becomes large at those grain boundaries that are perpendicular to the load axis, though there is large fluctuation. It was also shown that the normal GB stress tends to be large near the triple points due to the deformation constraint caused by adjacent grains. Finally, the maximum stress on the surface of a large component caused by the inhomogeneity was evaluated by using Gumbel statistics.

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For the purpose of clarifying the magnetoorientation mechanism of several biological membrane systems, xylene-suspended thin-layered single crystals of lecithin, which is a major component of membranes, were subjected to magnetic fields of various strengths, and the orientation behavior of the crystals was analyzed. Lecithin crystals oriented in such a way that the directions of both the hydrocarbon chains and the phosphorylcholine group of the lecithin molecule were perpendicular to the magnetic field, suggesting that the crystals were diamagnetically biaxial. In contrast, hydrocarbon chains of phospholipids in many biological membranes are known to orient parallel to magnetic fields. The value of the volume diamagnetic susceptibility anisotro~py, Ax (i.e. the difference between susceptibilities parallel and perpendicular to the direction of the hydrocarbon chain in the lecithin crystals), estimated from the magneto-orientation behavior was about -9 X 10-8 cgs. This is distinctly larger than that of vesicles of egg yolk lecithin measured by Boroske and Helfrich [Boroske, E. & Helfrich, W. (1978) Biophys. J. 24,863-868] and also larger than that of single crystals of polyethylene, which was measured for comparison by the same technique as that used for lecithin in this study. The differences between these values of AX seem to result from the contribution of the polar head (i.e., the part of the lecithin molecule other than the two hydrocarbon chains), which is ordered, less ordered, or deleted in the respective cases above, although mainly from the contribution of the hydrocarbon chains, which are ordered in crystals and disordered in vesicles.Suspensions of various biological membrane systems such as retinal-rod outer segments (1, 2), chloroplasts (3-6), and purple membranes from Halobacterium halobium (7) have been known to show magnetic field-induced orientation. All these systems align with the membrane normal parallel to the field direction, and it seems that this orientation effect is a common feature of biological membrane systems. In this effect, however, lecithin molecules, which are a major component of membranes, orient with their hydrocarbon chains parallel to the field; this orientation is contrary to the reported anisotropy of the magnetic susceptibility of hydrocarbon chains (8). The orientation effect, therefore, is assumed to be primarily caused by the anisotropy that results from oriented membrane proteins (9-11). The aim of this paper is to clarify the role of lecithin molecules in the magneto-orientation effect of biological membranes and to put it on a more quantitative basis. In the course of structure analysis of lecithins by x-ray and electron diffraction methods, we succeeded in making single crystals of lecithin, and we studied the effect of a magnetic field on lecithin crystals suspended in xylene. In the magnetic field, the crystals oriented in such a way that hydrocarbon-chain and phosphorylcholine-group directions, which are orthogonal to each other, are perpendicular to ...

Neuropeptide W (NPW) is a 30-amino-acid peptide initially isolated from the porcine hypothalamus as an endogenous ligand for the G protein-coupled receptors GPR7 and GPR8. An intracerebroventricular administration of NPW increased serum prolactin and corticosterone concentrations, decreased dark-phase feeding, raised energy expenditure, and lowered body weight. Peripherally, GPR7 receptors are abundantly expressed throughout the gastrointestinal tract; the presence of NPW in the gastrointestinal endocrine system, however, remains unstudied. Using monoclonal and polyclonal antibodies raised against rat NPW, we studied the localization of NPW in the rat, mouse, and human stomach by light and electron microscopy. NPW-immunoreactive cells were identified within the gastric antral glands in all three species. Double immunohistochemistry and electron-microscopic immunohistochemistry studies in rats demonstrated that NPW is present in antral gastrin (G) cells. NPW immunoreactivity localized to round, intermediate-to-high-density granules in G cells. NPWimmunoreactive cells accounted for 90% chromagranin A-and 85% gastrin-immunoreactive endocrine cells in the rat gastric antral glands. Using reversed-phase HPLC coupled with enzyme immunoassays specific for NPW, we detected NPW30 and its C-terminally truncated form, NPW23, in the gastric mucosa. Plasma NPW concentration of the gastric antrum was significantly higher than that of the systemic vein, suggesting that circulating NPW is derived from the stomach. Plasma NPW concentration of the gastric antrum decreased significantly after 15-h fast and increased after refeeding. This is the first report to clarify the presence of NPW peptide in the stomachs of rats, mice, and humans. In conclusion, NPW is produced in gastric antral G cells; our findings will provide clues to additional mechanisms of the regulation of gastric function by this novel brain/gut peptide.

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