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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
1996-5-20
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pubmed:abstractText |
Ras oncogene encode a protein p2l which in its mutated form transforms mammalian cells only after membrane anchoring by a series of enzymatic reactions where the initial step is catalyzed by farnesyltransferase (FTase). For this reason, FTase has become an attractive target for the development of novel anticancer agents. Virtually nothing is known about FTase activity and the association between the expression of its alpha and beta subunit genes with respect to the processing of Ras p21 in human cancers. In this study, we found that compared to normal skin, FTase activity and levels of both cytosolic and membrane-bound Ha-Ras p21 were significantly higher in human skin basal cell carcinomas (BCCs). In addition, the expression of both alpha and beta subunit genes was significantly higher in BCCs than the normal skin. These results suggest an association between enhanced FTase activity and the processing of overexpressed Ras p21 in such tumor type. This may have a bearing on the pathogenesis of activated Ras oncogene containing human malignancies.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Alkyl and Aryl Transferases,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Primers,
http://linkedlifedata.com/resource/pubmed/chemical/Farnesyltranstransferase,
http://linkedlifedata.com/resource/pubmed/chemical/HRAS protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Hypoxanthine...,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins p21(ras),
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Transferases
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0006-291X
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
27
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pubmed:volume |
220
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
795-801
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:8607844-Alkyl and Aryl Transferases,
pubmed-meshheading:8607844-Base Sequence,
pubmed-meshheading:8607844-Carcinoma, Basal Cell,
pubmed-meshheading:8607844-DNA, Complementary,
pubmed-meshheading:8607844-DNA Primers,
pubmed-meshheading:8607844-Farnesyltranstransferase,
pubmed-meshheading:8607844-Gene Expression,
pubmed-meshheading:8607844-Genes, ras,
pubmed-meshheading:8607844-Humans,
pubmed-meshheading:8607844-Hypoxanthine Phosphoribosyltransferase,
pubmed-meshheading:8607844-Macromolecular Substances,
pubmed-meshheading:8607844-Molecular Sequence Data,
pubmed-meshheading:8607844-Polymerase Chain Reaction,
pubmed-meshheading:8607844-Proto-Oncogene Proteins p21(ras),
pubmed-meshheading:8607844-RNA, Messenger,
pubmed-meshheading:8607844-Reference Values,
pubmed-meshheading:8607844-Skin,
pubmed-meshheading:8607844-Skin Neoplasms,
pubmed-meshheading:8607844-Transferases
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pubmed:year |
1996
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pubmed:articleTitle |
Farnesyltransferase activity and mRNA expression in human skin basal cell carcinomas.
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pubmed:affiliation |
Department of Dermatology, Case Western Reserve University, Cleveland, Ohio 44106-5028, USA.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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