Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: UMLS:C0019204 (
hepatocellular carcinoma
)
71,386
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
A novel splice variant of
hPirh2
, named hPirh2b, was isolated from human fetal liver cDNA library. hPirh2b has a 38-nucleotide deletion and encodes a 188-amino acid protein with a truncated RING-H2 domain. It shows no ubiquitin protein ligase activity. A low level of expression of
hPirh2
was found both at transcriptional and translational level in human
hepatocellular carcinoma
(
HCC
) when compared to non-cancerous tissue. Statistical analysis showed that the low expression is associated with lack of differentiation of
HCC
. In direct binding studies hPirh2b bound p53 indicating that RING-H2 domain is not needed for this interaction.
...
PMID:A novel hPirh2 splicing variant without ubiquitin protein ligase activity interacts with p53 and is down-regulated in hepatocellular carcinoma. 2045 52
Hepatocellular carcinoma
(
HCC
) is one of the most common malignancies in the world, especially in China. Recent researches have shown that E3 ubiquitin ligases Pirh2 (
p53-induced RING-H2 protein
) is highly expressed in
HCC
cell lines and is correlated with poor survival and prognostic in patients with
HCC
; however, the function of Pirh2 in the genesis and the development of
HCC
remains unclear. Pirh2, a member of the RING finger family, can target p53 for degradation and thereby repress a diverse group of biological activities and involved in many signalling pathways related to the genesis and evolution of cancer. Up to now, four Pirh2 variants had been reported and named Pirh2A, Pirh2B, Pirh2C and Pirh2D. Here we report the existence of two additional isoforms from human hepatocellular liver carcinoma cell line (HepG2 cell) and named as Pirh2E and Pirh2F. Compared to full-length Pirh2A, Pirh2E lacks amino acids 235-261, while Pirh2F is missing C-terminal amino acids 227-261 and both isoforms harbor the RING domain; therefore, we speculate that ubiquitin ligase activity maybe reversed by them. Further studies are required to determine whether Pirh2E and Pirh2F functions in a manner similar to Pirh2A.
...
PMID:Identification of Pirh2E and Pirh2F, two additional novel isoforms of Pirh2 ubiquitin ligase from human hepatocellular liver carcinoma cell line. 2276 6
