MENU
Anatomy
Anesthesiology
Biochemistry
Biomedical Informatics
Biophysics
Cell Biology
Clinical Cases
Dentistry
Dermatovenerology
Emergency Medicine
Family Medicine
Forensic Medicine
Gynecology and Obstetrics
Histology and Embryology
History of Medicine
Human Genetics
Hygiene
Infectious Diseases
Internal Medicine
Medical Deontology and Philosophy
Medical Psychology
Microbiology and Immunology
Neurology
Occupational Medicine
Oncology
Ophthalmology
Orthopaedics
Otorhinolaryngology
Pathology
Pathophysiology
Pediatrics
Pharmacology and Experimental Toxicology
Physical and Rehabilitation Medicine
Physiology
Psychiatry
Radiology
Social Medicine
Surgery
Toxicology
Research papers
Clinical research paper
Preclinical research paper
Sponsored articles
Archive » 2001 » 3 » | Archive » Medical field » Fields » History of Medicine »

Caspases

 
Abstract:

This post is also available in: enEnglish slSlovenščina (Slovenian)

Caspases are cysteine proteases, which cleave their substrates following an aspartate residue. They are present as inactive precursors (pro-caspases) in cells. Caspases are involved in cytokine processing and apoptosis (programmed cell death) regulation. Apoptotic caspases are acti­vator caspases (caspases 8 and 9) or effector caspases (caspases 3 and 7). Apoptosis can be initiated by either extracellular or intracellular pathways. Extracellular signals mediate apop­tosis by death receptors, which activate caspase 8. Intracellular signals provoke changes in the permeability of the outer mitochondrial membrane which permits cytochrome C release from mitochondria. In the cytosol, cytochrome C allows activation of caspase 9. Activated caspases 8 and/or 9 induce cascade activation of effector caspases which cleave different tar­get proteins. Demolition of target proteins plays an important role in morphological changes of apoptotic cells.

Authors:
Pižem Jože, Cör Andrej

Keywords:
caspases, apoptosis

Cite as:
Med Razgl. 2001; 40: 283−91.

Download PDF >>
© 2019 Društvo Medicinski razgledi | Na vrh strani / To top ↑