PMID- 10194414
OWN - NLM
STAT- MEDLINE
DCOM- 19990707
LR  - 20061115
IS  - 0021-9533 (Print)
IS  - 0021-9533 (Linking)
VI  - 112 ( Pt 9)
DP  - 1999 May
TI  - HP33: hepatocellular carcinoma-enriched 33-kDa protein with similarity to
      mitochondrial N-acyltransferase but localized in a microtubule-dependent manner
      at the centrosome.
PG  - 1353-64
AB  - Using a new subtraction method and chemically induced rat hepatocellular
      carcinomas, we identified a hepatocellular carcinogenesis and hepatocyte
      proliferation-related gene designated hp33 that encoded a 33-kDa protein. The
      predicted protein was similar to the bovine aralkyl N-acyltransferase and
      arylacetyl N-acyltransferase. HP33 was restrictively expressed in the liver and
      kidney, and its gene expression was stimulated in the regenerating liver as well 
      as in hepatocellular carcinoma. Interestingly, it was demonstrated in various
      hepatic cells that HP33 was localized in regions surrounding the centrosome,
      where mitochondria were not concentrated. Moreover, its centrosomal localization 
      was evident in the interphase but not in the mitotic phase of the cell cycle. The
      centrosomal localization of HP33 was dependent on microtubules, and ectopically
      expressed HP33 was seen at centrosomes even in fibroblasts, which do not exhibit 
      a typical staining pattern of HP33. The centrosomal localization of HP33 became
      invisible by nocodazole treatment, whereas the mitochondrial staining pattern was
      not affected by it. In vitro cosedimentation experiments using purified
      microtubules indicated that HP33 bound to MTs directly and that its MT-binding
      ability was dependent on the C-terminal basic domain of the protein. These
      results suggest that, different from early predictions based on its primary
      structure, HP33 has a growth- and carcinogenesis-related function that may be
      independent of mitochondrial function.
FAU - Nakadai, T
AU  - Nakadai T
AD  - Department of Biology, Faculty of Science, Chiba University, Inage-ku, Chiba
      263-8522, Japan.
FAU - Kishimoto, T
AU  - Kishimoto T
FAU - Miyazawa, Y
AU  - Miyazawa Y
FAU - Okada, N
AU  - Okada N
FAU - Makino, Y
AU  - Makino Y
FAU - Obinata, T
AU  - Obinata T
FAU - Tamura, T
AU  - Tamura T
LA  - eng
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - J Cell Sci
JT  - Journal of cell science
JID - 0052457
RN  - 0 (Neoplasm Proteins)
RN  - EC 2.3.- (Acyltransferases)
SB  - IM
MH  - Acyltransferases/*analysis
MH  - Amino Acid Sequence
MH  - Animals
MH  - Carcinoma, Hepatocellular/*chemistry
MH  - Cell Cycle/physiology
MH  - Centrosome/*chemistry/ultrastructure
MH  - Humans
MH  - Liver Neoplasms/*chemistry
MH  - Microtubules/*chemistry
MH  - Mitochondria/*enzymology
MH  - Molecular Sequence Data
MH  - Molecular Weight
MH  - Neoplasm Proteins/*analysis
MH  - Protein Binding
MH  - Protein Structure, Tertiary
MH  - Rats
MH  - Sequence Homology, Amino Acid
EDAT- 1999/04/09 00:00
MHDA- 1999/04/09 00:01
CRDT- 1999/04/09 00:00
PHST- 1999/04/09 00:00 [pubmed]
PHST- 1999/04/09 00:01 [medline]
PHST- 1999/04/09 00:00 [entrez]
PST - ppublish
SO  - J Cell Sci. 1999 May;112 ( Pt 9):1353-64.