A mutation in the TRPC6 cation channel causes familial focal segmental glomerulosclerosis

Focal and segmental glomerulosclerosis (FSGS) is a kidney disorder of unknown etiology, and up to 20% of patients on dialysis have been diagnosed with it. Here we show that a large family with hereditary FSGS carries a missense mutation in the TRPC6 gene on chromosome 11q, encoding the ion-channel protein transient receptor potential cation channel 6 (TRPC6). The proline-to-glutamine substitution at position 112, which occurs in a highly conserved region of the protein, enhances TRPC6-mediated calcium signals in response to agonists such as angiotensin II and appears to alter the intracellular distribution of TRPC6 protein. Previous work has emphasized the importance of cytoskeletal and structural proteins in proteinuric kidney diseases. Our findings suggest an alternative mechanism for the pathogenesis of glomerular disease.     

Expression and function of junctional adhesion molecule-C in myelinated peripheral nerves

JAM-C is an adhesion molecule that is expressed on cells within the vascular compartment and epithelial cells and, to date, has been largely studied in the context of inflammatory events. Using immunolabeling procedures in conjunction with confocal and electron microscopy, we show here that JAM-C is also expressed in peripheral nerves and that this expression is localized to Schwann cells at junctions between adjoining myelin end loops. Sciatic nerves from JAM-C-deficient [having the JAM-C gene knocked out (KO)] mice exhibited loss of integrity of the myelin sheath and defective nerve conduction as indicated by morphological and electrophysiological studies, respectively. In addition, behavioral tests showed motor abnormalities in the KO animals. JAM-C was also expressed in human sural nerves with an expression profile similar to that seen in mice. These results demonstrate that JAM-C is a component of the autotypic junctional attachments of Schwann cells and plays an important role in maintaining the integrity and function of myelinated peripheral nerves.     

Response of cotton water stress indicators to soil salinity

Summary A field study was conducted on cotton (Gossypium hirsutum L. c.v. Acala SJ-2) to investigate the effects of soil salinity on the responses of stress indices derived from canopy temperature, leaf diffusion resistance and leaf water potential. The four salinity treatments used in this study were obtained by mixtures of aqueduct and well water to provide mean soil water electrical conductivities of 17, 27, 32 and 38 dS/m in the upper 0.6 m of soil profile. The study was conducted on a sandy loam saline-alkali soil in the lower San Joaquin Valley of California on 30 July 1981, when the soil profile was adequately irrigated to remove any interference of soil matric potential on the stress measurements. Measurements of canopy temperature, leaf water potential and leaf diffusion resistance were made hourly throughout the day.Crop water stress index (CWSI) estimates derived from canopy temperature measurements in the least saline treatment had values similar to those found for cotton grown under minimum salinity profiles. Throughout the course of the day the treatments affected CWSI values with the maximum differences occurring in mid-afternoon. Salinity induced differences were also evident in the leaf diffusion resistance and leaf water potential measurements. Vapor pressure deficit was found to indicate the evaporative demand at which cotton could maintain potential water use for the various soil salinity levels studied. At vapor pressure deficits greater than 5 kPa, cotton would appear stressed at in situ soil water electrical conductivities exceeding 15 dS/m. The CWSI was as sensitive to osmotic stress as other, more traditional plant measures, provided a broader spatial resolution and appeared to be a practical tool for assessing osmotic stress occurring within irrigated cotton fields.     

Elucidation of the effect of formaldehyde and lipids on frozen stored cod collagen by FT-Raman spectroscopy and differential scanning calorimetry

The effect of frozen storage (-10 and -30 degrees C), formaldehyde, and fish oil on collagen, isolated from cod muscle, was investigated. Salt- and acid-soluble collagen fractions as well as insoluble collagen indicated changes in solubility on frozen storage. Differential scanning calorimetry (DSC) showed a highly cooperative transition at 28.2 degrees C for isolated collagen. Changes in the thermodynamic properties of collagen were observed on frozen storage at -10 degrees C compared with the control at -30 degrees C because of changes in structure. In the presence of formaldehyde, there were no changes in the DSC collagen transition; however, in the presence of fish oil there was an increase in enthalpy and an extra peak was observed at 44.6 degrees C, indicating collagen-fish oil interaction. Structural changes resulted in a decrease in the solubility of collagen in salt and acid solution. FT-Raman spectra obtained for collagen at -10 degrees C and -30 degrees C confirmed the alteration of the conformation of collagen not only at -10 degrees C but also in the presence of formaldehyde and fish oil.