Source:http://linkedlifedata.com/resource/pubmed/id/16316412
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
8
|
pubmed:dateCreated |
2005-11-30
|
pubmed:abstractText |
Lysyl oxidase (Lox) is a copper-dependent amine oxidase that catalyzes the cross-linking of collagen and elastin fibers in the extracellular matrix (ECM). In mammals, four closely related Lox-like enzymes have been described that share a highly conserved catalytic domain with Lox. We have characterized Xenopus laevis cDNAs for Lox, Loxl-1, and Loxl-3, and show that they are expressed during early embryonic development. Using RT-PCR we detected maternal transcripts for Xloxl-1, but levels remained low until tailbud stages. Transcripts for Xlox and Xloxl-3 were not detected until early neurulae, although transcripts for Xlox remained at low levels until tailbud stages. Whole mount in situ hybridization showed that transcripts for Xloxl-1 and Xloxl-3 are localized in the notochord, while transcripts for Xlox are found in the notochord, somites, and head. X. laevis Lox-like enzymes were inhibited by incubating embryos, from cleavage stages to tadpole stages, in beta-aminopropionitrile, a specific inhibitor of the catalytic domain. The resulting embryos appeared to differentiate normally but suffered from poor collagen fiber formation. Defects included kinks in the notochord, a posterior shift of the somites, abnormal gut coiling, and the formation of edemas. Our data suggest that Lox-related enzymes are required for the proper formation of the ECM during X. laevis development.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Oct
|
pubmed:issn |
0301-4681
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
73
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
414-24
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:16316412-Amino Acid Sequence,
pubmed-meshheading:16316412-Animals,
pubmed-meshheading:16316412-Molecular Sequence Data,
pubmed-meshheading:16316412-Protein-Lysine 6-Oxidase,
pubmed-meshheading:16316412-Sequence Homology,
pubmed-meshheading:16316412-Time Factors,
pubmed-meshheading:16316412-Xenopus Proteins,
pubmed-meshheading:16316412-Xenopus laevis
|
pubmed:year |
2005
|
pubmed:articleTitle |
Members of the lysyl oxidase family are expressed during the development of the frog Xenopus laevis.
|
pubmed:affiliation |
Department of Anatomy and Developmental Biology University College London Gower Street London WC1E 6BT, U.K.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|