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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
24
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pubmed:dateCreated |
2001-2-2
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pubmed:abstractText |
Papilin is an extracellular matrix glycoprotein that we have found to be involved in, (1) thin matrix layers during gastrulation, (2) matrix associated with wandering, phagocytic hemocytes, (3) basement membranes and (4) space-filling matrix during Drosophila development. Determination of its cDNA sequence led to the identification of Caenorhabditis and mammalian papilins. A distinctly conserved 'papilin cassette' of domains at the amino-end of papilins is also the carboxyl-end of the ADAMTS subgroup of secreted, matrix-associated metalloproteinases; this cassette contains one thrombospondin type 1 (TSR) domain, a specific cysteine-rich domain and several partial TSR domains. In vitro, papilin non-competitively inhibits procollagen N-proteinase, an ADAMTS metalloproteinase. Inhibiting papilin synthesis in Drosophila or Caenorhabditis causes defective cell arrangements and embryonic death. Ectopic expression of papilin in Drosophila causes lethal abnormalities in muscle, Malpighian tubule and trachea formation. We suggest that papilin influences cell rearrangements and may modulate metalloproteinases during organogenesis.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNA Primers,
http://linkedlifedata.com/resource/pubmed/chemical/Drosophila Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Insect Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Metalloendopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Ppn protein, Drosophila,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Antisense,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0950-1991
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pubmed:author |
pubmed-author:AckleyB DBD,
pubmed-author:ChenYY,
pubmed-author:FesslerJ HJH,
pubmed-author:FesslerL ILI,
pubmed-author:KawaguchiNN,
pubmed-author:KramerJ MJM,
pubmed-author:KramerovA AAA,
pubmed-author:KramerovaI AIA,
pubmed-author:Kusche-GullbergMM,
pubmed-author:NelsonR ERE,
pubmed-author:ProckopD JDJ,
pubmed-author:SieronA LAL
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pubmed:issnType |
Print
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pubmed:volume |
127
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
5475-85
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:11076767-Amino Acid Sequence,
pubmed-meshheading:11076767-Animals,
pubmed-meshheading:11076767-Base Sequence,
pubmed-meshheading:11076767-Caenorhabditis elegans,
pubmed-meshheading:11076767-DNA Primers,
pubmed-meshheading:11076767-Drosophila Proteins,
pubmed-meshheading:11076767-Drosophila melanogaster,
pubmed-meshheading:11076767-Gene Expression Regulation, Developmental,
pubmed-meshheading:11076767-Glycoproteins,
pubmed-meshheading:11076767-Humans,
pubmed-meshheading:11076767-In Situ Hybridization,
pubmed-meshheading:11076767-Insect Proteins,
pubmed-meshheading:11076767-Metalloendopeptidases,
pubmed-meshheading:11076767-Molecular Sequence Data,
pubmed-meshheading:11076767-Protein Structure, Tertiary,
pubmed-meshheading:11076767-RNA, Antisense,
pubmed-meshheading:11076767-RNA, Messenger
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pubmed:year |
2000
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pubmed:articleTitle |
Papilin in development; a pericellular protein with a homology to the ADAMTS metalloproteinases.
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pubmed:affiliation |
MCD Biology Department and Molecular Biology Institute, University of California at Los Angeles, CA 90095, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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