cathepsins
Sign in to saveAlso known as cathepsin
Cathepsins (Ancient Greek kata- 'down' and hepsein 'boil'; abbreviated CTS) are proteases (enzymes that degrade proteins) found in all animals as well as other organisms. There are approximately a dozen members of this family, which are distinguished by their structure, catalytic mechanism, and which proteins they cleave. Most of the members become activated at the low pH found in lysosomes. Thus, the activity of this family lies almost entirely within those organelles. There are, however, exceptions such as cathepsin K, which works extracellularly after secretion by osteoclasts in bone resorp
Key facts
- Protein family.Symbol
- CTP
- Protein family.Name
- Cathepsin
- Protein family.image
- Cathepsin K 1TU6.png
- Protein family.caption
- Structure of Cathepsin K
- Protein family.Pfam
- PF00112
- Protein family.Pfam_clan
- CL0125
- Protein family.InterPro
- IPR000668
- Protein family.SMART
- Pept_C1
- Protein family.PROSITE
- PDOC00126
- Protein family.SCOP
- 1aec
- Protein family.MEROPS
- C1
via Wikipedia infobox
Research
30,030 papers- Cathepsins in the osteoclast.Journal of electron microscopy · 2003
- The role of lysosomal cysteine cathepsins in NLRP3 inflammasome activation.Archives of biochemistry and biophysics · 2019
- Cathepsins and age-related macular degeneration: A Mendelian randomization study unveiling causal relationships.Medicine · 2025
- Tissue cathepsins as tumor markers.Clinica chimica acta; international journal of clinical chemistry · 1995
- Cysteine Cathepsins in the secretory vesicle produce active peptides: Cathepsin L generates peptide neurotransmitters and cathepsin B produces beta-amyloid of Alzheimer's disease.Biochimica et biophysica acta · 2012
via PubMed
~8 min read
Encyclopedic overview
12 sectionsContents
- Classification
- Clinical significance
- Cathepsin A
- Cathepsin B
- Cathepsin D
- Cathepsin K
- Cathepsin V
- Inhibitors
- Cathepsin zymography
- History
- References
- External links
Cathepsins (Ancient Greek kata- 'down' and hepsein 'boil'; abbreviated CTS) are proteases (enzymes that degrade proteins) found in all animals as well as other organisms. There are approximately a dozen members of this family, which are distinguished by their structure, catalytic mechanism, and which proteins they cleave. Most of the members become activated at the low pH found in lysosomes. Thus, the activity of this family lies almost entirely within those organelles. There are, however, exceptions such as cathepsin K, which works extracellularly after secretion by osteoclasts in bone resorption. Cathepsins have a vital role in mammalian cellular turnover.
== Classification == Cathepsin A (serine protease) Cathepsin B (cysteine protease) Cathepsin C (cysteine protease) Cathepsin D (aspartyl protease) Cathepsin E (aspartyl protease) Cathepsin F (cysteine proteinase) Cathepsin G (serine protease) Cathepsin H (cysteine protease) Cathepsin K (cysteine protease) Cathepsin L1 (cysteine protease) Cathepsin L2 (or V) (cysteine protease) Cathepsin O (cysteine protease) Cathepsin P (mouse cysteine protease) Cathepsin Q (rat cysteine protease) Cathepsin S (cysteine protease) Cathepsin W (cysteine proteinase) Cathepsin Z (or X) (cysteine protease)
Excerpted from Wikipedia’s “cathepsins” article, available under the CC BY-SA 4.0 licence.