ArticleProceedings of the National Academy of Sciences of the United States of America1990
Characterization of a fibrillar collagen gene in sponges reveals the early evolutionary appearance of two collagen gene families.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1990. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 142 citations in OpenAlex.
- The Fibrillar Collagens of Bony Fish: Genes, Proteins, and Biomedical Applications.Sub-cellular biochemistry · 2026Review
- Collagen from Marine Sources for Potential Application in Wound Treatment.Progress in molecular and subcellular biology · 2026Review
- Collagen Mechanics.Sub-cellular biochemistry · 2026Review
- First draft genome assembly of sponge Halisarca dujardinii reveals key components of basement membrane and broad repertoire of aggregation factors.Scientific reports · 2025Article
- Article
- Rheology of marine sponges reveals anisotropic mechanics and tuned dynamics.Journal of the Royal Society, Interface · 2022Article
- Production, Characterization and Biocompatibility Evaluation of Collagen Membranes Derived from Marine Sponge Chondrosia reniformis Nardo, 1847.Marine drugs · 2018Article
- Molecular Cloning, Characterization, and Expression Analysis of a Prolyl 4-Hydroxylase from the Marine Sponge Chondrosia reniformis.Marine biotechnology (New York, N.Y.) · 2015Article
- Structural constraints on the evolution of the collagen fibril: convergence on a 1014-residue COL domain.Open biology · 2015Article
- Adsorption of C.I. Natural Red 4 onto Spongin Skeleton of Marine Demosponge.Materials (Basel, Switzerland) · 2014Article
- A dynamic history of gene duplications and losses characterizes the evolution of the SPARC family in eumetazoans.Proceedings. Biological sciences · 2013Article
- Molecular characterization of a nonfibrillar collagen from the marine sponge Chondrosia reniformis Nardo 1847 and positive effects of soluble silicates on its expression.Marine biotechnology (New York, N.Y.) · 2012Article
- The fibrillar collagen family.International journal of molecular sciences · 2010Review
- Conservation of notochord gene expression across chordates: insights from the Leprecan gene family.Genesis (New York, N.Y. : 2000) · 2008Article
- Demosponge and sea anemone fibrillar collagen diversity reveals the early emergence of A/C clades and the maintenance of the modular structure of type V/XI collagens from sponge to human.The Journal of biological chemistry · 2008Article
- A receptor tyrosine kinase from choanoflagellates: molecular insights into early animal evolution.Proceedings of the National Academy of Sciences of the United States of America · 2001Article
- Molecular phylogeny of Metazoa (animals): monophyletic origin.Die Naturwissenschaften · 1995Review
- Cartilage collagens: strategies for the study of their organisation and expression in the extracellular matrix.Annals of the rheumatic diseases · 1994Review
- The complete intron/exon structure of Ephydatia mülleri fibrillar collagen gene suggests a mechanism for the evolution of an ancestral gene module.Journal of molecular evolution · 1993Article
- Characterization of an intronless collagen gene family in the marine sponge Microciona prolifera.Proceedings of the National Academy of Sciences of the United States of America · 1993Article
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2 authors at 1 institution in 1 country.
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Abstract
We have characterized cDNA and genomic clones coding for a sponge collagen. The partial cDNA has an open reading frame encoding 547 amino acid residues. The conceptual translation product contains a probably incomplete triple-helical domain (307 amino acids) with one Gly-Xaa-Yaa-Zaa imperfection in the otherwise perfect Gly-Xaa-Yaa repeats and a carboxyl propeptide (240 amino acids) that includes 7 cysteine residues. Amino acid sequence comparisons indicate that this sponge collagen is homologous to vertebrate and sea urchin fibrillar collagens. Partial characterization of the corresponding gene reveals an intron-exon organization clearly related to the fibrillar collagen gene family. The exons coding for the triple-helical domain are 54 base pairs (bp) or multiples thereof, except for a 57-bp exon containing the Gly-Xaa-Yaa-Zaa coding sequence and for two unusual exons of 126 and 18 bp, respectively. This latter 18-bp exon marks the end of the triple-helical domain, contrary to the other known fibrillar collagen genes that contain exons coding for the junction between the triple-helical domain and the carboxyl propeptide. Compared to other fibrillar collagen genes, the introns are remarkably small. Hybridization to blotted RNAs established that the gene transcript is 4.9 kilobases. Together with previous results that showed the existence of a nonfibrillar collagen in the same species, these data demonstrate that at least two collagen gene families are represented in the most primitive metazoa.
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