Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
48
pubmed:dateCreated
2000-1-6
pubmed:abstractText
Keratinocyte growth factor (KGF) is a potent and specific mitogen for epithelial cells, including the keratinocytes of the skin. We investigated the mechanisms of action of KGF by searching for genes which are regulated by this growth factor in cultured human keratinocytes. Using the differential display RT-PCR technology we identified the gene encoding adenylosuccinate lyase [EC 4.3.2.2] as a novel KGF-regulated gene. Adenylosuccinate lyase plays an important role in purine de novo synthesis. To gain further insight into the potential role of nucleotide biosynthesis in the mitogenic effect of KGF, we cloned cDNA fragments of the key regulatory enzymes involved in purine and pyrimidine metabolism (adenylosuccinate synthetase [EC 6.3.4.4], phosphoribosyl pyrophosphate synthetase [EC 2.7.6.1], amidophosphoribosyl transferase [EC 2.4.2.14], hypoxanthine guanine phosphoribosyl transferase [EC 2.4.2.8] and the multifunctional protein CAD which includes the enzymatic activities of carbamoyl-phosphate synthetase II [EC 6.3.5.59], aspartate transcarbamylase [EC 2.1.3.2] and dihydroorotase [EC 3.5.2.3]). Expression of all of these enzymes was upregulated after treatment with KGF and also with epidermal growth factor (EGF), indicating that these mitogens stimulate nucleotide production by induction of these enzymes. To determine a possible in vivo correlation between the expression of KGF, EGF and the enzymes mentioned above, we analysed the expression of the enzymes during cutaneous wound repair, where high levels of these mitogens are present. Indeed, we found a strong mRNA expression of all of these enzymes in the EGF- and KGF-responsive keratinocytes of the hyperproliferative epithelium at the wound edge, indicating that their expression might also be regulated by growth factors during wound healing.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/DNA Primers, http://linkedlifedata.com/resource/pubmed/chemical/Epidermal Growth Factor, http://linkedlifedata.com/resource/pubmed/chemical/FGF7 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Fgf7 protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Fibroblast Growth Factor 10, http://linkedlifedata.com/resource/pubmed/chemical/Fibroblast Growth Factor 7, http://linkedlifedata.com/resource/pubmed/chemical/Fibroblast Growth Factors, http://linkedlifedata.com/resource/pubmed/chemical/Growth Substances, http://linkedlifedata.com/resource/pubmed/chemical/Purine Nucleotides, http://linkedlifedata.com/resource/pubmed/chemical/Pyrimidine Nucleotides, http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0950-9232
pubmed:author
pubmed:issnType
Print
pubmed:day
18
pubmed:volume
18
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
6667-76
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:10597272-Animals, pubmed-meshheading:10597272-Base Sequence, pubmed-meshheading:10597272-Cloning, Molecular, pubmed-meshheading:10597272-DNA Primers, pubmed-meshheading:10597272-Epidermal Growth Factor, pubmed-meshheading:10597272-Fibroblast Growth Factor 10, pubmed-meshheading:10597272-Fibroblast Growth Factor 7, pubmed-meshheading:10597272-Fibroblast Growth Factors, pubmed-meshheading:10597272-Gene Expression Regulation, Enzymologic, pubmed-meshheading:10597272-Growth Substances, pubmed-meshheading:10597272-Humans, pubmed-meshheading:10597272-Mice, pubmed-meshheading:10597272-Mice, Inbred BALB C, pubmed-meshheading:10597272-Purine Nucleotides, pubmed-meshheading:10597272-Pyrimidine Nucleotides, pubmed-meshheading:10597272-RNA, Messenger, pubmed-meshheading:10597272-Reverse Transcriptase Polymerase Chain Reaction, pubmed-meshheading:10597272-Skin
pubmed:year
1999
pubmed:articleTitle
Growth factor-regulated expression of enzymes involved in nucleotide biosynthesis: a novel mechanism of growth factor action.
pubmed:affiliation
Max-Planck-Institute of Biochemistry, Martinsried, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't