Zinc in kidney

Impalas (Aepyceros melampus) found dead in Kruger National Park, South Africa, had elevated concentrations of copper in livers (maximum 444 mg/kg FW) and kidneys (maximum 141 mg/kg FW) authors assert that copper poisoning is the most likely cause of death (Gummow et al. 1991), but this needs verification. Copper concentrations in bones, kidneys, and livers of white-tailed deer (Odocoileus virginianus) near a copper smelter and from distant sites are about the same. However, deer near the smelter have significantly elevated concentrations of cadmium in kidneys and livers, lead in bone, and zinc in kidneys (Storm et al. 1994). 

Ellen, G., J.W. van Loon, and K. Tolsma. 1989. Copper, chromium, manganese, nickel and zinc in kidneys of cattle, pigs and sheep and in chicken livers in the Netherlands. Zeit. Lebens. Untersuchung Forschung 189 534-537. 

Fig. 5.7. (A) Assembly used in the determination of cadmium and zinc in kidney and liver tissue by simultaneous microwave-assisted acid digestion of 6 samples, FI and AAS CT collector tube, FS flowing sample collector, R recorder. (B) Experimental design for the continuous microwave-assisted leaching, liquid-liquid extraction, sorption/clean-up of phenol compounds in soil samples IV, injection valve, PS membrane phase separator, o.p. and a.p. organic and aqueous phase, W waste. (Reproduced with permission of Elsevier.)...

Mogilnicka, E.M. and Webb, M. (1981) Comparative studies on the distribution of gold, copper and zinc in the livers and kidneys of rats and hamsters after treatment with sodium gold-195-labeled-aurofhiomalate. Journal of Applied Toxicology, 1, 287—291. 

There is a protein, metallothionine, which is found in kidney and which binds cadmium and zinc very effectively. This may well be related to the bacterial protein. We see that biological systems have developed highly selective ways of countering the influence of poisonous metals. The protection involves the interaction between a selected protein and a given metal. We can now return to platinum chemistry. 

Gerhardsson L, Brune D, Nordberg GF, et al. 1986a. Distribution of cadmium, lead, and zinc in lung, liver, and kidney in long-term exposed smelter workers. Sci Total Environ 50 65-85. 

Pedersen, H.C. and I. Myklebust. 1993. Age-dependent accumulation of cadmium and zinc in the liver and kidneys of Norwegian willow ptarmigan. Bull. Environ. Contam. Toxicol. 51 381-388. 

In birds, copper and zinc concentrations are positively correlated in kidneys of the willow ptarmigan (Lagopus lagopus, Wren et al. 1994) and in kidneys and livers of common murres (Uria aalge Stewart et al. 1994). 

Newt, Triturus cristatus, adults, held in tank with a zinc-plated base South African clawed frog, Xenopus laevis 200 to 3000 overa 7-day period Zinc-poisoned newts were lethargic, ate poorly, and had skin darkening prior to death. Zinc residues were elevated in kidney, brain, liver, and intestine, when compared to controls. The hippocampus region of the brain of poisoned newts contained zinc-rich cells 82... 

All dead at 16,000 mg/kg diet. The 8000 mg/kg group had 80% mortality survivors had significantly reduced growth and feed conversion. At 4000 mg/kg, no significant effect on growth or survival zinc concentrations elevated in kidney, liver, intestinal mucosa, and pancreas— but values normal after 10 days on basal diet (Oh et al. 1979). 

Hens started to molt and ceased laying. Feed intake decreased about 90%. Zinc concentrations in pancreas increased 7-fold, in liver 6-fold, kidney 3-fold, and were elevated in shell gland and yolk. High Zn levels in kidney reflect high Zn excretion rates high pancreatic Zn (410 mg Zn/kg FW) may suppress the release of insulin by calmodulin inhibition, and could account for the rapid cessation of lay (Verheyen etal. 1990). 

Domestic ewe, age 5 years, found moribund, suspected zinc poisoning Elevated zinc levels (mg/kg DW) in liver of 650 vs. 144 in controls, and in kidney 760 vs. 84 in controls muscle residues same as controls, i.e., 154 vs. 158 generalized jaundice liver degeneration and blockage of bile ducts. 18... 

Found dead, zinc-poisoned naturally Zinc concentrations, in mg/kg DW, were 463 in liver (vs. 165 in controls), 274 in kidney (vs. 150 in controls), and 752 in pancreas (vs. 88 in controls). 19... 

Although tissue residues are not yet reliable indicators of zinc contamination, zinc poisoning usually occurs in birds when liver or kidney contains >2.1 g Zn/kg DW, and in mammals when concentrations, in mg Zn/kg DW, exceed 274 in kidney, 465 in liver, or 752 in pancreas. The proposed air quality criterion for human health protection is <5 mg Zn/m3, but guinea pigs were more sensitive with adverse effects evident at >0.8 to 4.0 mg/m3. 

Holterman, W.F.M.O., P. de Voogt, and J.H.J.C. Peereboom-Stegeman. 1984. Cadmium/zinc relationships in kidney cortex and metallothionein of horse and red deer histopathological observations on horse kidneys. Environ. Res. 35 466-481. 

Wood, C.M. and E.S. Van Vleet. 1996. Copper, cadmium and zinc in liver, kidney and muscle tissues of bottlenose dolphins (Tursiops truncatus) stranded in Florida. Mar. Pollut. Bull. 32 886-889. 

Finally we should briefly mention the purple acid phosphatases, which, unlike the alkaline phosphatases, are able to hydrolyse phosphate esters at acid pH values. Their purple colour is associated with a Tyr to Fe(III) charge transfer band. The mammalian purple acid phosphatase is a dinuclear Fe(II)-Fe(III) enzyme, whereas the dinuclear site in kidney bean purple acid phosphatase (Figure 12.13) has a Zn(II), Fe(III) centre with bridging hydroxide and Asp ligands. It is postulated that the iron centre has a terminal hydroxide ligand, whereas the zinc has an aqua ligand. We do not discuss the mechanism here, but it must be different from the alkaline phosphatase because the reaction proceeds with inversion of configuration at phosphorus. 

Carbonate anhydrase (carbonic anhydrase, EC 4.2.1.1) catalyzes the reversible interconversion of C02 and HCO3 (see Sect. 3.7.3). The enzyme is found in erythrocytes, and in kidney and gastric juices where it contributes to the control of the acid-base balance. The esterase activity of carbonic anhydrase is probably due to the similarity between its active site and that of the zinc proteases. A possible physiological role of the esterase activity of this enzyme remains to be established. 

---