Journal
NUCLEOSIDES NUCLEOTIDES & NUCLEIC ACIDS
Volume 25, Issue 9-11, Pages 1271-1276Publisher
TAYLOR & FRANCIS INC
DOI: 10.1080/15257770600890921
Keywords
cervix; epithelium; P2X7; receptor; truncated; variant; apoptosis
Categories
Funding
- NHLBI NIH HHS [HL65492] Funding Source: Medline
- NIA NIH HHS [AG15955] Funding Source: Medline
- NICHD NIH HHS [HD29924] Funding Source: Medline
- EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH &HUMAN DEVELOPMENT [R29HD029924] Funding Source: NIH RePORTER
- NATIONAL HEART, LUNG, AND BLOOD INSTITUTE [R01HL065492] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE ON AGING [R01AG015955, R55AG015955] Funding Source: NIH RePORTER
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A truncated naturally occurring variant of the human purinergic receptor P2X7 ( P2X7-R) was found in human cancer cervical cells. The novel protein consists of 258 amino acids, and compared to the wild-type P2X7-R it lacks the entire intracellular carboxy terminus, the second transmembrane domain, and the distal third of the extracellular loop. The truncated P2X7-R failed to form pores and mediate apoptosis, and it interacted with the wild-type P2X7-R in a manner suggesting auto-hetero-oligomerization. In contrast to cancer cells the novel truncated P2X7-R was expressed relatively little in normal cervical cells. These data raise the possibility that coexpression of the truncated form could block P2X7 mediated apoptosis and promote uncontrolled growth of cells.
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