Identification of chicken and C. elegans fibulin-1 homologs and characterization of the C. elegans fibulin-1 gene

• Published in: Matrix biology 1998-12, Vol.17 (8), p.635-646
• Main Authors: Barth, Jeremy L., Argraves, Kelley M., Roark, Eileen F., Little, Charles D., Argraves, W.Scott
• Format: Article
• Language: English
• Subjects: alternative splicing; Amino Acid Sequence; Animals; Base Sequence; Caenorhabditis elegans - genetics; Calcium-Binding Proteins - genetics; Chickens - genetics; DNA, Complementary; epidermal growth factor-like repeats; extracellular matrix; Extracellular Matrix Proteins - genetics; gene structure; Genes, Helminth; Humans; Mice; Molecular Sequence Data; Sequence Analysis
• ISSN: 0945-053X; 1569-1802
• DOI: 10.1016/S0945-053X(98)90114-7

Fibulin-1, a member of the emerging family of fibulin proteins, is a component of elastic extracellular matrix fibers, basement membranes and blood. Homologs of fibulin-1 have been described in man, mouse and zebrafish. In this study, we describe the isolation and sequencing of chicken fibulin-1C and D cDNA variants. We also describe identification of a C. elegans cDNA encoding fibulin-1D and cosmids containing the C. elegans fibulin-1 gene. Using the cDNA, RT-PCR and computer-based analysis of genomic sequences, the exon/intron organization of the C. elegans fibulin-1 gene was determined. The C. elegans fibulin-1 gene is located on chromosome IV, is approximately 6 kb in length, contains 16 exons and encodes fibulin-1C and D variants. Comparative analysis of the deduced amino acid sequences of nematode and chicken fibulin-1 variants with other known vertebrate fibulin-1 polypeptides showed that the number and organization of structural modules are identical. The results of this study indicate that the structure of the fibulin-1 protein has remained highly conserved over a large period of evolution, suggestive of functional conservation.