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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
7
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pubmed:dateCreated |
1997-7-1
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pubmed:databankReference | |
pubmed:abstractText |
Fibulin-1 is an extracellular matrix (ECM) component of basement membranes and connective tissue elastic fibers, and a blood protein. Multiple forms of fibulin-1 that differ in their C-terminal regions are produced through the process of alternative splicing of their precursor RNA. Two transcripts of 2.4 and 2.7 kb are the predominant fibulin-1 mRNAs expressed in human tissues and cultured cells. While the 2.4 kb transcript had been shown to encode fibulin-1C, the 2.7 kb transcript did not correspond to any of the previously identified human fibulin-1 variants. Herein, we report on the isolation and sequencing of cDNA corresponding to the 2.7 kb fibulin-1 transcript which encodes a novel, alternatively spliced form of human fibulin-1 that we term the D form. The deduced amino acid sequence of the D form is identical in its first 566 residues to the three known fibulin-1 variants (fibulin-1A-C); however, it has a unique 137 amino acid-C-terminal segment encoded by the alternatively spliced portion of its transcript. RNA hybridization analysis showed that the fibulin-1D transcript is coordinately expressed with that of fibulin-1C both in tissues and in cultured cells. Using antibodies specific to the unique C-terminal segment of fibulin-1D and -1C, both proteins were found to be expressed in human placenta. Recombinant fibulin-1D generated in transfected mammalian cells displayed similar ligand-binding properties as placenta-derived fibulin-1 and recombinant fibulin-1C, and it was capable of incorporating into cultured cell ECM in the absence of other fibulin-1 forms. A comparative sequence analysis revealed that the unique C-terminal region of fibulin-1D is similar to the C-terminal regions of fibulin-1C and fibulin-2. Furthermore, the C-terminal regions of fibulin-1C, -1D and -2 are similar to the C-terminal region of a recently described protein termed S1-5. In addition to this C-terminal similarity, S1-5 also contains repeated EGF-like modules and a conserved N-terminal element, thereby leading to the conclusion that S1-5 is a third member of the fibulin gene family.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Extracellular Matrix Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Fibrinogen,
http://linkedlifedata.com/resource/pubmed/chemical/Fibronectins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/fibulin
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0945-053X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
15
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
479-93
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:9106159-Amino Acid Sequence,
pubmed-meshheading:9106159-Animals,
pubmed-meshheading:9106159-Base Sequence,
pubmed-meshheading:9106159-Calcium-Binding Proteins,
pubmed-meshheading:9106159-Cells, Cultured,
pubmed-meshheading:9106159-Cloning, Molecular,
pubmed-meshheading:9106159-Extracellular Matrix,
pubmed-meshheading:9106159-Extracellular Matrix Proteins,
pubmed-meshheading:9106159-Female,
pubmed-meshheading:9106159-Fibrinogen,
pubmed-meshheading:9106159-Fibronectins,
pubmed-meshheading:9106159-Gene Expression,
pubmed-meshheading:9106159-Genes,
pubmed-meshheading:9106159-Humans,
pubmed-meshheading:9106159-Isomerism,
pubmed-meshheading:9106159-Molecular Sequence Data,
pubmed-meshheading:9106159-Placenta,
pubmed-meshheading:9106159-RNA, Messenger,
pubmed-meshheading:9106159-Rabbits,
pubmed-meshheading:9106159-Sequence Analysis, DNA,
pubmed-meshheading:9106159-Sequence Homology, Amino Acid,
pubmed-meshheading:9106159-Transcription, Genetic
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pubmed:year |
1997
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pubmed:articleTitle |
Human fibulin-1D: molecular cloning, expression and similarity with S1-5 protein, a new member of the fibulin gene family.
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pubmed:affiliation |
Biochemistry Department, American Red Cross, Rockville, Maryland, USA.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.
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