Fibrillar Collagen

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Jean-yves Exposito - One of the best experts on this subject based on the ideXlab platform.

  • The Fibrillar Collagen family.
    International Journal of Molecular Sciences, 2010
    Co-Authors: Jean-yves Exposito, Caroline Cluzel, Ulrich Valcourt, Claire Lethias
    Abstract:

    Collagens, or more precisely Collagen-based extracellular matrices, are often considered as a metazoan hallmark. Among the Collagens, Fibrillar Collagens are present from sponges to humans, and are involved in the formation of the well-known striated fibrils. In this review we discuss the different steps in the evolution of this protein family, from the formation of an ancestral Fibrillar Collagen gene to the formation of different clades. Genomic data from the choanoflagellate (sister group of Metazoa) Monosiga brevicollis, and from diploblast animals, have suggested that the formation of an ancestral α chain occurred before the metazoan radiation. Phylogenetic studies have suggested an early emergence of the three clades that were first described in mammals. Hence the duplication events leading to the formation of the A, B and C clades occurred before the eumetazoan radiation. Another important event has been the two rounds of “whole genome duplication” leading to the amplification of Fibrillar Collagen gene numbers, and the importance of this diversification in developmental processes. We will also discuss some other aspects of Fibrillar Collagen evolution such as the development of the molecular mechanisms involved in the formation of proCollagen molecules and of striated fibrils.

  • 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
    Journal of Biological Chemistry, 2008
    Co-Authors: Jean-yves Exposito, Caroline Cluzel, Ulrich Valcourt, Claire Larroux, Claire Lethias, Bernhard M Degnan
    Abstract:

    Collagens are often considered a metazoan hallmark, with the fibril-forming Fibrillar Collagens present from sponges to human. From evolutionary studies, three Fibrillar Collagen clades (named A, B, and C) have been defined and shown to be present in mammals, whereas the emergence of the A and B clades predates the protostome/deuterostome split. Moreover, several C clade Fibrillar Collagen chains are present in some invertebrate deuterostome genomes but not in protostomes whose genomes have been sequenced. The newly sequenced genomes of the choanoflagellate Monosiga brevicollis, the demosponge Amphimedon queenslandica, and the cnidarians Hydra magnipapillata (Hydra) and Nematostella vectensis (sea anemone) allow us to have a better understanding of the origin and evolution of Fibrillar Collagens. Analysis of these genomes suggests that an ancestral Fibrillar Collagen gene arose at the dawn of the Metazoa, before the divergence of sponge and eumetazoan lineages. The duplication events leading to the formation of the three Fibrillar Collagen clades (A, B, and C) occurred before the eumetazoan radiation. Interestingly, only the B clade Fibrillar Collagens preserved their characteristic modular structure from sponge to human. This observation is compatible with the suggested primordial function of type V/XI Fibrillar Collagens in the initiation of the formation of the Collagen fibrils.

  • Invertebrate data predict an early emergence of vertebrate Fibrillar Collagen clades and an anti-incest model.
    Journal of Biological Chemistry, 2004
    Co-Authors: Abdel Aouacheria, Caroline Cluzel, Claire Lethias, Robert Garrone, Manolo Gouy, Jean-yves Exposito
    Abstract:

    Fibrillar Collagens are involved in the formation of striated fibrils and are present from the first multicel-lular animals, sponges, to humans. Recently, a new evolutionary model for Fibrillar Collagens has been suggested (Boot-Handford, R. P., Tuckwell, D. S., Plumb, D. A., Farrington Rock, C., and Poulsom, R. (2003) J. Biol. Chem. 278, 31067–31077). In this model, a rare genomic event leads to the formation of the founder vertebrate Fibrillar Collagen gene prior to the early vertebrate ge-nome duplications and the radiation of the vertebrate Fibrillar Collagen clades (A, B, and C). Here, we present the modular structure of the Fibrillar Collagen chains present in different invertebrates from the protostome Anopheles gambiae to the chordate Ciona intestinalis. From their modular structure and the use of a triple helix instead of C-propeptide sequences in phylogenetic analyses, we were able to show that the divergence of A and B clades arose early during evolution because chains related to these clades are present in protos-tomes. Moreover, the event leading to the divergence of B and C clades from a founder gene arose before the appearance of vertebrates; altogether these data contradict the Boot-Handford model. Moreover, they indicate that all the key steps required for the formation of fibrils of variable structure and functionality arose step by step during invertebrate evolution.

  • Sea urchin Fibrillar Collagen 2α chain participates in heterotrimeric molecules of (1α)22α stoichiometry
    Matrix Biology, 2000
    Co-Authors: Caroline Cluzel, Claire Lethias, Robert Garrone, Jean-yves Exposito
    Abstract:

    Abstract In sea urchin, two Fibrillar Collagen chains (α1 and α2) have been characterized by molecular biology while two biochemically detected chains (α1 and α2) have been reported. Here, to determine the relationship between these results, Western-blotting and Edman degradation sequencing of the amino-termini of pepsinized sea urchin Fibrillar Collagen chains were performed. The data demonstrate that the 2α chain corresponds to the α2 chain and is involved in the formation of heterotrimeric molecules [(1α) 2 2α].

  • Cloning of an annelid Fibrillar-Collagen gene and phylogenetic analysis of vertebrate and invertebrate Collagens
    European Journal of Biochemistry, 1997
    Co-Authors: Fx Sicot, Jean-yves Exposito, Robert Garrone, M. Masselot, Jean S. Deutsch, Françoise Gaill
    Abstract:

    Arenicola marina possesses cuticular and interstitial Collagens, which are mostly synthesised by its epidermis. A cDNA library was constructed from the body wall. This annelid cDNA library was screened with a sea-urchin-Collagen cDNA probe, and several overlapping clones were isolated. Nucleotide sequencing of these clones revealed an open reading frame of 2052 nucleotides. The translation product exhibits a triple helical domain of 138 Gly-Xaa-Yaa repeats followed by a 269-residue-long C-terminal non-Collagenous domain (C-propeptide). The triple helical domain exhibits an imperfection that has been previously described in a peptide produced by cyanogen bromide digestion (CNBr peptide) of A. marina interstitial Collagen. This imperfection occurs at the same place in the interstitial Collagen of the vestimen-tiferan Riftia pachyptila. This identifies the clone as coding for the C-terminal part of a Fibrillar Collagen chain. It was called Fam1α, for Fibrillar Collagen 1α chain of A. marina. The non-Collagenous domain possesses a structure similar to carboxy-terminal propeptides of Fibrillar pro-α chains. Only six conserved cysteine residues are observed in A. marina compared with seven or eight in all other known C-propeptides. This provides information on the importance of disulfide bonds in C-propeptide interactions and in the Collagen-assembly process. Phylogenetic studies indicate that the Fibrillar Collagen 1α chain of A. marina is homologous to the R. pachyptila interstitial Collagen and that the Fam1α gene evolved independently from the other a-chain genes. Complementary analyses indicate that the vertebrate Fibrillar Collagen family is composed of two monophyletic subgroups with a specific position of the Collagen type-V chains.

Michael R. Zile - One of the best experts on this subject based on the ideXlab platform.

Caroline Cluzel - One of the best experts on this subject based on the ideXlab platform.

  • The Fibrillar Collagen family.
    International Journal of Molecular Sciences, 2010
    Co-Authors: Jean-yves Exposito, Caroline Cluzel, Ulrich Valcourt, Claire Lethias
    Abstract:

    Collagens, or more precisely Collagen-based extracellular matrices, are often considered as a metazoan hallmark. Among the Collagens, Fibrillar Collagens are present from sponges to humans, and are involved in the formation of the well-known striated fibrils. In this review we discuss the different steps in the evolution of this protein family, from the formation of an ancestral Fibrillar Collagen gene to the formation of different clades. Genomic data from the choanoflagellate (sister group of Metazoa) Monosiga brevicollis, and from diploblast animals, have suggested that the formation of an ancestral α chain occurred before the metazoan radiation. Phylogenetic studies have suggested an early emergence of the three clades that were first described in mammals. Hence the duplication events leading to the formation of the A, B and C clades occurred before the eumetazoan radiation. Another important event has been the two rounds of “whole genome duplication” leading to the amplification of Fibrillar Collagen gene numbers, and the importance of this diversification in developmental processes. We will also discuss some other aspects of Fibrillar Collagen evolution such as the development of the molecular mechanisms involved in the formation of proCollagen molecules and of striated fibrils.

  • 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
    Journal of Biological Chemistry, 2008
    Co-Authors: Jean-yves Exposito, Caroline Cluzel, Ulrich Valcourt, Claire Larroux, Claire Lethias, Bernhard M Degnan
    Abstract:

    Collagens are often considered a metazoan hallmark, with the fibril-forming Fibrillar Collagens present from sponges to human. From evolutionary studies, three Fibrillar Collagen clades (named A, B, and C) have been defined and shown to be present in mammals, whereas the emergence of the A and B clades predates the protostome/deuterostome split. Moreover, several C clade Fibrillar Collagen chains are present in some invertebrate deuterostome genomes but not in protostomes whose genomes have been sequenced. The newly sequenced genomes of the choanoflagellate Monosiga brevicollis, the demosponge Amphimedon queenslandica, and the cnidarians Hydra magnipapillata (Hydra) and Nematostella vectensis (sea anemone) allow us to have a better understanding of the origin and evolution of Fibrillar Collagens. Analysis of these genomes suggests that an ancestral Fibrillar Collagen gene arose at the dawn of the Metazoa, before the divergence of sponge and eumetazoan lineages. The duplication events leading to the formation of the three Fibrillar Collagen clades (A, B, and C) occurred before the eumetazoan radiation. Interestingly, only the B clade Fibrillar Collagens preserved their characteristic modular structure from sponge to human. This observation is compatible with the suggested primordial function of type V/XI Fibrillar Collagens in the initiation of the formation of the Collagen fibrils.

  • Invertebrate data predict an early emergence of vertebrate Fibrillar Collagen clades and an anti-incest model.
    Journal of Biological Chemistry, 2004
    Co-Authors: Abdel Aouacheria, Caroline Cluzel, Claire Lethias, Robert Garrone, Manolo Gouy, Jean-yves Exposito
    Abstract:

    Fibrillar Collagens are involved in the formation of striated fibrils and are present from the first multicel-lular animals, sponges, to humans. Recently, a new evolutionary model for Fibrillar Collagens has been suggested (Boot-Handford, R. P., Tuckwell, D. S., Plumb, D. A., Farrington Rock, C., and Poulsom, R. (2003) J. Biol. Chem. 278, 31067–31077). In this model, a rare genomic event leads to the formation of the founder vertebrate Fibrillar Collagen gene prior to the early vertebrate ge-nome duplications and the radiation of the vertebrate Fibrillar Collagen clades (A, B, and C). Here, we present the modular structure of the Fibrillar Collagen chains present in different invertebrates from the protostome Anopheles gambiae to the chordate Ciona intestinalis. From their modular structure and the use of a triple helix instead of C-propeptide sequences in phylogenetic analyses, we were able to show that the divergence of A and B clades arose early during evolution because chains related to these clades are present in protos-tomes. Moreover, the event leading to the divergence of B and C clades from a founder gene arose before the appearance of vertebrates; altogether these data contradict the Boot-Handford model. Moreover, they indicate that all the key steps required for the formation of fibrils of variable structure and functionality arose step by step during invertebrate evolution.

  • Sea urchin Fibrillar Collagen 2α chain participates in heterotrimeric molecules of (1α)22α stoichiometry
    Matrix Biology, 2000
    Co-Authors: Caroline Cluzel, Claire Lethias, Robert Garrone, Jean-yves Exposito
    Abstract:

    Abstract In sea urchin, two Fibrillar Collagen chains (α1 and α2) have been characterized by molecular biology while two biochemically detected chains (α1 and α2) have been reported. Here, to determine the relationship between these results, Western-blotting and Edman degradation sequencing of the amino-termini of pepsinized sea urchin Fibrillar Collagen chains were performed. The data demonstrate that the 2α chain corresponds to the α2 chain and is involved in the formation of heterotrimeric molecules [(1α) 2 2α].

Yves A Declerck - One of the best experts on this subject based on the ideXlab platform.

Claire Lethias - One of the best experts on this subject based on the ideXlab platform.

  • The Fibrillar Collagen family.
    International Journal of Molecular Sciences, 2010
    Co-Authors: Jean-yves Exposito, Caroline Cluzel, Ulrich Valcourt, Claire Lethias
    Abstract:

    Collagens, or more precisely Collagen-based extracellular matrices, are often considered as a metazoan hallmark. Among the Collagens, Fibrillar Collagens are present from sponges to humans, and are involved in the formation of the well-known striated fibrils. In this review we discuss the different steps in the evolution of this protein family, from the formation of an ancestral Fibrillar Collagen gene to the formation of different clades. Genomic data from the choanoflagellate (sister group of Metazoa) Monosiga brevicollis, and from diploblast animals, have suggested that the formation of an ancestral α chain occurred before the metazoan radiation. Phylogenetic studies have suggested an early emergence of the three clades that were first described in mammals. Hence the duplication events leading to the formation of the A, B and C clades occurred before the eumetazoan radiation. Another important event has been the two rounds of “whole genome duplication” leading to the amplification of Fibrillar Collagen gene numbers, and the importance of this diversification in developmental processes. We will also discuss some other aspects of Fibrillar Collagen evolution such as the development of the molecular mechanisms involved in the formation of proCollagen molecules and of striated fibrils.

  • 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
    Journal of Biological Chemistry, 2008
    Co-Authors: Jean-yves Exposito, Caroline Cluzel, Ulrich Valcourt, Claire Larroux, Claire Lethias, Bernhard M Degnan
    Abstract:

    Collagens are often considered a metazoan hallmark, with the fibril-forming Fibrillar Collagens present from sponges to human. From evolutionary studies, three Fibrillar Collagen clades (named A, B, and C) have been defined and shown to be present in mammals, whereas the emergence of the A and B clades predates the protostome/deuterostome split. Moreover, several C clade Fibrillar Collagen chains are present in some invertebrate deuterostome genomes but not in protostomes whose genomes have been sequenced. The newly sequenced genomes of the choanoflagellate Monosiga brevicollis, the demosponge Amphimedon queenslandica, and the cnidarians Hydra magnipapillata (Hydra) and Nematostella vectensis (sea anemone) allow us to have a better understanding of the origin and evolution of Fibrillar Collagens. Analysis of these genomes suggests that an ancestral Fibrillar Collagen gene arose at the dawn of the Metazoa, before the divergence of sponge and eumetazoan lineages. The duplication events leading to the formation of the three Fibrillar Collagen clades (A, B, and C) occurred before the eumetazoan radiation. Interestingly, only the B clade Fibrillar Collagens preserved their characteristic modular structure from sponge to human. This observation is compatible with the suggested primordial function of type V/XI Fibrillar Collagens in the initiation of the formation of the Collagen fibrils.

  • Invertebrate data predict an early emergence of vertebrate Fibrillar Collagen clades and an anti-incest model.
    Journal of Biological Chemistry, 2004
    Co-Authors: Abdel Aouacheria, Caroline Cluzel, Claire Lethias, Robert Garrone, Manolo Gouy, Jean-yves Exposito
    Abstract:

    Fibrillar Collagens are involved in the formation of striated fibrils and are present from the first multicel-lular animals, sponges, to humans. Recently, a new evolutionary model for Fibrillar Collagens has been suggested (Boot-Handford, R. P., Tuckwell, D. S., Plumb, D. A., Farrington Rock, C., and Poulsom, R. (2003) J. Biol. Chem. 278, 31067–31077). In this model, a rare genomic event leads to the formation of the founder vertebrate Fibrillar Collagen gene prior to the early vertebrate ge-nome duplications and the radiation of the vertebrate Fibrillar Collagen clades (A, B, and C). Here, we present the modular structure of the Fibrillar Collagen chains present in different invertebrates from the protostome Anopheles gambiae to the chordate Ciona intestinalis. From their modular structure and the use of a triple helix instead of C-propeptide sequences in phylogenetic analyses, we were able to show that the divergence of A and B clades arose early during evolution because chains related to these clades are present in protos-tomes. Moreover, the event leading to the divergence of B and C clades from a founder gene arose before the appearance of vertebrates; altogether these data contradict the Boot-Handford model. Moreover, they indicate that all the key steps required for the formation of fibrils of variable structure and functionality arose step by step during invertebrate evolution.

  • Sea urchin Fibrillar Collagen 2α chain participates in heterotrimeric molecules of (1α)22α stoichiometry
    Matrix Biology, 2000
    Co-Authors: Caroline Cluzel, Claire Lethias, Robert Garrone, Jean-yves Exposito
    Abstract:

    Abstract In sea urchin, two Fibrillar Collagen chains (α1 and α2) have been characterized by molecular biology while two biochemically detected chains (α1 and α2) have been reported. Here, to determine the relationship between these results, Western-blotting and Edman degradation sequencing of the amino-termini of pepsinized sea urchin Fibrillar Collagen chains were performed. The data demonstrate that the 2α chain corresponds to the α2 chain and is involved in the formation of heterotrimeric molecules [(1α) 2 2α].