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  • In situ hybridization  (3)
  • HSP60  (2)
  • 1
    Digitale Medien
    Digitale Medien
    Heat shock proteins HSP25, HSP60, HSP72, HSP73 in isoosmotic cortex and hyperosmotic medulla of rat kidney (1996)
    Springer
    Pflügers Archiv 431 (1996), S. 608-617 
    Details
    ISSN: 1432-2013
    Schlagwort(e): Key words Osmotic stress ; Heat shock proteins (HSP25 ; HSP60 ; HSP72 ; HSP73) ; Intrarenal distribution ; Phosphorylation of HSP25 ; Anaesthesia
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: Abstract The distribution of heat shock proteins (HSP) HSP60, HSP73, HSP72 and HSP25 in the isoosmotic cortex and the hyperosmotic medulla of the rat kidney was investigated using Western blot analysis and immunohistochemistry. HSP73 was homogeneously distributed throughout the whole kidney. The level of HSP60 was high in the renal cortex and low in the medulla. HSP25 and HSP72 were present in large amounts in the medulla. Only low levels of HSP25 and almost undetectable amounts of HSP72 were found in the cortex. HSP25 exists in one nonphosphorylated and several phosphorylated isoforms. Western blot analysis preceded by isoelectric focussing showed that HSP25 predominates in its nonphosphorylated form in the outer medulla but in its phosphorylated form in cortex and inner medulla. Although this intrarenal distribution pattern was not changed during prolonged anaesthesia (thiobutabarbital sodium), a shift from the nonphosphorylated to the phosphorylated isoforms of HSP25 occurred in the medulla. The characteristic intrarenal distribution of the constitutively expressed HSPs (HSP73, HSP60, HSP25) may reflect different states of metabolic activity in the isoosmotic (cortex) and hyperosmotic (medulla) zones of the kidney. The high content of inducible HSP72 in the medulla most likely is a consequence of the osmotic stress imposed upon the cells by the high urea and salt concentrations in the hyperosmotic medullary environment.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/s004240050042
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  • 2
    Digitale Medien
    Digitale Medien
    Effects of long-term changes in medullary osmolality on heat shock proteins HSp25, hsp60, HSP72 and HSP73 in the rat kidney (1998)
    Springer
    Pflügers Archiv 435 (1998), S. 705-712 
    Details
    ISSN: 1432-2013
    Schlagwort(e): Key words Diuresis/antidiuresis ; Osmotic stress ; HSP25 ; HSP60 ; HSP72 ; HSP73 ; Transcription ; Translation ; Medullary hypertonicity ; Phosphorylation
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: Abstract  The influence of diuresis and antidiuresis on the expression of heat shock proteins (HSP) 25, 60, 72 and 73 in the renal cortex and outer and inner medulla of Wistar rats was analysed. Medullary osmolality was reduced by long-term diuresis (3% sucrose in the drinking water for 3 weeks) and subsequently enhanced by transition to a concentrating state by giving normal drinking water again in combination with deamino-D-arginine vasopressin (dDAVP) for 5 days. Western blot analyses revealed that neither HSP73 nor HSP60 was influenced by any treatment. The HSP72 level in the medulla was markedly reduced (50%) when osmolality was lowered and increased when tonicity was high. RNAse protection assays showed that the effects on HSP72 are parallelled in general by changes in HSP72 mRNA. While levels of HSP25 were not influenced, isoelectric focusing revealed that the degree of phosphorylation of outer and inner medullary HSP25 increased following both treatments. It thus seems that HSP73 and HSP60 are not directly involved in the long-term adaptation to varying medullary osmolalities. The correlation between changes in osmolality and amounts of the major stress-inducible HSP72 in the medulla implies that medullary hypertonicity is stressful for kidney cells. Furthermore, adaptation to pronounced changes in the osmolality of the environment most likely involves phosphorylation of HSP25.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/s004240050572
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  • 3
    Digitale Medien
    Digitale Medien
    Expression of Na+/Cl–/betaine and Na+/myo-inositol transporters, aldose reductase and sorbitol dehydrogenase in macula densa cells of the kidney (1998)
    Springer
    Pflügers Archiv 436 (1998), S. 807-809 
    Details
    ISSN: 1432-2013
    Schlagwort(e): Key words Aldose reductase ; In situ hybridization ; Macula densa ; Na+/Cl ; /betaine cotransporter ; Na+/myo-inositol cotransporter ; Osmolytes ; Sorbitol dehydrogenase
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: Abstract  It has been suggested that macula densa cells may be exposed to hyperosmotic stress. Since chronic exposure to hypertonic stress causes the amount of intracellular organic osmolytes to increase, the expression of transporters and enzymes that participate in the intracellular accumulation of organic osmolytes was examined using non-radioactive in situ hybridization in the macula densa region of control rats and furosemide-treated animals. Both the sodium- and chloride-dependent betaine transporter (BGT) and sodium-dependent myo-inositol transporter (SMIT) were expressed preferentially in macula densa cells and for both mRNAs the signal intensity was visibly reduced by furosemide. The enzymes aldose reductase (which mediates the conversion of glucose to sorbitol) and sorbitol dehydrogenase (which converts sorbitol into fructose) were expressed not only in macula densa cells but also in the surrounding tubular cells, and the expression was insensitive to furosemide. Thus it remains unclear whether the expression of BGT and SMIT is related to a putative hypertonic juxtaglomerular region.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/s004240050707
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  • 4
    Digitale Medien
    Digitale Medien
    The expression of the gene coding for parathyroid hormone-related protein (PTHrP) during tooth development in the rat (1995)
    Springer
    Cell & tissue research 280 (1995), S. 283-290 
    Details
    ISSN: 1432-0878
    Schlagwort(e): Parathyroid hormone-related protein (PTHrP) ; Teeth ; In situ hybridization ; Rat (Sprague Dawley)
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Medizin
    Notizen: Abstract By means of in situ hybridisation studies, it is shown that parathyroid hormone-related protein (PTHrP) mRNA is strongly expressed in the developing enamel organs of rat teeth. In particular, the cervical loop hybridises strongly with the PTHrP probe and expression is maintained at this site throughout life in the permanently erupting incisor teeth. In mature molar teeth, expression is downregulated to low levels and confined to the epithelial cell rests of Malassez and/or cementoblasts which may derive from these. The gene is also expressed at low levels in the tissue overlying the erupting molars and, thereafter, in the junctional epithelia and connective tissue cells of the epithelial attachment on all tooth surfaces. The premise that PTHrP may undergo post-translational processing and that the resultant products could act in different ways raises the possibility of its exerting multiple paracrine actions during tooth development. These could include the control of cell division and local vascular dilation during development.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00307800
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  • 5
    Digitale Medien
    Digitale Medien
    The expression of the gene coding for parathyroid hormone-related protein (PTHrP) during tooth development in the rat (1995)
    Springer
    Cell & tissue research 280 (1995), S. 283-290 
    Details
    ISSN: 1432-0878
    Schlagwort(e): Key words: Parathyroid hormone-related protein (PTHrP) ; Teeth ; In situ hybridization ; Rat (Sprague Dawley)
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Medizin
    Notizen: Abstract. By means of in situ hybridisation studies, it is shown that parathyroid hormone-related protein (PTHrP) mRNA is strongly expressed in the developing enamel organs of rat teeth. In particular, the cervical loop hybridises strongly with the PTHrP probe and expression is maintained at this site throughout life in the permanently erupting incisor teeth. In mature molar teeth, expression is downregulated to low levels and confined to the epithelial cell rests of Malassez and/or cementoblasts which may derive from these. The gene is also expressed at low levels in the tissue overlying the erupting molars and, thereafter, in the junctional epithelia and connective tissue cells of the epithelial attachment on all tooth surfaces. The premise that PTHrP may undergo post-translational processing and that the resultant products could act in different ways raises the possibility of its exerting multiple paracrine actions during tooth development. These could include the control of cell division and local vascular dilation during development.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00307800
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