Trace-element concentrations in human autopsy tissue.

Aalbers, Th.G.; Houtman, J.P.W.; Makkink, B.

doi:10.1093/clinchem/33.11.2057

Cited by 46 publications

(9 citation statements)

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“…Studies on copper have been conducted for many years [1, 5, 11, 30]. However, little data is available, especially on human pathologically altered kidneys, including renal grafts.…”

Section: Discussionmentioning

confidence: 99%

Comparison of Copper Concentration Between Rejected Renal Grafts and Cancerous Kidneys

Wilk

Wiszniewska

Rzuchowska

et al. 2019

Biol Trace Elem Res

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In the body, disorders in the composition and concentration of trace elements, including copper, can lead to the development of various alterations that may result in incorrect functioning of the kidneys. Data on the concentrations of copper in human kidneys are discussed; however, little is known about the concentration of trace elements within rejected renal grafts and kidneys with tumor lesions. The aim of our study was to compare the copper concentration between cancerous kidneys and rejected renal grafts with the division on renal cortex and renal medulla. Material consisted of kidneys from patients hospitalized at the Department of Urology and General Surgery and Transplantation of the Independent Public Clinical Hospital No. 2 at the Pomeranian Medical University in Szczecin, north-western Poland. The study material consisted of kidneys with tumor lesions ( n = 33), and renal grafts ( n = 10), obtained from patients belongs to the north-western areas of Poland. The examination was performed using ICP-AES method. Regarding the pathological kidneys, excluding grafts, the concentration of Cu in the renal cortex was 52% higher than in medullary region and the difference between the compared concentrations was statistically confirmed ( p < 0.05). Taking into account renal grafts, the concentration of Cu in the medulla was slightly lower than in the cortex (less than 3%). In summary, copper in rejected and cancerous kidneys tends to accumulate in higher amount in the renal cortex than medulla, what can be explained by the fact that renal corpuscles, where the first phase of filtration is performed, are located only in the cortical region of the kidney. Furthermore, renal grafts accumulate significantly less copper than kidneys with neoplastic changes, what could have been caused by immunosuppressive medicines used by the graft recipients. The lower copper concentration in renal grafts could be a consequence of the altered immune system, including inflammatory process or/and non-immune mechanisms. Additionally, cancerous and non-cancerous kidneys exhibit different perfusion rate in renal glomeruli, what can finally lead to disparity in chemical elements concentration, including copper.

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“…Studies on copper have been conducted for many years [1, 5, 11, 30]. However, little data is available, especially on human pathologically altered kidneys, including renal grafts.…”

Section: Discussionmentioning

confidence: 99%

Comparison of Copper Concentration Between Rejected Renal Grafts and Cancerous Kidneys

Wilk

Wiszniewska

Rzuchowska

et al. 2019

Biol Trace Elem Res

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“…A careful evaluation of the data reported in the literature about the dissociation constants measured for the readily exchangeable site of blLAP ( K Mn 2+ / K Zn 2+ = 35) () and the intracellular Zn 2+ and Mn 2+ concentration values in various tissues ( − ) suggests that the most abundant enzyme form is probably (Zn/Zn)blLAP. However, independent from the relative amount of the two blLAP forms, a specific cysteinylglycine-hydrolyzing activity was clearly measured in lens homogenates, purified, and identified as being associated with (Mn/Zn)blLAP ().…”

Section: Discussionmentioning

confidence: 99%

Metal Ion Substitution in the Catalytic Site Greatly Affects the Binding of Sulfhydryl-Containing Compounds to Leucyl Aminopeptidase^,

et al. 2006

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Bovine lens leucyl aminopeptidase (blLAP), a homohexameric metallopeptidase preferring bulky and hydrophobic amino acids at the N-terminus of (di)peptides, contains two Zn(2+) ions per subunit that are essential for catalytic activity. They may be replaced by other divalent cations with different exchange kinetics. The protein readily exchangeable site (site 1) can be occupied by Zn(2+), Mn(2+), Mg(2+), or Co(2+), while the tight binding site (site 2) can be occupied by Zn(2+) or Co(2+). We recently reported that introduction of Mn(2+) into site 1 generates a novel activity of blLAP toward CysGly [Cappiello, M., et al. (2004) Biochem. J. 378, 35-44], which in contrast is not hydrolyzed by the (Zn/Zn) enzyme. This finding, while disclosing a potential specific role for blLAP in glutathione metabolism, raised a question about the features required for molecules to be a substrate for the enzyme. To clarify the interaction of the enzyme with sulfhydryl-containing derivatives, (Zn/Zn)- and (Mn/Zn)blLAP forms were prepared and functional-structural studies were undertaken. Thus, a kinetic analysis of various compounds with both enzyme forms was performed; the crystal structure of (Zn/Zn)blLAP in complex with the peptidomimetic derivative Zofenoprilat was determined, and a modeling study on the CysGly-(Zn/Zn)blLAP complex was carried out. This combined approach provided insight into the interaction of blLAP with sulfhydryl-containing derivatives, showing that the metal exchange in site 1 modulates binding to these molecules that may result in enzyme substrates or inhibitors, depending on the nature of the metal.

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“…However, of the elements analyzed in our study, only Na concentration may increase with latency (measured in human heart-muscle up to 50 hours) of post-mortem autolysis (Aalbers et al 1987). Furthermore, intracellular elements and proteinbound trace elements are not vulnerable to autolysis (Aalbers et al 1987). One may speculate that postmortem processes include decomposition of the digestive system along with their content, resulting in an additional factor influencing the level of some elements in adjacent tissues, especially in species with small body size (like some birds or nestlings).…”

Section: Discussionmentioning

confidence: 52%

“…autolysis) that are associated with tissue swelling and destruction of cellular structures. However, of the elements analyzed in our study, only Na concentration may increase with latency (measured in human heart-muscle up to 50 hours) of post-mortem autolysis (Aalbers et al 1987). Furthermore, intracellular elements and proteinbound trace elements are not vulnerable to autolysis (Aalbers et al 1987).…”

Section: Discussionmentioning

confidence: 57%

Relationships between stomach content and concentrations of essential and non-essential elements in tissues of omnivorous nestling rooksCorvus frugilegus: Is the size and composition of stomach content relevant?

et al. 2013

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Trace-element concentrations in human autopsy tissue.

Cited by 46 publications

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Comparison of Copper Concentration Between Rejected Renal Grafts and Cancerous Kidneys

Comparison of Copper Concentration Between Rejected Renal Grafts and Cancerous Kidneys

Metal Ion Substitution in the Catalytic Site Greatly Affects the Binding of Sulfhydryl-Containing Compounds to Leucyl Aminopeptidase^,

Relationships between stomach content and concentrations of essential and non-essential elements in tissues of omnivorous nestling rooksCorvus frugilegus: Is the size and composition of stomach content relevant?

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Trace-element concentrations in human autopsy tissue.

Cited by 46 publications

References 0 publications

Comparison of Copper Concentration Between Rejected Renal Grafts and Cancerous Kidneys

Comparison of Copper Concentration Between Rejected Renal Grafts and Cancerous Kidneys

Metal Ion Substitution in the Catalytic Site Greatly Affects the Binding of Sulfhydryl-Containing Compounds to Leucyl Aminopeptidase,

Relationships between stomach content and concentrations of essential and non-essential elements in tissues of omnivorous nestling rooksCorvus frugilegus: Is the size and composition of stomach content relevant?

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Metal Ion Substitution in the Catalytic Site Greatly Affects the Binding of Sulfhydryl-Containing Compounds to Leucyl Aminopeptidase^,