GLORIA

GEOMAR Library Ocean Research Information Access

X
feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
Filter
  • HIV infection  (1)
  • Immunosuppression and metalloproteinases  (1)
  • Inhibitors  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Inhibition of Tryptase TL2 from Human T4+ Lymphocytes and Inhibition of HIV-1 Replication in H9 Cells by Recombinant Aprotinin and Bikunin Homologues (1997)
    Springer
    The protein journal 16 (1997), S. 651-660 
    Details
    ISSN: 1573-4943
    Keywords: Kunitz-type inhibitor ; aprotinin ; bikunin ; tryptase TL2 ; HIV infection
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The serine esterase TL2 from human T4+ lymphocytes is a binding component to HIV-1 glycoprotein gp120 and seems to play a role in the HIV-1 infection mechanism. Recombinant variants of the Kunitz-type serine proteinase inhibitor aprotinin were investigated for their ability to inhibit tryptase TL2 and the binding of gp120 to this enzyme. Furthermore, the viral replication of HIV-1 was investigated in H9 cell cultures under the influence of recombinant aprotinin and bikunin variants. In contrast to native aprotinin, the recombinant variant [Arg15, Phe17, Glu52]aprotinin with a reactive-site sequence homologous to the V3 loop of HIV-1 gp120 showed a specific inhibition of tryptase TL2 (〉80%). However, the [Leu15, Phe17, Glu52]aprotinin variant with hydrophobic subsites was the most potent inhibitor of the binding of gp120 to tryptase TL2 (68%). Our results show that the enzyme activity of purified tryptase TL2 is inhibited not only by variants with basic amino acids, but also those with hydrophobic residues in the reactive-site region. Therefore, tryptase TL2 is not a typical trypsin-like or chymotrypsin-like protease. Investigations on inhibition of HIV-1 replication in H9 cell cultures showed that tryptase TL2 is involved in the mechanism of virus internalization into human lymphocytes. The [Leu15, Phe17, Glu52]aprotinin showed a significant retardation of syncytium formation over a period of 5 days in a 1 μM concentration. Similar investigations were performed with recombinant variants of bikunin, the light chain of human inter-α-trypsin inhibitor. Only the single-headed variant [Arg94]82bikunin inhibited slightly the syncytium formation over a period of 2 days in a 2.2 μM concentration. Wild-type bikunin and all full-length variants showed no effect, possibly due to steric hindrance by the second domain of the double-headed inhibitor.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1026379109403
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Effect of immunosuppressive drugs on the release of metalloproteinases from human polymorphonuclear leukocytes (1991)
    Springer
    Transplant international 4 (1991), S. 26-30 
    Details
    ISSN: 1432-2277
    Keywords: Immunosuppression and metalloproteinases ; Metalloproteinases and immunosuppression
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The concentration of the metalloproteinases type I collagenase and gelatinase was measured in isolated polymorphonuclear leukocytes (PMNLs) of renal transplant recipients treated either with cyclosporin A (CyA) and prednisolone (Pr) (n=8) or azathioprine (Aza) and Pr (n=8), and of healthy subjects (n=12). PMNLs of CyA- and Aza-treated transplant patients displayed markedly higher gelatinase content (2427±489 and 3284±357 ng/107 cells) than PMNLs of controls (528±83 ng/107 cells). There was also a higher content of type I collagenase in PMNLs (3374±292 ng/107 cells) of Aza-treated patients and significantly elevated levels in PMNLs of patients receiving CyA (3625±229 ng/107 cells) compared with healthy subjects (2878±151 ng/107 cells). In contrast, neutrophil lactoferrin content was lower in transplant patients. Thus, immunosuppressive drugs may reduce the release of leukocyte proteinases, which are known for their deleterious role in proteolytic tissue and matrix breakdown. In vitro, the effects of different immunosuppressive drugs on the release of lactoferrin, collagenase and gelatinase were investigated on FMLPNTL-stimulated PMNLs isolated from healthy subjects. CyA but not Aza or Pr caused inhibition of gelatinase, collagenase and lactoferrin release.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00335512
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Biochemistry of Natural Proteinase Inhibitors (1974)
    Weinheim : Wiley-Blackwell
    Angewandte Chemie International Edition in English 13 (1974), S. 10-28 
    Details
    ISSN: 0570-0833
    Keywords: Inhibitors ; Inhibitors ; Chemistry ; General Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The natural inhibitors of proteolytic enzymes are proteins. These inhibitors associate reversibly with the enzymes to form stoichiometric protein-protein complexes, in which substrate-analogous association at the active center of the enzyme results in competitive inhibition of all catalytic functions. The very widespread occurrence of inhibitors in the animal and plant kingdoms underlines their biological importance in the intermediate metabolism, which can be understood as an extension of the possibilities for temporary and local limitations of enzyme activities. Existing knowledge includes a series of covalent structures, detailed kinetic data on the reversible protein-protein interaction, the processes involved in inactivation, and chemical methods for the modification of these proteins. Early X-ray structural data for an inhibitor and its enzyme complex provide an insight into the molecular structure of the latter and the interactions involved in the association to form the complex.
    Additional Material: 16 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/anie.197400101
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...