ETD system

Electronic theses and dissertations repository

 

Tesi etd-02282012-160834


Thesis type
Tesi di dottorato di ricerca
Author
RICCI, CLAUDIO
URN
etd-02282012-160834
Title
Structure and Enzyme Kinetics Studies on Different Forms of Cathepsin L: Implication on Development of Anticancer Agents
Settore scientifico disciplinare
CHIM/08
Corso di studi
BIOMATERIALI
Commissione
correlatore Dott. Massarelli, Ilaria
correlatore Dott. Pietra, Daniele
tutor Dott.ssa Bianucci, Anna Maria
Parole chiave
  • Tumor
  • Cathepsin L
  • Kinetic Enzyme
Data inizio appello
23/03/2012;
Consultabilità
completa
Riassunto analitico
Cathepsin L (enzyme classification number: EC 3.4.22.15) belongs to the family of Cathepsins, which are proteases and share a conserved active site formed by cysteine and histidine residues. Cathepsin L is widely distributed in the cell; particularly, it is mainly located in lysosomes, in the nucleus and in extracellular compartment. Cathepsin L is responsible for different physiological processes, depending on its particular location. Indeed, cathepsins not only mediate terminal protein degradation in lysosomes, they also process and activate proteins including growth factors in extracellular environment and transcription factors in the nucleus. Consequently, they are involved in several pathological states, ranging from cancer and methastasis to inflammatory disorders. In this work, the kinetics of cathepsin L binding to its substrate Z-Phe-Arg-AMC was studied by modifying some environment parameters, in order to simulate various cellular compartments and explore how the kinetics of this enzyme may change in different biological conditions.
File