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  • 1
    Digitale Medien
    Digitale Medien
    INTERIM REPORT ON GENOMICS OF ESCHERICHIA COLI (2000)
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Microbiology 54 (2000), S. 341-411 
    Details
    ISSN: 0066-4227
    Quelle: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Thema: Biologie
    Notizen: Abstract We present a summary of recent progress in understanding Escherichia coli K-12 gene and protein functions. New information has come both from classical biological experimentation and from using the analytical tools of functional genomics. The content of the E. coli genome can clearly be seen to contain elements acquired by horizontal transfer. Nevertheless, there is probably a large, stable core of 〉3500 genes that are shared among all E. coli strains. The gene-enzyme relationship is examined, and, in many cases, it exhibits complexity beyond a simple one-to-one relationship. Also, the E. coli genome can now be seen to contain many multiple enzymes that carry out the same or closely similar reactions. Some are similar in sequence and may share common ancestry; some are not. We discuss the concept of a minimal genome as being variable among organisms and obligatorily linked to their life styles and defined environmental conditions. We also address classification of functions of gene products and avenues of insight into the history of protein evolution.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1146/annurev.micro.54.1.341
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  • 2
    Digitale Medien
    Digitale Medien
    Withdrawal of TNF-α after the fifth day of differentiation of CD34+ cord blood progenitors generates a homogeneous population of Langerhans cells and delays their maturation (2003)
    Oxford, UK : Blackwell Science Ltd
    Experimental dermatology 12 (2003), S. 0 
    Details
    ISSN: 1600-0625
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Medizin
    Notizen: Abstract: Human cord blood CD34+ progenitors cultured in the presence of granulocyte-macrophage colony-stimulating factor (GM-CSF), tumor necrosis factor-α (TNF-α) and transforming growth factor-β (TGF-β) generate a heterogeneous population of dendritic cells (DC), including Langerhans cells (LC). This combination of cytokines has been shown to be crucial for differentiation into LC. After day 5 of culture, TNF-α has been maintained in the medium in most studies despite the observation of spontaneous maturation of LC after day 12. Five-day samples of in vitro differentiated LC were cultured in parallel with or without TNF-α. The absence of TNF-α was shown to: (1) slow down proliferation without triggering apoptotic cell death, (2) enhance the percentage of LC, (3) delay or abrogat the expression of CD83, CD86, HLA-DR and CD208 molecules, and (4) maintain endocytosis by receptor and macropinocytosis. The withdrawal of TNF-α abrogated the spontaneous synthesis of matrix metalloproteinases. At day 12, TNF-α-deprived LC were less efficient in allogeneic T cell activation than LC cultivated with TNF-α. These data indicate that the suppression of TNF-α after day 5 maintains cells in an immature state and provides a population with 80% of LC at day 12.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1034/j.1600-0625.2003.00043.x
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  • 3
    Digitale Medien
    Digitale Medien
    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
    Schlagwort(e): Annexin I ; Human epidermal cells ; Keratinocytes ; Langherans cells ; Inflammation
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: 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.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00387599
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  • 4
    Digitale Medien
    Digitale Medien
    Glucocorticoid receptor localization in human epidermal cells (1996)
    Springer
    Archives of dermatological research 288 (1996), S. 140-146 
    Details
    ISSN: 1432-069X
    Schlagwort(e): Key words Glucocorticoid receptors ; Human epidermal ; cells ; Keratinocytes ; Langerhans cells ; Melanocytes
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: Abstract Glucocorticoids, which are widely used in therapy, exert their immunosuppressive actions through specific receptors. These receptors have been characterized in cultured human skin fibroblasts and keratinocytes, but their localization in vitro and in vivo has not been established. To determine the tissue and cellular distribution of glucocorticoid receptors (GR), two specific polyclonal rabbit anti-human GR antibodies were used to detect these receptors in skin biopsy specimens, in freshly isolated and cultured human epidermal cells and in keratinocyte cell lines. Immunoreactive GR were only faintly detected in normal and abnormal differentiated cells and as well as those in the stratum granulosum and corneocytes. These immunolocalization studies were confirmed by fluorescence cell sorter analysis of isolated basal and suprabasal keratinocytes. Immunoreactive GR were highly expressed in normal cultured human keratinocytes, Langerhans cells and several cell lines whereas they were less expressed in melanocytes. Based upon these results the main targets of glucocorticoids in the epidermis appear to be basal and Langerhans cells.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/s004030050036
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  • 5
    Digitale Medien
    Digitale Medien
    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
    Schlagwort(e): Alzheimer's disease ; β-amyloid precursor protein ; acetylcholinesterase ; β/A4 peptide ; secretase ; amyloidosis
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: 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.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00733756
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