PLZEŇSKÝ LÉKAŘSKÝ SBORNÍK
PLZEŇSKÝ LÉKAŘSKÝ SBORNÍK
A multi-disciplinary medical journal publishing scientific works from theoretical and clinical fields with English summaries as well as works by foreign contributors in English. The chapter "Faculty Life" offers personal messages, reports on the faculty's activities in the past year and presents a complete bibliography of the medical faculty's departments and clinics in the year. The journal has been published since 1956.

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PLZEŇSKÝ LÉKAŘSKÝ SBORNÍK, Vol 2018 No 84 (2018), 29–36

Inhibitory serinových proteáz serpinového TYPU inhibující cysteinové proteázy: příklad „cross-class“ inhibice

[Serine proteinase inhibitors (serpins) inhibiting cysteine proteinases: an example of “cross-class” inhibition .]

J. Kotyza

published online: 12. 12. 2018

abstract

Proteolytic enzymes are classified into four mechanistic classes: serine, cysteine, aspartic proteases, and metalloproteinases, respectively. Active proteases of each class may be inhibited by a class-specific group of proteinaceous inhibitors. The most common serine-type proteinase inhibitors are called sepins. Leukocyte elastase, the blood clottingand blood clot dissolving enzymes, to name some, belong to the target serine proteases. During evolution, some serpine-like molecules lost their enzyme inhibitory action, others changed their properties, and a specific group of serpins gained an abberant inhibitory against cysteine proteinases. The first of such „cross-class“ serpine inhibitors identified was crmA (cytokine response modifier), inhibiting interleukin-1 beta converting enzyme (ICE), a cysteine protease implicated in the promotion of inflammatory reaction and apoptosis upon a cow-pox virus infection. A dozen other cross-class inhibitory serpins has been identified so far, and found to be involved in the process of apoptosis, protein processing, embryonic development, cancerogenesis and inflammation. The molecular basis of the cysteine protease inhibition by serpins appars to be analogous with serine protease inhibition by serpins, namely a stable enzyme-serpin complex formation.

157 x 230 mm
periodicity: 1 x per year
ISSN: 0551-1038

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