Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
1997-7-1
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.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0945-053X
pubmed:author
pubmed:issnType
Print
pubmed:volume
15
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
479-93
pubmed:dateRevised
2007-11-14
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
pubmed:year
1997
pubmed:articleTitle
Human fibulin-1D: molecular cloning, expression and similarity with S1-5 protein, a new member of the fibulin gene family.
pubmed:affiliation
Biochemistry Department, American Red Cross, Rockville, Maryland, USA.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S.