rdf:type |
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lifeskim:mentions |
|
pubmed:issue |
3
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pubmed:dateCreated |
2002-2-12
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pubmed:abstractText |
During early development, cells receive positional information from neighboring cells to form tissue patterns in initially uniform germ layers. Ligands of the transforming growth factor (TGF-beta) superfamily are known to participate in this pattern formation. In particular, activin has been shown to act as a long-range dorsalizing signal to establish a concentration gradient in Xenopus. In contrast, BMP-2 and BMP-4, other members of the family, appear to influence and induce ventral fates only where they are expressed. This raises a question as to how the action of BMPs is tightly restricted to the region within and around the cells that produce them. Here, we have demonstrated that a basic core of only three amino acids in the N-terminal region of BMP-4 is required for its restriction to the non-neural ectoderm as its expression domain. Our results also suggest that heparan sulfate proteoglycans bind to this basic core and thus play a role in trapping BMP-4. The present study is the first to identify the critical domain of BMP that is responsible for its interaction with the extracellular environment that restricts its diffusion in vivo.
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/BMP2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/BMP4 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Bone Morphogenetic Protein 2,
http://linkedlifedata.com/resource/pubmed/chemical/Bone Morphogenetic Protein 4,
http://linkedlifedata.com/resource/pubmed/chemical/Bone Morphogenetic Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Transforming Growth Factor beta,
http://linkedlifedata.com/resource/pubmed/chemical/Xenopus Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/bmp4 protein, Xenopus
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
|
pubmed:issn |
0960-9822
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:day |
5
|
pubmed:volume |
12
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
205-9
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:11839272-Amino Acid Sequence,
pubmed-meshheading:11839272-Animals,
pubmed-meshheading:11839272-Blotting, Western,
pubmed-meshheading:11839272-Bone Morphogenetic Protein 2,
pubmed-meshheading:11839272-Bone Morphogenetic Protein 4,
pubmed-meshheading:11839272-Bone Morphogenetic Proteins,
pubmed-meshheading:11839272-Humans,
pubmed-meshheading:11839272-In Situ Hybridization,
pubmed-meshheading:11839272-Mutation,
pubmed-meshheading:11839272-RNA, Messenger,
pubmed-meshheading:11839272-Structure-Activity Relationship,
pubmed-meshheading:11839272-Transforming Growth Factor beta,
pubmed-meshheading:11839272-Xenopus Proteins,
pubmed-meshheading:11839272-Xenopus laevis
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pubmed:year |
2002
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pubmed:articleTitle |
Action range of BMP is defined by its N-terminal basic amino acid core.
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pubmed:affiliation |
Division of Morphogenesis, Department of Development Biology, National Institute for Basic Biology, Okazaki, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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