For example it is clearly evident that rge birds suffer from glomerulopathy as the sections show enhanced glomerular size at the same magnification in comparison to wt kidney sections . Red blood cells were noted in the urinary filtration space of glomeruli . Abundant red blood cells were also seen in tubular lumina, and tubular injury with flattening of the tubular epithelium was associated with red blood cells in rge kidney sections but not in wt . There was a marked focal tubulo-interstitial inflammatory infiltrate, with lymphocytes and macrophages infiltrating tubules in rge kidney sections . In some, but not all, foci neutrophils were present in rge sections but not in wt . GNB3 immunohisto reactivity was totally diminished in the renal cells of the rge birds compared with an overt expression pattern of GNB3 in proximal convoluted tubule and glomerulus in wt sections . CoxIV, a mitochondrial protein, was present in both wt and rge sections confirming the reliability of the IHC technique . The GNB3 immuno reactivity order SB431542 results are consistent with our previous findings that the LDN-193189 D153del mutation affected GNB3 protein structure , stability, and cellular localisation with much shorter half-life than the normal GNB3 protein, as shown in our present degradation studies . Given the prominent GNB3 expression in rge kidney sections the related pathological finding observed in rge chickens are considered to be a primary genetic defect causing loss of function of a specific renal transport protein or signaling molecule. Consequently, the functional disturbances of certain tubule segments lead to defects in tubular reabsorption . The changes of GNB3 protein expression in whole kidney observed by Western blot likely reflect GNB3 expression, as observed in the IHC. Our results indicate that the D153del mutation results in an unstable GNB3d protein. This structurally abnormal protein is probably misfolded and targeted for early degradation by the cells ubiquitin proteasome system , when compared to the normal GNB3 protein. The lack of GNB3 protein in the cell machinery will probably inhibit trafficking and tethering of the Ga subunit to the plasma membrane and coatomer binding to the Golgi membranes . Recent studies on Gbc signalling in endomembranes of the cell have implied a role in protein transport through the trans Golgi network .