Caspase: Difference between revisions

From The School of Biomedical Sciences Wiki
Jump to navigation Jump to search
No edit summary
Nnjm2 (talk | contribs)
No edit summary
Line 1: Line 1:
<span style="line-height: 1.5em; font-size: 13.28px;">Capsases belong to a subfamily of </span>[[Proteases|proteases]]&nbsp;known as endopeptidases<span style="line-height: 1.5em; font-size: 13.28px;">&nbsp;which cleave target </span>[[Protein|proteins]]&nbsp;<span style="line-height: 1.5em; font-size: 13.28px;">&nbsp;at specific </span>[[Aspartic acid|aspartic acids]]<span style="line-height: 1.5em; font-size: 13.28px;">. They hydrolze petide bonds C-terminally in aspartate residues.<ref>Marks F, Klingmuller U, Muller-Decker K, (2009)fckLRCellular Signalling Processing 1st edition page 465fckLRGarland Science 2009</ref> The caspases have </span>[[Cysteine|cysteine]]<span style="line-height: 1.5em; font-size: 13.28px;"> at their </span>[[Enzyme active site|active site]]<span style="line-height: 1.5em; font-size: 13.28px;"> and are named due to the 'C' for </span>[[Cysteine|cysteine]]<span style="line-height: 1.5em; font-size: 13.28px;"> and the 'asp' for </span>[[Aspartic acid|aspartic acid]]<span style="line-height: 1.5em; font-size: 13.28px;">. Caspases are synthesised in the cell as </span>[[Procaspases|procaspases]]<span style="line-height: 1.5em; font-size: 13.28px;">&nbsp;</span><ref>Alberts et al (2008) Molecular Biology of the Cell, 6th Edition, New York: Garland Science</ref><span style="line-height: 1.5em; font-size: 13.28px;">.</span>  
Capsases belong to a subfamily of [[Proteases|proteases]] known as endopeptidases which cleave target [[Protein|proteins]] at specific [[Aspartic acid|aspartic acids]]. They hydrolze petide bonds C-terminally in aspartate residues.<ref>Marks F, Klingmuller U, Muller-Decker K, (2009)fckLRCellular Signalling Processing 1st edition page 465fckLRGarland Science 2009</ref> The caspases have [[Cysteine|cysteine]] at their [[Enzyme active site|active site]] and are named due to the 'C' for [[Cysteine|cysteine]] and the 'asp' for [[Aspartic acid|aspartic acid]]. Caspases are synthesised in the cell as [[Procaspases|procaspases]] <ref>Alberts et al (2008) Molecular Biology of the Cell, 6th Edition, New York: Garland Science</ref>.<br>  


<br>
=== Capases and [[Apoptosis|Apoptosis]] ===
 
'''Capases and [[Apoptosis|Apoptosis]]'''
 
----


Capases are responsible for the programmed death of a cell. In their inactive state capases are present as zymogens, precapases or blocked by specific capases inhibitors. When [[Javascript:void(0);/*1448212232783*/|apoptosis]] is triggered the capases activate each other forming a cascade. The signal becomes amplified along the cascade and leads to the death of the cell.  
Capases are responsible for the programmed death of a cell. In their inactive state capases are present as zymogens, precapases or blocked by specific capases inhibitors. When [[Javascript:void(0);/*1448212232783*/|apoptosis]] is triggered the capases activate each other forming a cascade. The signal becomes amplified along the cascade and leads to the death of the cell.  
<br>
<br>


=== References  ===
=== References  ===


<references /><br>
<references />

Revision as of 04:22, 23 November 2015

Capsases belong to a subfamily of proteases known as endopeptidases which cleave target proteins at specific aspartic acids. They hydrolze petide bonds C-terminally in aspartate residues.[1] The caspases have cysteine at their active site and are named due to the 'C' for cysteine and the 'asp' for aspartic acid. Caspases are synthesised in the cell as procaspases [2].

Capases and Apoptosis

Capases are responsible for the programmed death of a cell. In their inactive state capases are present as zymogens, precapases or blocked by specific capases inhibitors. When apoptosis is triggered the capases activate each other forming a cascade. The signal becomes amplified along the cascade and leads to the death of the cell.

References

  1. Marks F, Klingmuller U, Muller-Decker K, (2009)fckLRCellular Signalling Processing 1st edition page 465fckLRGarland Science 2009
  2. Alberts et al (2008) Molecular Biology of the Cell, 6th Edition, New York: Garland Science