Linked Life Data

8853991

Source:http://linkedlifedata.com/resource/pubmed/id/8853991

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1997-3-14
pubmed:databankReference
pubmed:abstractText
We have identified the Xenopus homologue of mammalian FGF-9 (XFGF-9). Sequence comparison between Xenopus and mammals shows that they share 93% identity at the amino acid level, making FGF-9 the most highly conserved member within the family. The sequence shows that there is no N-terminal signal sequence but that there is an internal hydrophobic sequence resembling a transmembrane domain. By using an in vitro translation system, we demonstrate that XFGF-9 can be glycosylated by microsomes but shows no signal peptide cleavage. This suggests that it can be secreted using the internal hydrophobic domain to cross the endoplasmic reticulum membrane. Expression studies using RNAse protections and in situ hybridization show that XFGF-9 is expressed both maternally and zygotically. The maternal mRNA is detected at a higher level than other forms (XFGF-2 and eFGF), mainly in the animal hemisphere. A proportion of the maternal transcript persists until the early gastrula stage when it is joined by zygotic expression around the blastopore region, and thereafter the mRNA content shows some increase during further development. Zygotic XFGF-9 is expressed uniformly along the dorsal axis, as well as in the head region. We have expressed recombinant XFGF-9 protein in bacteria, and show that it has a mesoderm-inducing activity in the animal cap assay, with a similar specific activity to other fibroblast growth factor (FGFs). We have injected a synthetic mRNA into eggs, and show that it has both mesoderm-inducing activity in animal caps and also a posteriorizing activity in whole embryos. The levels of biological activity shown by the XFGF-9 mRNA injections compared to XFGF-2 and eFGF show that there is at least some extracellular function. This supports the biochemical results, suggesting that the protein has at least some capacity to be secreted.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
1058-8388
pubmed:author
pubmed:issnType
Print
pubmed:volume
206
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
427-36
pubmed:dateRevised
2009-9-29
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
XFGF-9: a new fibroblast growth factor from Xenopus embryos.
pubmed:affiliation
Whitehead Institute for Biomedical Research, Cambridge, Massachusetts 02412-1479, USA.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't