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  • 1
    Electronic Resource
    Electronic Resource
    Expression of Annexin I in freshly isolated human epidermal cells and in cultured keratinocytes (1994)
    Springer
    Archives of dermatological research 286 (1994), S. 268-272 
    Details
    ISSN: 1432-069X
    Keywords: Annexin I ; Human epidermal cells ; Keratinocytes ; Langherans cells ; Inflammation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Annexin I belongs to a newly characterized family of intracellular proteins involved in the regulation of the production of inflammatory lipid mediators such as prostaglandins and leucotrienes. Annexin I (named p35, lipocortin I or calpactin II) was initially described as a protein inducible by glucocorticoids. In the skin, the role of annexins has still not been elucidated. In the study reported here we investigated the expression of annexin I both in freshly isolated epidermal cells and in cultured keratinocytes using immunofluorescence, FACS analysis and immunoblotting techniques. Using epidermal cells freshly isolated from normal skin, annexin I was detected by double immunostaining mainly in basal and suprabasal keratinocytes. Langerhans cells isolated from Ficoll gradient were faintly stained compared with keratinocytes. Annexin I was also highly expressed in keratinocytes maintained in culture in a serum-free medium without hydrocortisone. By confocal microscopy, annexin I was shown to be mainly localized in the cytoplasm of the cells. The protein was characterized by Western blot and immunoprecipitation as a 35-kDa protein in freshly isolated epidermal cells and cultured keratinocytes. Results from in vivo studies confirmed the presence of annexin I in the basal and suprabasal layers of normal human skin with modified reactivity patterns in hyperproliferative lesions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00387599
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  • 2
    Electronic Resource
    Electronic Resource
    Proteolysis at the secretase and amyloidogenic cleavage sites of theβ-amyloid precursor protein by acetylcholinesterase and butyrylcholinesterase using model peptide substrates (1993)
    Springer
    Cellular and molecular neurobiology 13 (1993), S. 279-287 
    Details
    ISSN: 1573-6830
    Keywords: Alzheimer's disease ; β-amyloid precursor protein ; acetylcholinesterase ; β/A4 peptide ; secretase ; amyloidosis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary 1. It was recently proposed that acetylcholinesterase (AChE), in addition to its esteratic activity, has proteolytic activity such that it may cleave theβ-amyloid precursor (β-APP) within theβ-amyloid sequence. The purpose of this paper was to examine further whether AChE or butyrylcholinesterase (BuChE) had associated proteinase activity that was involved in the metabolism ofβ-APP. 2. The ability of various preparations of AChE and BuChE to hydrolyze two synthetic fragments ofβ-APP695 as model substrates containing the normal and aberrant cleavage sites was studied. 3. Digestion of these synthetic substrates with commercial preparations ofElectrophorus electricus AChE indicated the presence of a trypsin-like proteolytic activity cleaving each peptide at the carboxy-terminal side of an internal lysine residue. 4. Purification of the trypsin-like proteinase activity by aminobenzamidine affinity chromatography yielded a preparation that was devoid of AChE activity but retained all of the proteinase activity. 5. Amino-terminal sequence analysis of this preparation showed that the first 13 amino acid residues were identical toβ-pancreatic trypsin. 6. These data indicate that the proteinase activity found in these commercial preparations of AChE is due to contamination with trypsin.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00733756
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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