Characterization and Clinical Significance of Membrane Bound Proteases from Human Kidney Cortex

1984 ◽  
pp. 179-190 ◽  
Author(s):  
J. Scherberich ◽  
C. Gauhl ◽  
G. Heinert ◽  
W. Mondorf ◽  
W. Schoeppe
Keyword(s):  
Clinical Significance ◽  
Human Kidney ◽  
Kidney Cortex ◽  
Membrane Bound

scholarly journals Nuclear Expression and DNA Binding Capacity of Receptor for Advanced Glycation End Products in Renal Tissue

2019 ◽  
Author(s):  
Brooke E. Harcourt ◽  
Aaron D. McClelland ◽  
Hiroshi Yamamoto ◽  
Hideto Yonekura ◽  
Yasuhiko Yamamoto ◽  
...  
Keyword(s):  
Dna Sequences ◽  
Binding Capacity ◽  
Self Regulation ◽  
Gene Promoter ◽  
Human Kidney ◽  
Renal Tissue ◽  
Kidney Cortex ◽  
Soluble Rage ◽  
Membrane Bound

AbstractThe AGER gene encodes for a number of RAGE isoforms, with the membrane bound signal transduction and “decoy” circulating soluble RAGE being the best characterised. Here we demonstrate a novel nuclear isoform of RAGE in mice and human kidney cortex which by cell and size fractionation we determined to be approximately 37kda. This nuclear RAGE isoform is functional and binds to DNA sequences within the upstream 5’ promoter region of its own gene, AGER. This binding was shown to be abrogated by mutating the DNA consensus binding sequences during electromobility shift assay (EMSA) and was independent of NF-□B or AP-1 binding. Cotransfection of expression constructs encoding various RAGE isoforms along with AGER gene promoter reporter-plasmids identified that the most likely source of the nuclear isoform of RAGE was a cleavage product of the nt-RAGE isoform. In obese mice with impaired kidney function, there was increased binding of nuclear RAGE within the A. Region of ager gene promoter with corresponding increases in membrane bound RAGE in renal cells. These findings were reproduced in vitro using proximal tubule cells. Hence, we postulate that RAGE expression is in part, self-regulated by the binding of a nuclear RAGE isoform to the promoter of the AGER gene (encoding RAGE) in the kidney. We also suggest that this RAGE self-regulation is altered under pathological conditions and this may have implications for chronic kidney disease.

17-Oxidoreduction of 17β-Estradiol, Estrone and Their 3-Sulfates by Kidney Slices from Guinea Pig and Human

1975 ◽  
Vol 53 (12) ◽  
pp. 1333-1336 ◽  
Author(s):  
R. Hobkirk ◽  
Mona Nilsen ◽  
Barbara Jennings
Keyword(s):  
Guinea Pig ◽  
Marked Reduction ◽  
Human Kidney ◽  
Kidney Cortex ◽  
Limited Extent ◽  
Tissue Slices ◽  
Ample Evidence ◽  
Sulfatase Activity ◽  
17Β Estradiol ◽  
Dehydrogenation Reactions

Slices of whole kidney and kidney cortex from the female guinea pig catalyzed a marked reduction of estrone 3-sulfate (E13S) and estrone (E1) to 17β-estradiol 3-sulfate (E23S) and 17β-estradiol (E2), respectively, as well as the reverse (dehydrogenation) reactions. Slices of medulla did not appear active in E23S–E13S interconversion but did possess the ability to interconvert E2 and E1, besides possessing considerable sulfatase activity. The use of [3H-35S]E13S and [3H-35S]E23S as substrates, together with a demonstrated lack of estrogen sulfate synthesis by the tissue slices, provided ample evidence that the intact sulfates were involved in direct oxidoreduction. Slices of human kidney cortex catalyzed the reduction of E13S to a very limited extent. Slices of whole kidney and of cortex from guinea pig formed small amounts of estrogen glucuronide(s).

scholarly journals Detection of hematopoietic stem cell transcriptome in human fetal kidneys and kidney organoids derived from human induced pluripotent stem cells (iPSC)

2021 ◽  
Author(s):  
Jin Wook Hwang ◽  
Christophe Desterke ◽  
Julien Loisel-Duwattez ◽  
Frank Griscelli ◽  
Annelise Bennaceur-Griscelli ◽  
...  
Keyword(s):  
Stem Cells ◽  
Fetal Liver ◽  
Human Kidney ◽  
Kidney Cortex ◽  
Hematopoietic Stem ◽  
Adult Kidney ◽  
Whole Transcriptome Analysis ◽  
Induced Pluripotent ◽  
Cell Transcriptome ◽  
Kidney Organoids

AbstractBackgroundIn mammalians, hematopoietic stem cells (HSC) arise in the dorsal aorta from the hemogenic endothelium, followed by their migration to fetal liver and to bone marrow. In zebrafish, kidney is the site of primary hematopoiesis. In humans, the presence of HSC in the fetal or adult kidney has not been established.MethodsWe analyzed the presence of HSC markers in human fetal kidneys by analysis of single-cell datasets. We then analyzed in kidney organoids derived from iPSC, the presence of hematopoietic markers using transcriptome analyses.Results12 clusters were identified of stromal, endothelial, and nephron cell type-specific markers in the two fetal stage (17 weeks) kidney datasets. Among these, expression of hematopoietic cells in Cluster 9 showed expression of primitive markers. Moreover, whole transcriptome analysis of our iPSC-derived kidney organoids revealed induction of the primitive hematopoietic transcription factor RUNX1 as found in the human fetal kidney cortex.ConclusionsThese finding support the presence of cells expressing HSC transcriptome in human kidney. The mechanisms of the appearance of the cells with the same transcriptional features during iPSC-derived kidney organoid generation requires further investigation.

Polarized Zeeman-effect flameless atomic absorption spectrometry of cadmium, copper, lead, and manganese in human kidney cortex.

1981 ◽  
Vol 27 (1) ◽  
pp. 68-72 ◽  
Author(s):  
P A Pleban ◽  
J Kerkay ◽  
K H Pearson
Keyword(s):  
Atomic Absorption ◽  
Zeeman Effect ◽  
Human Kidney ◽  
Absorption Spectrometry ◽  
Kidney Cortex ◽  
Flameless Atomic Absorption ◽  
Flameless Atomic Absorption Spectroscopy ◽  
Coefficients Of Variation ◽  
Cadmium And Lead ◽  
Copper Lead

Abstract We used polarized Zeeman-effect flameless atomic absorption spectroscopy to quantitatively measure cadmium, copper, lead, and manganese in a nitric acid digest of lyophilized human kidney cortex. Within-run coefficients of variation for cadmium, copper, lead, and manganese, 15.3, 177.2, 84.2, and 56.3 microgram/L, respectively, were 4.1, 6.3, 3.7, and 5.6%, respectively. Between-run coefficients of variation were 6.9, 5.5, 5.9, and 6.3%, respectively, for cadmium, copper, lead, and manganese concentrations of 135.1, 12.8, 2.72, and 3.80 microgram/g, respectively. For cadmium, copper, lead, and manganese digest concentrations (mean +/- SE) of 15.3 +/- 0.6, 41.4 +/- 2.6, 9.4 +/- 0.6, and 20.9 +/- 0.4 microgram/L, respectively, the detection limits were 5.2 microgram/L for copper, 1.2 microgram/L for both cadmium and lead, and 0.8 microgram/L for manganese. Assays were linear to 75 microgram/L for cadmium, 100 microgram/L for manganese, and 200 microgram/L for copper and lead. Average analytical recoveries for the four metals ranged between 95 and 101%. Because these metals were quantitated in the same digest of kidney cortex, the values for each digest gave a trace-metal profile for each autopsy specimen.

Cloning, sequencing, and expression of Na(+)-H+ antiporter cDNAs from human tissues

1992 ◽  
Vol 262 (4) ◽  
pp. C1069-C1076 ◽  
Author(s):  
K. Takaichi ◽  
D. Wang ◽  
D. F. Balkovetz ◽  
D. G. Warnock
Keyword(s):  
Plasma Membranes ◽  
Mutant Mouse ◽  
Human Kidney ◽  
Kidney Cortex ◽  
Human Tissues ◽  
Specific Expression ◽  
Reading Frame ◽  
Mouse Fibroblasts ◽  
Cloned Cdna ◽  
Sequencing And Expression

Two types of Na(+)-H+ antiporter with different sensitivities to amiloride analogues have been identified in mammalian plasma membranes. A human Na(+)-H+ antiporter cDNA was obtained by Sardet and co-workers (C. Sardet, L. Counillon, A. Franchi, and J. Pouyssegur. Cell 56: 271-280, 1989) using mutant mouse fibroblasts lacking Na(+)-H+ antiporter transformed with human genomic DNA. However, the amiloride sensitivity of this cloned Na(+)-H+ antiporter was not precisely determined. Furthermore, the reported cDNA sequence may be a chimera of human and mouse genes. Hence we isolated a Na(+)-H+ antiporter cDNA actually expressed in human tissues and characterized its amiloride sensitivity. Our 4 kb cDNA obtained from human kidney cortex contained the identical open reading frame to that previously reported and the entire 3' terminus, which was quite different from that reported. This discrepancy was not due to differences in tissue-specific expression because cDNAs from different human tissues were identical, and single bands were observed under high stringency on Northern blots of various human tissues. Na(+)-H+ antiporter activity of mutant mouse fibroblasts deficient in Na(+)-H+ antiporter activity transfected with the cloned cDNA was very sensitive to amiloride and 5-N substituted analogues of amiloride. Thus the cloned cDNA represents the NHE-1 isoform of the Na(+)-H+ antiporter.

scholarly journals Reduced cadmium levels in human kidney cortex in sweden.

1998 ◽  
Vol 106 (4) ◽  
pp. 175-178 ◽  
Author(s):  
L Friis ◽  
L Petersson ◽  
C Edling
Keyword(s):  
Human Kidney ◽  
Kidney Cortex

scholarly journals Characterization of a secretase activity which releases angiotensin-converting enzyme from the membrane

1993 ◽  
Vol 292 (2) ◽  
pp. 597-603 ◽  
Author(s):  
S Y Oppong ◽  
N M Hooper
Keyword(s):  
Angiotensin Converting Enzyme ◽  
Human Kidney ◽  
Soluble Form ◽  
Converting Enzyme ◽  
Ph Optimum ◽  
Secretase Activity ◽  
Sds Page ◽  
Microsomal Membranes ◽  
Membrane Bound ◽  
Triton X

Angiotensin-converting enzyme (ACE; EC 3.4.1.15.1) exists in both membrane-bound and soluble forms. Phase separation in Triton X-114 and a competitive e.l.i.s.a. have been employed to characterize the activity which post-translationally converts the amphipathic, membrane-bound form of ACE in pig kidney microvilli into a hydrophilic, soluble form. This secretase activity was enriched to a similar extent as other microvillar membrane proteins, was tightly membrane-associated, being resistant to extensive washing of the microvillar membranes with 0.5 M NaCl, and displayed a pH optimum of 8.4. The ACE secretase was not affected by inhibitors of serine-, thiol- or aspartic-proteases, nor by reducing agents or alpha 2-macroglobulin. The metal chelators, EDTA and 1,10-phenanthroline, inhibited the secretase activity, with, in the case of EDTA, an inhibitor concentration of 2.5 mM causing 50% inhibition. In contrast, EGTA inhibited the secretase by a maximum of 15% at a concentration of 10 mM. The inhibition of EDTA was reactivated substantially (83%) by Mg2+ ions, and partially (34% and 29%) by Zn2+ and Mn2+ ions respectively. This EDTA-sensitive secretase activity was also present in microsomal membranes prepared from pig lung and testis, and from human lung and placenta, but was absent from human kidney and human and pig intestinal brush-border membranes. The form of ACE released from the microvillar membrane by the secretase co-migrated on SDS/PAGE with ACE purified from pig plasma, thus the action and location of the secretase would be consistent with it possibly having a role in the post-translational proteolytic cleavage of membrane-bound ACE to generate the soluble form found in blood, amniotic fluid, seminal plasma and other body fluids.

scholarly journals Different handling of parathyrin by basal-lateral and brush-border membranes of the bovine kidney cortex

1980 ◽  
Vol 188 (3) ◽  
pp. 649-656 ◽  
Author(s):  
H Mohr ◽  
R D Hesch
Keyword(s):  
Plasma Membrane ◽  
Brush Border ◽  
Brush Border Membrane ◽  
Kidney Cortex ◽  
Small Peptides ◽  
Uniform Size ◽  
Bovine Kidney ◽  
Brush Border Membranes ◽  
Membrane Bound ◽  
Uniform Size Distribution

The two parts of the bovine kidney cortex plasma membrane, the basal-lateral and the brush-border membrane, were simultaneously prepared from the same organ. Both types of membrane bound parathyrin, but only from the basal-lateral fraction was the hormone displaceable by its bioactive N-terminal fragment. In parallel, parathyrin-stimulated adenylate cyclase was predominantly found in basal-lateral membranes. The hormone was fragmented by both membrane types. Basal-lateral membranes generated fragments with a rather uniform size distribution (somewhat smaller than the intact peptide) and apparently preferred the hormone itself as a substrate. In contrast, the fragments produced by brush-border membranes were numberous small peptides.

Mercury and selenium distribution in human kidney cortex

1994 ◽  
Vol 40 (3) ◽  
pp. 255-265 ◽  
Author(s):  
Lars Björkman ◽  
Brita Palm ◽  
Magnus Nylander ◽  
Monica Nordberg
Keyword(s):  
Human Kidney ◽  
Kidney Cortex
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