Hypothetical mechanisms have been postulated to explain the presence of proteins in urine after severe exercise. Recently, it has been shown that several amino acids inhibit tubular protein reabsorption. Seven healthy men, hyperhydrated, were studied during a 2-min bicycle exercise at supramaximal load. The subjects were tested without or with lysine perfusion (0.4 g/kg body wt iv). In both testing conditions, blood lactate increased to 13.8 mmol/l. Total protein urinary excretion increased to 1.10 and 1.67 mg/min, without and with lysine perfusion, compared with 79 micrograms/min at rest. In the meantime, albumin excretion increased 48- and 74-fold, respectively, while beta 2-microglobulin excretion increased 97- and 1,043-fold compared with basal values. The renal clearance of albumin increased to 8.4 microliters/min without lysine and to 12.0 microliters/min with lysine perfusion (rest 0.18). beta 2-Microglobulin clearance increased to 10.0 and 39.3 ml/min, respectively (rest 0.05). These data clearly demonstrate that postexercise proteinuria is of mixed type after exhaustive short-term exertion. Both increased glomerular permeability and partial tubular reabsorption inhibition to proteins appear to be involved.
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http://dx.doi.org/10.1152/ajprenal.1988.254.2.F277 | DOI Listing |
Arterioscler Thromb Vasc Biol
February 2025
Department of Pediatrics (T.S., J.-R.M., Y.H.C., J.M.S., J. Kaplan, A.C., L.W., D.G., S.T., S.I., M.D., W.Y., A.L.M., M.R.).
Background: Computational modeling indicated that pathological high shear stress (HSS; 100 dyn/cm) is generated in pulmonary arteries (PAs; 100-500 µm) in congenital heart defects causing PA hypertension (PAH) and in idiopathic PAH with occlusive vascular remodeling. Endothelial-to-mesenchymal transition (EndMT) is a feature of PAH. We hypothesize that HSS induces EndMT, contributing to the initiation and progression of PAH.
View Article and Find Full Text PDFNat Commun
October 2024
Department of Molecular Medicine, The Scripps Research Institute, La Jolla, California, USA.
Mass spectrometry-based methods can provide a global expression profile and structural readout of proteins in complex systems. Preserving the in vivo conformation of proteins in their innate state is challenging during proteomic experiments. Here, we introduce a whole animal in vivo protein footprinting method using perfusion of reagents to add dimethyl labels to exposed lysine residues on intact proteins which provides information about protein conformation.
View Article and Find Full Text PDFBackground: Angiotensin-II (Ang-II) perfusion stimulates Kir4.1/Kir5.1 in the distal-convoluted-tubule (DCT) and thiazide-sensitive Na-Cl-cotransporter (NCC).
View Article and Find Full Text PDFCurr Eye Res
November 2024
Zunyi Medical University, Zunyi City, Guizhou Province, China.
Purpose: To investigate the effect of reducing Lysyl oxidase (LOX) overexpression on retinal ganglion cells (RGCs) apoptosis in an acute ocular hypertension (AOH) rat model.
Methods: AOH rat model was performed by anterior chamber perfusion and either received an intravitreal injection with β-aminopropionitrile (BAPN) or normal saline. After 2wk, Quantification of survival RGCs in the retina was performed using Retrograde FluoroGold labeling.
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