Linked Life Data

11891989

Source:http://linkedlifedata.com/resource/pubmed/id/11891989

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2002-3-13
pubmed:abstractText
It has been suggested that a family of tissue remodelling enzymes called matrix metalloproteinases (MMPs) play a causal role in the process of tail resorption during thyroid hormone-induced metamorphosis of the anuran tadpole; however, this hypothesis has never been directly substantiated. We cloned two new Xenopus MMPs, gelatinase A (MMP-2) and MT3-MMP (MMP-16), and the MMP inhibitor TIMP-2. These clones were used along with several others to perform a comprehensive expression study. We show that all MMPs and TIMP-2 are dramatically induced in the resorbing tail during spontaneous metamorphosis and are spatially coexpressed, primarily in the remodelling mesenchymal tissues. By Northern blotting, we show that all the examined MMPs/TIMP-2 are also induced by treatment of organ-cultured tails with thyroid hormone (T(3)). Using the organ culture model, we provide the first direct evidence that MMPs are required for T(3)-induced tail resorption by showing that a synthetic inhibitor of MMP activity/expression can specifically retard the resorption process. By gelatin zymography, we also show T(3) induction of a fifth MMP, preliminarily identified as gelatinase B (GelB; MMP-9). Moreover, T(3) not only induces MMP/TIMP expression but also MMP activation, and we provide evidence that TIMP-2 participates in the latter process. These findings suggest that MMPs and TIMPs act in concert to effect the dismantling of mesenchymal structures during T(3)-induced metamorphic tadpole tail resorption.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
1058-8388
pubmed:author
pubmed:copyrightInfo
Copyright 2002 Wiley-Liss, Inc.
pubmed:issnType
Print
pubmed:volume
223
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
402-13
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:11891989-Amino Acid Sequence, pubmed-meshheading:11891989-Animals, pubmed-meshheading:11891989-Blotting, Northern, pubmed-meshheading:11891989-Cloning, Molecular, pubmed-meshheading:11891989-Culture Media, Conditioned, pubmed-meshheading:11891989-DNA, Complementary, pubmed-meshheading:11891989-Immunoblotting, pubmed-meshheading:11891989-In Situ Hybridization, pubmed-meshheading:11891989-Matrix Metalloproteinases, pubmed-meshheading:11891989-Matrix Metalloproteinases, Membrane-Associated, pubmed-meshheading:11891989-Mesoderm, pubmed-meshheading:11891989-Metalloendopeptidases, pubmed-meshheading:11891989-Molecular Sequence Data, pubmed-meshheading:11891989-Organ Culture Techniques, pubmed-meshheading:11891989-Precipitin Tests, pubmed-meshheading:11891989-Sequence Homology, Amino Acid, pubmed-meshheading:11891989-Thyroid Hormones, pubmed-meshheading:11891989-Time Factors, pubmed-meshheading:11891989-Tissue Inhibitor of Metalloproteinase-2, pubmed-meshheading:11891989-Xenopus, pubmed-meshheading:11891989-Xenopus laevis
pubmed:year
2002
pubmed:articleTitle
Matrix metalloproteinases mediate the dismantling of mesenchymal structures in the tadpole tail during thyroid hormone-induced tail resorption.
pubmed:affiliation
New England Eye Center, Tufts University School of Medicine, 750 Washington Street, Box 450, Boston, MA 02111, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't