Kidney proteins

Witzmann FA et al. Toxicity of chemical mixtures proteomic analysis of persisting liver and kidney protein alterations induced by repeated exposure of rats to... 

Hydrocephaly decreases in weight of brain, lung, liver, and kidney decreases in liver glycogen, kidney proteins and alkaline phosphatase and disrupted brain DNA and protein metabolism (Kav-lock et al. 1982)... 

Pharmacokinetics Rapidly absorbed from the G1 tract, ffighest concentration is in the liver, spleen, and kidney. Protein binding 30%-50%. Reenters the intestinal tract by biliary secretion and is reabsorbed from the intestines. Partially metabolized in the liver. Eliminated primarily in feces. 

Figure 5.7. Schematic representation of therapeutic protein (A) being filtered and (B) metabolized in the kidneys. Protein reabsorption in proximai tabie is iimited.

Rutin, quercetin 3-rutinoside, i.e., 3-rhamnoglucoside, has been reported to suppress glycation,609 but it is only sparingly soluble in water. Nagasawa el al.6W have therefore examined the water-soluble 4G-a-D-glucopyranosyl derivative (G-rutin), obtained from a sugar factory. Streptozotocin-treated rats were fed for 4 weeks on a 20% casein diet, when they showed an increase in fructosyllysine obtained on hydrolysis of their protein however, when their diet had been supplemented with 0.2% G-rutin, the increase was reduced by 20% for kidney protein. Supplementation reduced AGE accumulation, as measured with an anti-AGE monoclonal antibody, in the serum and kidney proteins to the level of the control rats. Supplementation inhibited aldose reductase activity in the kidney, but not in the liver. 

Other derivatives of lysine, c-(y-glytamyl) lysine and c-formyllysine, are hydrolyzed in the kidneys, and the lysine moiety is regenerated and incorporated into the kidney proteins in the cells where hydrolysis occurs. No retention of radioactivity occurs with derivatives such as a-formyl-14C-lysine which is not hydrolyzed in the kidneys (83) (see Figure 2). At present, we do not know yet whether these derivatives of lysine induce nephrocytomegaly. 

The assay was used to measure enzyme activity in dialyzed cytosolic fractions from rat kidney (protein concentration 2 mg/mL) and in rat kidney mitochondria (protein concentration 3 mg/mL). 

Cappellano, F., FIughes, G., etal. (1997). Renal cell carcinoma and normal kidney protein expression. Electrophoresis 18, 599-604. 

Swine kidney protein kinase Posphoenolpyruvate carboxy-kinase (GTP)... 

Mudge GH, Gemborys MW, Duggin GG. Covalent binding of metabolites of acetaminophen to kidney protein and depletion of renal glutathione. J Pharmacol ExpTher 1978 206 218-226. 

D-Fructose 6-phosphate and ammonia interact to produce hexosamine when they are added to a fraction of pig-kidney protein together with catalytic amounts of A -acetyl-n-glucosamine 6-phosphate. Neither L-glutamine nor L-asparagine can replace ammonium sulfate as a nitrogen source in this system, and D-fructose 6-phosphate cannot be replaced by D-fructose, n-xylose, n-glucose, or D-ribose. The presence of N-acetyl-D-glucosamine is also essential for this reaction. 

Unlike fractions of pig-kidney protein, Neurospora crassa extracts can use L-glutamine, but not ammonium salts nor ammonium salts plus adeno-sine-5-triphosphoric acid. No synthesis of D-glucosamine is stimulated in Neurospora extracts by L-glutamic acid, L-aspartic acid, L-asparagine, L-alanine, glycine, L-valine, L-leucine, L-lysine, L-arginine, L-serine, L-cys-teine, L-citrulline, L-ornithine, butyramide, putrescine, or urea. Recently, a protein fraction has been discovered, in rat liver, that converts D-glucose... 

Jorgensen and Majumdar125 reported that a single tube-feeding of L-tryp-tophan to well-fed adrenalectomized rats stimulated in vivo incorporation of [3H]leucine into kidney proteins. 

The administration of TNT to laboratory animals leads to the excretion of 4-NHOH-DNT, 2-NH2-DNT, and 4-NH2-DNT in the urine [59], and to the formation of covalent adducts with microsomal liver and kidney proteins, hemoglobin, and other blood proteins [60], The acid hydrolysis of adducts yielded mainly 2-NH2-DNT (2-ADNT) and 4-NH2-DNT (4-ADNT). Incubation of rat liver microsomes with TNT and NADPH under aerobic conditions resulted in the formation of NH2-DNTs and the transient metabolite 4-NHOH-DNT [57], The formation of covalent protein adducts with TNT metabolites was enhanced by the presence of 02 and decreased by GSH. This is consistent with the scheme of the TNT adduct formation with the central role of the nitroso metabolite (NO-DNT) reaction with protein or nonprotein thiols (RSH Equation 9.11) [57], The acid hydrolysis of the sulfinamide adduct (RS(0)-NH-DNT) formed after the rearrangement of the semimercaptal (RS-N(OH)-DNT Equation 9.12) will yield NH2-DNT. The mixture of NHOH-DNTs inhibits bacterial glyceraldehyde-3-phosphate dehydrogenase and glucose-6-phosphate dehydrogenase more efficiently than TNT [61]. This was attributed to the covalent modification of protein -SH groups. 

Witzmann, F.A., R.L. Carpenter, G.D. Ritchie, C.L. Wilson, A.F. Nordholm, and J. Rossi III. 2000. Toxicity of chemical mixtures Proteomic analysis of persisting liver and kidney protein alterations induced by repeated exposure of rats to JP-8 jet fuel vapor. Electrophoresis 21 (11) 2138-2147. 

Life is a conquest for energy. Energy is required for practically all life processes—for the action of the heart, maintenance of blood pressure and muscle tone, transmission of nerve impulses, ion transport across membranes, reabsorption in the kidneys, protein and fat synthesis, the secretion of milk, and muscular contraction. A deficiency of energy is manifested by slow or stunted growth, body tissue losses, and/or weakness. 

At the same time, mass spectrometry offered exquisite details on the mass and structure of small (<5000 Da) molecules but was unable to efficiently ionize larger ones. The dilemma of the mid-1980s is illustrated in Fig. 1. The results of a two-dimensional gel electrophoresis separation of kidney proteins showed a wealth of information in the >5000 Da range. Results from mass spectrometry, however, left off all molecular species in this region. The lack of efficient ion sources for these molecules started a decade-long race to produce gas-phase ions from ever larger molecules. This quest culminated in the discovery of electrospray ionization (ESI) and matrix-assisted laser desorption ionization (MALDI) by the end of the decade. Almost overnight, molecules with masses in excess of 100 kDa could be studied by... 

The sulfur present in different liver and plasma protein fractions (pseudoglobulin, euglobulin, albumin 1, and albumin 2) has the same specific activity, while the specific activity of cystine is found to be only two-thirds of the specific activity of methionine. From this result it is apparent that the conversion of methionine sulfur to cystine sulfur is not a slow process. Radioactive cystine is found in liver and kidney proteins. 

---