Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2001-1-16
pubmed:abstractText
Teneurin-2 is a member of a novel family of transmembrane proteins characterized to date in fish, birds, mammals, and Drosophila (e.g., the pair-rule gene product Ten-m). We have shown that teneurin-2 is expressed by neurons in the developing avian visual system in a pattern complementary to the expression of teneurin-1 and that recombinant teneurin-2 induces morphologic changes in neuronal cells in culture (Rubin et al., 1999). Here we have used cRNA probes to two newly identified splice variants and a teneurin-2-specific antibody to determine whether teneurin-2 is also expressed outside the nervous system. Both reverse transcriptase-polymerase chain reaction and in situ hybridization indicate that the three splice variants known so far are coexpressed at sites of pattern formation during development. Teneurin-2 mRNAs and protein are found in the developing limbs, somites, and craniofacial mesenchyme. In addition to expression of teneurin-2 by the apical ectodermal ridge, teneurin-2 transcripts also appear transiently at sites of tendon development. Teneurin-2 expression patterns were strikingly similar to those of fibroblast growth factor 8 (FGF8). In agreement with the overlapping expression pattern, FGF8-coated beads implanted into chicken limb buds induced the ectopic expression of teneurin-2 and soluble FGF8 induced teneurin-2 in limb explant cultures. Thus, teneurin-2 could act downstream of FGF8 during morphogenesis.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
1058-8388
pubmed:author
pubmed:copyrightInfo
Copyright 2001 Wiley-Liss, Inc.
pubmed:issnType
Print
pubmed:volume
220
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
27-39
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed-meshheading:11146505-Alternative Splicing, pubmed-meshheading:11146505-Amino Acid Sequence, pubmed-meshheading:11146505-Animals, pubmed-meshheading:11146505-Avian Proteins, pubmed-meshheading:11146505-Chick Embryo, pubmed-meshheading:11146505-Cloning, Molecular, pubmed-meshheading:11146505-Embryo, Nonmammalian, pubmed-meshheading:11146505-Extremities, pubmed-meshheading:11146505-Fibroblast Growth Factor 8, pubmed-meshheading:11146505-Fibroblast Growth Factors, pubmed-meshheading:11146505-Gene Library, pubmed-meshheading:11146505-Immunohistochemistry, pubmed-meshheading:11146505-In Situ Hybridization, pubmed-meshheading:11146505-Limb Buds, pubmed-meshheading:11146505-Membrane Proteins, pubmed-meshheading:11146505-Mesoderm, pubmed-meshheading:11146505-Molecular Sequence Data, pubmed-meshheading:11146505-Nerve Tissue Proteins, pubmed-meshheading:11146505-Nervous System, pubmed-meshheading:11146505-Organ Culture Techniques, pubmed-meshheading:11146505-RNA, Complementary, pubmed-meshheading:11146505-RNA, Messenger, pubmed-meshheading:11146505-Receptors, Fibroblast Growth Factor, pubmed-meshheading:11146505-Reverse Transcriptase Polymerase Chain Reaction, pubmed-meshheading:11146505-Sequence Homology, Amino Acid, pubmed-meshheading:11146505-Signal Transduction, pubmed-meshheading:11146505-Somites, pubmed-meshheading:11146505-Tendons, pubmed-meshheading:11146505-Time Factors
pubmed:year
2001
pubmed:articleTitle
Teneurin-2 is expressed in tissues that regulate limb and somite pattern formation and is induced in vitro and in situ by FGF8.
pubmed:affiliation
Department of Cell Biology and Human Anatomy, University of California at Davis, Davis, California.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't