Peptidases are proteolytic enzymes that catalyze the hydrolysis of the peptide bonds in diverse biological systems in all living organisms. Humans peptidase genes comprise around 7% of the protein-encoding genome. According to their structure and their catalytic mechanism, peptidases are classified into seven main groups – aspartic, cysteine, glutamic, metallo, asparagine, serine, and threonine peptidases. Peptidases cleave substrates either as endopeptidases, in the middle of polypeptide chain, or as exopeptidases, at N or C termini ends. Peptidases are found localized extracellularly or intracellularly in cytoplasmic, in the nucleus or packaged within lysosomal/endosomal vesicles. Peptidases have important physiological roles in a number of biological processes where they act either as degradative enzymes, completely degrading target proteins, or as regulatory enzymes by altering peptide function after cleavage of one or more specific amino acid bonds.
In physiological conditions, the activity of peptidases is regulated very precisely by a multitude of factors. They can be regulated both transcriptional and translational. Their proteolytic activity is tightly controlled by, the specificity of the active site cleft, synthesis as inactive precursors (zymogens), activation by co-factors, and suppression of proteolytic activity by endogenous peptidase inhibitors. The dysregulation of these control factors can result in uncontrolled proteolytic activity which is subsequently associated with a number of pathological processes including cancer, neurodegeneration, immune disorders, cardiovascular diseases, and virus infections. Due to their important role in disease progression, peptidases have been identified as promising therapeutic targets for the development on new therapeutic approaches that could improve management of diseases.
This Research Topic will focus on the biological functions of proteases during disease development and progression and the possibility of their regulation with the goal of achieving improved disease management specifically focusing on cancer. Studies addressing the role and mechanisms of peptidases in cancer progression and management as well as studies on peptidases as therapeutic targets for improving current therapies are welcome. Emphases will be given to the peptidase in cancer, neurodegeneration and immune disorders.
We welcome original research and review articles on, but not limited to, the following topics:
- Peptidases in cancer progression
- Mechanisms of the peptidases in cancer management
- Peptidases as therapeutic targets in cancer management
- Peptidases as biomarkers for prediction of disease progression and therapeutic response
- New therapeutics for regulation of increase peptidase activity in pathological processes
Peptidases are proteolytic enzymes that catalyze the hydrolysis of the peptide bonds in diverse biological systems in all living organisms. Humans peptidase genes comprise around 7% of the protein-encoding genome. According to their structure and their catalytic mechanism, peptidases are classified into seven main groups – aspartic, cysteine, glutamic, metallo, asparagine, serine, and threonine peptidases. Peptidases cleave substrates either as endopeptidases, in the middle of polypeptide chain, or as exopeptidases, at N or C termini ends. Peptidases are found localized extracellularly or intracellularly in cytoplasmic, in the nucleus or packaged within lysosomal/endosomal vesicles. Peptidases have important physiological roles in a number of biological processes where they act either as degradative enzymes, completely degrading target proteins, or as regulatory enzymes by altering peptide function after cleavage of one or more specific amino acid bonds.
In physiological conditions, the activity of peptidases is regulated very precisely by a multitude of factors. They can be regulated both transcriptional and translational. Their proteolytic activity is tightly controlled by, the specificity of the active site cleft, synthesis as inactive precursors (zymogens), activation by co-factors, and suppression of proteolytic activity by endogenous peptidase inhibitors. The dysregulation of these control factors can result in uncontrolled proteolytic activity which is subsequently associated with a number of pathological processes including cancer, neurodegeneration, immune disorders, cardiovascular diseases, and virus infections. Due to their important role in disease progression, peptidases have been identified as promising therapeutic targets for the development on new therapeutic approaches that could improve management of diseases.
This Research Topic will focus on the biological functions of proteases during disease development and progression and the possibility of their regulation with the goal of achieving improved disease management specifically focusing on cancer. Studies addressing the role and mechanisms of peptidases in cancer progression and management as well as studies on peptidases as therapeutic targets for improving current therapies are welcome. Emphases will be given to the peptidase in cancer, neurodegeneration and immune disorders.
We welcome original research and review articles on, but not limited to, the following topics:
- Peptidases in cancer progression
- Mechanisms of the peptidases in cancer management
- Peptidases as therapeutic targets in cancer management
- Peptidases as biomarkers for prediction of disease progression and therapeutic response
- New therapeutics for regulation of increase peptidase activity in pathological processes
