| Human fibulin-1D: molecular cloning, expression and similarity with S1-5 protein, a new member of the fibulin gene family. | |
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MedLine Citation:
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PMID: 9106159 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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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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Authors:
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H Tran; M Mattei; S Godyna; W S Argraves |
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Publication Detail:
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Type: Comparative Study; Journal Article; Research Support, U.S. Gov't, P.H.S. |
Journal Detail:
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Title: Matrix biology : journal of the International Society for Matrix Biology Volume: 15 ISSN: 0945-053X ISO Abbreviation: Matrix Biol. Publication Date: 1997 Mar |
Date Detail:
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Created Date: 1997-07-01 Completed Date: 1997-07-01 Revised Date: 2007-11-14 |
Medline Journal Info:
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Nlm Unique ID: 9432592 Medline TA: Matrix Biol Country: GERMANY |
Other Details:
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Languages: eng Pagination: 479-93 Citation Subset: IM |
Affiliation:
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Biochemistry Department, American Red Cross, Rockville, Maryland, USA. |
| Data Bank Information | |
Bank Name/Acc. No.:
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GENBANK/U01244 |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Amino Acid Sequence Animals Base Sequence Calcium-Binding Proteins / biosynthesis*, genetics*, metabolism, physiology Cells, Cultured Cloning, Molecular* Extracellular Matrix / metabolism Extracellular Matrix Proteins / genetics*, physiology Female Fibrinogen / metabolism Fibronectins / metabolism Gene Expression / genetics*, physiology Genes / genetics*, physiology Humans Isomerism Molecular Sequence Data Placenta / metabolism RNA, Messenger / metabolism Rabbits Sequence Analysis, DNA Sequence Homology, Amino Acid Transcription, Genetic / genetics, physiology |
| Grant Support | |
ID/Acronym/Agency:
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GM42912/GM/NIGMS NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Calcium-Binding Proteins; 0/Extracellular Matrix Proteins; 0/Fibronectins; 0/RNA, Messenger; 0/fibulin; 9001-32-5/Fibrinogen |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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