Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P02794 (ferritin)
 17,525 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The early effects of gentamicin treatment on the inner ear glycocalyx were investigated using two cationic probes, colloidal thorium and cationized ferritin. Gentamicin treatment resulted in a diminished thorium reactivity of both the endolymphatic and perilymphatic glycocalyx of the hair cells after 1 day and complete abolishment of reactivity after 5 days. Cationized ferritin reactivity of the perilymphatic and endolymphatic glycocalyx was not significantly influenced. The cytochemistry of the inner ear glycocalyx and the possible biochemical changes induced by gentamicin are discussed.
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PMID:Early effects of gentamicin on inner ear glycocalyx cytochemistry. 318 8

Aminoglycosides bind to apical and basolateral (BL) membranes of renal epithelial cells. However, little is known regarding differential uptake and intracellular processing after internalization across these distinct surface membrane domains. To examine these processes independently, LLC-PK1 cells were grown on porous filters, which allow selective access to both domains. Apical and BL membrane uptakes of gentamicin (0.5 mM), quantified using [3H]gentamicin, were linear from 2 to 24 h (r = 0.99). The 4-h apical gentamicin uptake was 667 +/- 59 pmol/mg protein, the BL 748 +/- 26 pmol/mg protein, and concurrent apical and BL uptake 1,389 +/- 22 pmol/mg protein. Aminoglycoside uptake, documented using indirect immunogold techniques, occurred via the apical and BL endocytic systems and colocalized with cationic ferritin. Aminoglycosides internalized via the apical (gentamicin) and BL (tobramycin) membrane converged at the lysosomal level. Gentamicin incorporated via either domain significantly decreased lysosomal N-acetylglucosaminidase below control values (P < 0.05). We conclude that, after binding, aminoglycosides are internalized equally across apical and BL membranes of LLC-PK1 cells via receptor-mediated endocytosis, colocalize within the lysosomal compartment, and alter cellular function similarly.
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PMID:Apically and basolaterally internalized aminoglycosides colocalize in LLC-PK1 lysosomes and alter cell function. 830 30

Myosin VIIA is expressed by sensory hair cells and has a primary structure predicting a role in membrane trafficking and turnover, processes that may underlie the susceptibility of hair cells to aminoglycoside antibiotics. [3H]Gentamicin accumulation and the effects of aminoglycosides were therefore examined in cochlear cultures of mice with different missense mutations in the myosin VIIA gene, Myo7a, to see whether myosin VIIA plays a role in aminoglycoside ototoxicity. Hair cells from homozygous mutant Myo7ash1 mice, with a mutation in a nonconserved region of the myosin VIIA head, respond rapidly to aminoglycoside treatment and accumulate high levels of gentamicin. Hair cells from homozygous mutant Myo7a6J mice, with a mutation at a highly conserved residue close to the ATP binding site of the myosin VIIA head, do not accumulate [3H]gentamicin and are protected from aminoglycoside ototoxicity. Hair cells from heterozygotes of both alleles accumulate [3H]gentamicin and respond to aminoglycosides. Although aminoglycoside uptake is thought to be via apical surface-associated endocytosis, coated pit numbers on the apical membrane of heterozygous and homozygous Myo7a6J hair cells are similar. Pulse-chase experiments with cationic ferritin confirm that the apical endocytotic pathway is functional in homozygous Myo7a6J hair cells. Transduction currents can be recorded from both heterozygous and homozygous Myo7a6J hair cells, suggesting it is unlikely that the drug enters via diffusion through the mechanotransducer channel. The results show that myosin VIIA is required for aminoglycoside accumulation in hair cells. Myosin VIIA may transport a putative aminoglycoside receptor to the hair cell surface, indirectly translocate it to sites of membrane retrieval, or retain it in the endocytotic pathway.
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PMID:Myosin VIIA is required for aminoglycoside accumulation in cochlear hair cells. 939 Oct 6

The present study was designed to look at the hematological disorders in gentamicin nephrotoxicity model, as kidney is considered as one of the hemopoietic organs. In a previous study, novel and classical kidney injury biomarkers were utilized to evaluate the nephroprotective potential of Carica papaya leaf extract (CPLE) in the same model in albino rats. Gentamicin (100 mg/kg, subcutaneously, for 21 consecutive days) resulted in significant decreases in red blood cell (RBC) count, hemoglobin concentration (HGB), and packed cell volume (PCV) value, with minimal alterations in erythrocytic indices. Leucogram showed leukocytosis, granulocytosis, and thrombocytopenia. Erythropoietin (EPO) levels were also drastically decreased by the end of the experimental course. Serum iron, unsaturated iron-binding capacity (UIBC), total iron binding capacity (TIBC), transferrin saturation %, and serum transferrin concentration values were significantly decreased in contrast to ferritin, which was increased. When concurrently administered with gentamicin, CPLE (150 and 300 mg/kg, orally via gastric tube, for 21 days) significantly protected against the drastic effects of the former on the blood profile with improving potentials on erythrogram, leukogram, thrombocytes, EPO, iron and its indices, in a dose-dependent manner. These data may suggest CPLE as an appreciated blood homeostatic and nephroprotective agent from a natural source that could be a good remedy in conditions associated with blood disorders.
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PMID:Hemogram and iron indices in renal anemia and the amelioration with Carica papaya leaf extract applied on albino rat model. 3093 64