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  • 1995-1999  (6)
  • Mouse  (2)
  • acetylHmb  (2)
  • in situ neutralisation  (2)
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Cell & tissue research 281 (1995), S. 413-419 
    ISSN: 1432-0878
    Keywords: Key words: Apoptosis ; Mammary gland ; Lactation ; Involution ; DNA laddering ; Mouse
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. Mammary involution after cessation of milk removal is associated with extensive loss of secretory epithelial cells. Ultrastructural changes and the appearance of oligonucleosomal DNA laddering in ethidium bromide-stained gels indicates that cell loss during involution occurs by apoptosis. In this study, a technique for nick end-labelling of genomic DNA with radiolabelled deoxynucleotide has been used to monitor the induction of programmed cell death in mice after litter removal at peak lactation. This technique proved more sensitive than conventional ethidium bromide staining, and results suggested that apoptosis was induced rapidly by milk stasis, before extensive tissue re-modelling had begun. Oligonucleosomal DNA laddering on agarose gels was detected within 24 h of milk stasis, and increased progressively for at least 4 days. Nick-end labelling also detected laddering before litter removal, suggesting that programmed cell death is a normal feature of the lactating tissue. The DNA end-labelling technique was also adapted for in situ visualisation of apoptotic cells in tissue sections. By this criterion, apoptotic cells were identified in both the secretory epithelium lining the alveoli of the gland and, increasingly with prolonged milk stasis, amongst those sloughed into the alveolar lumen. The results demonstrate the utility of these techniques for study of mammary cell death and suggest that, whilst apoptosis is rapidly induced by milk stasis, it is also a normal physiological event in the lactating mammary gland.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Cell & tissue research 281 (1995), S. 413-419 
    ISSN: 1432-0878
    Keywords: Apoptosis ; Mammary gland ; Lactation ; Involution ; DNA laddering ; Mouse
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Mammary involution after cessation of milk removal is associated with extensive loss of secretory epithelial cells. Ultrastructural changes and the appearance of oligonucleosomal DNA laddering in ethidium bromide-stained gels indicates that cell loss during involution occurs by apoptosis. In this study, a technique for nick end-labelling of genomic DNA with radiolabelled deoxynucleotide has been used to monitor the induction of programmed cell death in mice after litter removal at peak lactation. This technique proved more sensitive than conventional ethidium bromide staining, and results suggested that apoptosis was induced rapidly by milk stasis, before extensive tissue re-modelling had begun. Oligonucleosomal DNA laddering on agarose gels was detected within 24 h of milk stasis, and increased progressively for at least 4 days. Nick-end labelling also detected laddering before litter removal, suggesting that programmed cell death is a normal feature of the lactating tissue. The DNA end-labelling technique was also adapted for in situ visualisation of apoptotic cells in tissue sections. By this criterion, apoptotic cells were identified in both the secretory epithelium lining the alveoli of the gland and, increasingly with prolonged milk stasis, amongst those sloughed into the alveolar lumen. The results demonstrate the utility of these techniques for study of mammary cell death and suggest that, whilst apoptosis is rapidly induced by milk stasis, it is also a normal physiological event in the lactating mammary gland.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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  • 3
    ISSN: 1573-3904
    Keywords: amyloid ; circular dichroism ; ‘difficult sequence’ ; in situ neutralisation ; N-(2-hydroxy-4-methoxybenzyl) ; tetramethylfluoroformamidinium hexafluorophosphate
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Summary A peptide corresponding to residues 106–126 of the human prion protein (PrP) possesses the neurotoxic and amyloidogenic properties of the infectious form of the parental protein. This peptide is now identified as a ‘difficult sequence’ and synthesis using conventional manual Fmoc chemistry was unsuccessful with acylation terminating at a central core of hydrophobic amino acids. The use of tetramethylfluoroformamidinium hexafluorophosphate and 1-methyl-2-pyrrolidone as anti-aggregatory agents in the coupling steps improved the synthesis but still resulted in an incomplete peptide. The incorporation ofN-(2-hydroxy-4-methoxybenzyl)protection at glycine residues 119 and 124 enabled synthesis of the full length peptide in low yield. Synthesis using Boc chemistry within situ neutralisation gave the full length peptide in high yield.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1573-3904
    Keywords: amyloid ; circular dichroism ; 'difficult sequence' ; in situ neutralisation ; N-(2-hydroxy-4-methoxybenzyl) ; tetramethylfluoroformamidinium hexafluorophosphate
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract A peptide corresponding to residues 106-126 of the human prion protein (PrP) possesses the neurotoxic and amyloidogenic properties of the infectious form of the parental protein. This peptide is now identified as a 'difficult sequence' and synthesis using conventional manual Fmoc chemistry was unsuccessful with acylation terminating at a central core of hydrophobic amino acids. The use of tetramethylfluoroformamidinium hexafluorophosphate and 1-methyl-2- pyrrolidone as anti-aggregatory agents in the coupling steps improved the synthesis but still resulted in an incomplete peptide. The incorporation of N-(2-hydroxy-4-methoxybenzyl) protection at glycine residues 119 and 124 enabled synthesis of the full length peptide in low yield. Synthesis using Boc chemistry with in situ neutralisation gave the full length peptide in high yield.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    International journal of peptide research and therapeutics 6 (1999), S. 289-293 
    ISSN: 1573-3904
    Keywords: Aβ(1–40) ; acetylHmb ; circular dichroism ; electron microscopy ; fibril formation ; secondary structure
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Summary Modifications to secondary structure and fibril formation caused by multiple acetylHmb backbone amide protection of Alzheimer's disease Aβ(1–40) were investigated using circular dichroism spectroscopy and electron microscopy. Penta(acetylHmb) Aβ(1–40) was observed to have a reduced ability to form α-helix and β-sheet structures under the same solution conditions as the native peptide, with α-helical propensity being reduced more significantly than β-sheet propensity. Further, acetylHmb backbone protection was found to alter Aβ(1–40) interaction with SDS-micelles by preventing α-helix formation. Aβ fibril formation, a characteristic property of this peptide, was also not observed for penta(acetylHmb) Aβ(1–40).
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Springer
    International journal of peptide research and therapeutics 6 (1999), S. 289-293 
    ISSN: 1573-3904
    Keywords: Aβ(1-40) ; acetylHmb ; circular dichroism ; electron microscopy ; fibril formation ; secondary structure
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Modifications to secondary structure and fibril formation caused by multiple acetylHmb backbone amide protection of Alzheimer's disease Aβ(1-40) were investigated using circular dichroism spectroscopy and electron microscopy. Penta(acetylHmb)Aβ(1-40) was observed to have a reduced ability to form α-helix and β-sheet structures under the same solution conditions as the native peptide, with α-helical propensity being reduced more significantly than β-sheet propensity. Further, acetylHmb backbone protection was found to alter Aβ(1-40) interaction with SDS-micelles by preventing α-helix formation. Aβ fibril formation, a characteristic property of this peptide, was also not observed for penta(acetylHmb)Aβ(1-40).
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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