The intrinsic innervation of the kidney is described based on studies using ultrastructural, fluorescent, immunocytochemical, and autoradiographic techniques. The efferent sympathetic innervation reaches all the segments of the renal vasculature and to a much lesser extent the tubular nephron. The afferent renal nerves are localized predominantly in the pelvic region, the major vessels, and the corticomedullary connective tissue. The pathways of the renal innervation to the corresponding ganglia, as reported from observations resulting from the combination of axonal transport labeling and immunocytochemical methods, are presented. In the rat the ganglia of origin of the sympathetic efferent innervation include T13-L1 ipsilateral and contralateral paravertebral ganglia and the prevertebral superior mesenteric and celiac ganglia. The sensory afferent innervation presents a different segmental distribution of the dorsal root ganglia for the right and left kidney. For the left kidney, the corresponding ganglia extend from T8 to L2 with the greatest numbers in T12 and T13. For the right kidney, ganglia as high as T6 and as low as L2 harbor neurons innervating the kidney. Current knowledge of the anatomical bases of the function of the renal nerves is discussed.
Current information indicates that the mammalian kidney is a significant site of EGF synthesis, second only to the salivary gland in the rodent and probably exceeding most other tissues in the human species. The prepro EGF mRNA is localized to the cells of the TALH and the DCT. The EGF mRNA transcript in kidney is similar to that in salivary gland; the molecular mass of the prepro EGF protein in kidney approximates 130,000 kDa. Several EGF peptides are excreted in urine, including 6000-molecular weight peptides (composed of EGF 1-53, 1-52, 1-51, and 1-50) and a 30,000-molecular weight species with an aminoterminus portion corresponding to amino acids 829-848 of the prepro molecule. It has been suggested that prepro EGF could be a membrane protein since it contains an internal hydrophobic domain (amino acids 1039-1058) adjacent to the EGF sequence (amino acids 976-1029). The 30,000-molecular weight urinary product appears to represent a protein derived from amino acids 829 to approximately 1029 of prepro EGF, adjacent (distal) to the hydrophobic domain. Moreover, immunoelectron microscopy localizes the EGF immunoreactivity to the apical plasma membrane of the TALH and DCT cells. The molecular form of this apically localized, EGF immunoreactivity is not yet clear. Proximal, distal, and TALH cells of the renal tubules and renal medullary interstitial cells appear to have EGF receptors and respond to EGF with increased DNA synthesis and mitogenesis. Also, there is a relatively late increase in prepro EGF mRNA levels in TALH and DCT cells during the process of renal hypertrophy. Limited evidence suggests a role of EGF on tubular function mediated via basal EGF receptors. EGF peptides processed intracellularly or by membrane localized peptidases appear to be continuously excreted and secreted into urine from the apical membrane surface of the TALH and DCT cells. This urinary EGF is constantly bathing urinary tract epithelial surfaces and could play a role in maintaining surface integrity. A similar role for salivary gland EGF in saliva has been proposed for the gastrointestinal tract. It also is possible that prepro EGF is anchored in the apical membrane, where it could function as a receptor, and a role for renal tubular EGF in regulation of membrane transport events has been proposed.
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