Caspases: Difference between revisions
m I only made few adjustments on rearranging some sentences. |
some reference from old school wiki's document and some from other website references |
||
| Line 1: | Line 1: | ||
Caspases are a crucial element in the process of [[Apoptosis|apoptosis]]. They are a type of enzyme called [[Proteases|proteases]] and have a [[Cysteine|cysteine]] molecule in the active site. Their target proteins are specific aspartic acids. Caspases are made within the [[Cell|cell]] as an inactive form, [[Procaspases|procaspases]]. Activation occurs by proteolytic cleavage at one or two aspartic acids and catalysed by | "Caspases are a crucial element in the process of [[Apoptosis|apoptosis]]. They are a type of enzyme called [[Proteases|proteases]] and have a [[Cysteine|cysteine]] molecule in the active site. Their target proteins are specific aspartic acids. Caspases are made within the [[Cell|cell]] as an inactive form, [[Procaspases|procaspases]]. Activation occurs by proteolytic cleavage at one or two aspartic acids"[1] and catalysed by <span style="line-height: 1.5em;">activated caspases. Each activated caspades molecule will cleave many procaspase molecules."Once activated an amplifying proteolytic cascade is formed thus activating other procaspases."[1]</span> | ||
The leakage of | "The leakage of Cytochrome C from the mitochondial intermembrane space initiates the activation of the first caspases. In apoptosis, there are two forms of caspase that are used"[1] : "initiator caspases (caspase-8,-9) and executioner caspases (-3,-6 and -7). " [2] "Initiator pro-caspases will be activated first, and then go onto cleave and activate the executioner pro-caspases."[1]<br> | ||
The activated caspases progress apoptosis by cleaving [[Nuclear lamins|nuclear lamins]], which leads to nuclear fragmentation. [[DNase|DNase]] is activated and fragements the cell [[DNA|DNA]] and DNase inhibitor is cleaved. The cell detaches from it's neighbours through caspases cleaving the [[Cytoskeleton|cytoskeleton]]. This leads to loss of communication with the extracellular | "The activated caspases progress apoptosis by cleaving [[Nuclear lamins|nuclear lamins]], which leads to nuclear fragmentation. [[DNase|DNase]] is activated and fragements the cell [[DNA|DNA]] and DNase inhibitor is cleaved. The cell detaches from it's neighbours through caspases cleaving the [[Cytoskeleton|cytoskeleton]]."[4] "This leads to loss of communication with the extracellular matrix." | ||
<span style="line-height: 1.5em;">"Several caspases are mediators of innate immune response (caspase-1, -4, -5, -12 in humans and caspase-1, -11, and -12 in mice)." [3]</span> | |||
<references /> | |||
1. School of Biomedical Science Wiki, https://teaching.ncl.ac.uk/bms/wiki/index.php/Caspases | |||
2.<span style="line-height: 1.5em;">David R. McIlwain1,2, Thorsten Berger1 and Tak W. Mak</span> | |||
The Campbell Family Institute for Breast Cancer Research and Ontario Cancer Institute, University Health Network, Toronto, Ontario M5G 2C1, Canada<br>↵2 Present address: Department of Gastroenterology, Hepatology and Infectious Diseases, University of Düsseldorf, 40225 Düsseldorf, Germany | |||
http://cshperspectives.cshlp.org/content/5/4/a008656.fullhttp://cshperspectives.cshlp.org/content/5/4/a008656.full | |||
3. <span style="line-height: 1.5em;">Department of Immunology, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, USA.Apoptosis. 2002 Aug;7(4):313-9.</span> | |||
http://www.ncbi.nlm.nih.gov/pubmed/12101390 | |||
4.James W. Wilson, Catherine Booth, Christopher S. PottenApoptosis Genes page 2Springer Science & Business Media. Copyright.<span style="line-height: 1.5em;"> </span> | |||
<span style="line-height: 1.5em;" /><span style="font-family: Helvetica; line-height: normal; -webkit-text-stroke-color: rgb(0, 0, 0); -webkit-text-stroke-width: initial;">https://books.google.com.my/books?id=7Z_xBwAAQBAJ&pg=PA2&lpg=PA2&dq=will+cell+detach+from+neighbour+cell+through+apoptosis&source=bl&ots=Z-VE0Tiq8s&sig=1e5VZL2khGegHM-n58LCLaeNvK4&hl=en&sa=X&redir_esc=y#v=onepage&q=will%20cell%20detach%20from%20neighbour%20cell%20through%20apoptosis&f=falseedited</span><span style="font-family: Helvetica; line-height: normal; -webkit-text-stroke-color: rgb(0, 0, 0); -webkit-text-stroke-width: initial;"> </span> | |||
Revision as of 14:36, 21 November 2015
"Caspases are a crucial element in the process of apoptosis. They are a type of enzyme called proteases and have a cysteine molecule in the active site. Their target proteins are specific aspartic acids. Caspases are made within the cell as an inactive form, procaspases. Activation occurs by proteolytic cleavage at one or two aspartic acids"[1] and catalysed by activated caspases. Each activated caspades molecule will cleave many procaspase molecules."Once activated an amplifying proteolytic cascade is formed thus activating other procaspases."[1]
"The leakage of Cytochrome C from the mitochondial intermembrane space initiates the activation of the first caspases. In apoptosis, there are two forms of caspase that are used"[1] : "initiator caspases (caspase-8,-9) and executioner caspases (-3,-6 and -7). " [2] "Initiator pro-caspases will be activated first, and then go onto cleave and activate the executioner pro-caspases."[1]
"The activated caspases progress apoptosis by cleaving nuclear lamins, which leads to nuclear fragmentation. DNase is activated and fragements the cell DNA and DNase inhibitor is cleaved. The cell detaches from it's neighbours through caspases cleaving the cytoskeleton."[4] "This leads to loss of communication with the extracellular matrix."
"Several caspases are mediators of innate immune response (caspase-1, -4, -5, -12 in humans and caspase-1, -11, and -12 in mice)." [3]
1. School of Biomedical Science Wiki, https://teaching.ncl.ac.uk/bms/wiki/index.php/Caspases
2.David R. McIlwain1,2, Thorsten Berger1 and Tak W. Mak
The Campbell Family Institute for Breast Cancer Research and Ontario Cancer Institute, University Health Network, Toronto, Ontario M5G 2C1, Canada
↵2 Present address: Department of Gastroenterology, Hepatology and Infectious Diseases, University of Düsseldorf, 40225 Düsseldorf, Germany
3. Department of Immunology, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, USA.Apoptosis. 2002 Aug;7(4):313-9.
http://www.ncbi.nlm.nih.gov/pubmed/12101390
4.James W. Wilson, Catherine Booth, Christopher S. PottenApoptosis Genes page 2Springer Science & Business Media. Copyright.