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  • 1995-1999  (1)
  • 1990-1994  (1)
  • C-terminal peptide  (1)
  • Chondrocyte  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Expression of parathyroid hormone-related protein in rat articular cartilage (1995)
    Springer
    Calcified tissue international 57 (1995), S. 196-200 
    Details
    ISSN: 1432-0827
    Keywords: PTHrP ; Articular cartilage ; Chondrocyte ; Development
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Abstract Expression and localization of parathyroid hormone-related protein (PTHrP) in rat articular cartilage during fetal and postnatal periods were investigated by immunohistochemistry and in situ hybridization. PHTrP displayed distinct distribution and intensity of staining at different ages. In fetal (18-day-old) and young (3-week-old) rats, articular chondrocytes expressed abundant PTHrP throughout the entire thickness of cartilage. In contrast, in 60-week-old rats, PTHrP was expressed in a few articular chondrocytes of superficial and middle layers. Regulation of PTHrP and PTH/PTHrP receptor mRNA was also studied in cultured rat articular chondrocytes. Northern blot analysis revealed that both transforming growth factor-β (TGF-β), an important stimulator for chondrocyte proliferation and differentiation, and 10% fetal bovine serum (FBS) stimulated the expression of PTHrP mRNA with down-regulation of its receptor mRNA. In contrast, 12-O-tetradecanoylphorbol-13-acetate (TPA) down-regulated the expression of receptor without changes of PTHrP mRNA level. These results suggest that the changes in abundance and localization of PTHrP and its receptor may be directly involved in the cell growth and differentiation of articular cartilage.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00310258
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Solid-phase C-terminal sequencing of peptides (1992)
    Springer
    Amino acids 2 (1992), S. 289-296 
    Details
    ISSN: 1438-2199
    Keywords: Amino acids ; C-terminal peptide ; Thiohydantoin derivatives ; C-terminal sequencing ; Solid phase peptide sequencing
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary C-terminal amino acid sequence analysis seemed to be established procedure, as the counterpart of Edman's N-terminal sequencing method. However, poor recovery of the C-terminal amino acids in the reaction in homogeneous solution suggested further improvement of the method. In the present study, N-terminal amino acid was fixed covalently to the controlled pore glass (CPG) beads and the C-terminal amino acid was activated (by treating with acetic anhydride), coupled with thiocyanate to form thiohydantoin (TH) ring at the C-terminus. Then, the C-terminal amino acid was split off as the corresponding TH derivative, and analyzed by HPLC. Hydrolysis of the TH derivative was achieved at 60°C in the presence of 2 M HC1 for 2 h. Solid phase fixed peptide was washed simply with acetone, and dried for the next cycle of the reaction. So far obtained results in the heterogeneous mixture are not satisfactory in terms of the recovery of the C-terminal TH, and improvement of the recovery and further steps are under progress.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00805950
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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