Medical Knowledge Cockpit lung cancer, protection against

 

• Chagas disease (American trypanosomiasis)
  Homo sapiens (human) one gene

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• Apoptosis
  Homo sapiens (human) one gene

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MPO

• Purification of myeloperoxidase from equine polymorphonuclear leucocytes

CASP8

• Knock-out of the neural death effector domain protein PEA-15 demonstrates that its expression protects astrocytes from TNFalpha-induced apoptosis
• PED/PEA-15: an anti-apoptotic molecule that regulates FAS/TNFR1-induced apoptosis
• Activation of the NF-kappaB pathway by caspase 8 and its homologs
• ABIN-1 is a ubiquitin sensor that restricts cell death and sustains embryonic development

 

CASP8

This gene encodes a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation ofcaspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymescomposed of a prodomain, a large protease subunit, and a small protease subunit. Activation of caspases requiresproteolytic processing at conserved internal aspartic residues to generate a heterodimeric enzyme consisting ofthe large and small subunits. This protein is involved in the programmed cell death induced by Fas and variousapoptotic stimuli. The N-terminal FADD-like death effector domain of this protein suggests that it may interactwith Fas-interacting protein FADD. This protein was detected in the insoluble fraction of the affected brainregion from Huntington disease patients but not in those from normal controls, which implicated the role inneurodegenerative diseases. Many alternatively spliced transcript variants encoding different isoforms have beendescribed, although not all variants have had their full-length sequences determined. (provided by RefSeq, Jul2008)

This gene encodes a member of the cysteine-aspartic acid protease (caspase) family

Sequential activation ofcaspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymescomposed of a prodomain, a large protease subunit, and a small protease subunit. Activation of caspases requiresproteolytic processing at conserved internal aspartic residues to generate a heterodimeric enzyme consisting ofthe large and small subunits. This protein is involved in the programmed cell death induced by Fas and variousapoptotic stimuli. The N-terminal FADD-like death effector domain of this protein suggests that it may interactwith Fas-interacting protein FADD. This protein was detected in the insoluble fraction of the affected brainregion from Huntington disease patients but not in those from normal controls, which implicated the role inneurodegenerative diseases. Many alternatively spliced transcript variants encoding different isoforms have beendescribed, although not all variants have had their full-length sequences determined. (provided by RefSeq, Jul2008)

 

CASP8

Somatic tumors

hepatocellular, oral squamous cell, breast

Tumor types germline

Cancer Syndrom

Translocation partner

Name

caspase 8, apoptosis-related cysteine peptidase

Chromosome banding

2q33-q34

Cancer molecular gen.

Rec

Mutation type

N, S, F

Other syndrome disease