Cathepsin

From Wikipedia, the free encyclopedia

A cathepsin is one of a family of proteases, a type of protein that breaks apart other proteins, found in many types of cells including those in all animals. There are approximately a dozen members of this family, which are distinguished by their structure 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.

The earliest record of "cathepsin" found in PubMed [1] is from the Journal of Biological Chemistry in 1949 (Maver, 1949). However, references within this article indicate that they were first identified and named around the turn of the 20th century. Much of this earlier work was done in the laboratory of Max Bergmann, who spent the first several decades of the century defining these proteases.

[edit] Conditions associated

Cathepsins have been implicated in cancer (Nomura, 2005), stroke (Lipton, 1999), Alzheimer's disease, and arthritis (Pham, 2005).

Cathepsin B seems to actually break down the proteins which cause amyloid plaquethe root of Alzheimer's symptoms, and may even be a pivotal part of the natural defense against this disease used by people who do not get it[2].

[edit] References in medical literature

• Maver and Greco. The hydrolysis of nucleoproteins by cathepsins from calf thymus. J Biol Chem. 1949 Dec;181(2):853-60.
• Nomura and Katunuma. Involvement of cathepsins in the invasion, metastasis and proliferation of cancer cells. J Med Invest. 2005 Feb;52(1-2):1-9. Review.
• Lipton. Ischemic cell death in brain neurons. Physiol Rev. 1999 Oct;79(4):1431-568.
• Pham. Immunity. 2005 Jun
• Bergmann and Fruton. Science 1936; 84(2169):89-90.
• http://de.wikipedia.org/wiki/Max_Bergmann

[edit] See also

• Cathepsin C