Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1996-2-26
pubmed:abstractText
Glycolipid sulfotransferase activity in a human renal cancer cell line, SMKT-R3, is enhanced by the action of growth factors such as EGF, TGF-alpha and HGF, whose receptors possess tyrosine kinase domains. We investigated whether tyrosine kinases are involved in the regulation of the sulfotransferase in the cells by using specific tyrosine kinase inhibitors. Genistein and tyrphostin 51 not only cancelled the enhancement of the sulfotransferase by EGF but also reduced the enzyme level to a point much lower than that seen in non-treated cells, whereas they did not affect the sulfotransferase activity in vitro. The activity-reducing effects of genistein were dose- and time-dependent. Genistein also inhibited the cell growth of SMKT-R3 cells. Western blotting using anti-phosphotyrosine monoclonal antibody revealed a tyrosine-phosphorylated protein with an apparent molecular mass of 116 kDa in the non-treated cells. The EGF receptor was tyrosine-phosphorylated by the addition of EGF. The phosphorylations of the 116 kDa protein and EGF receptor were attenuated by co-incubation with genistein. These results indicate that tyrosine kinases including the EGF receptor are involved in the growth of SMKT-R3 cells and in the regulatory mechanisms of glycolipid sulfotransferase in the cells.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
1299
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
141-5
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Regulation of glycolipid sulfotransferase by tyrosine kinases in human renal cancer cells.
pubmed:affiliation
Biochemistry Laboratory, Hokkaido University School of Medicine, Sapporo, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't