Evolution of collagens

  title={Evolution of collagens},
  author={Jean-Yves Exposito and Caroline Cluzel and Robert Garrone and C. Lethias},
  journal={The Anatomical Record},
The extracellular matrix is often defined as the substance that gives multicellular organisms (from plants to vertebrates) their structural integrity, and is intimately involved in their development. Although the general functions of extracellular matrices are comparable, their compositions are quite distinct. One of the specific components of metazoan extracellular matrices is collagen, which is present in organisms ranging from sponges to humans. By comparing data obtained in diploblastic… 

The Fibrillar Collagen Family

The different steps in the evolution of this protein family are discussed, from the formation of an ancestral fibrillar collagen gene to theformation of different clades and the importance of this diversification in developmental processes.

Invertebrate and Vertebrate Collagens

Collagens form a family of extracellular matrix proteins that is often associated with metazoan multicellularity and evolution and provide protection against pathogens while bacterial collagens seem to be involved in pathogen virulence.

New insights into structure and function of type I collagen

Collagen is one of the most abundant proteins in mammalians and strongly conserved throughout evolution. It constitutes one third of the human proteome and comprises three-quarters of the dry weight

Evolution of collagen-based adhesion systems.

An Overview of Extracellular Matrix Structure and Function

It is argued that ECM components together with integrin receptors on the cell surface can be viewed as intricate nanodevices that allow cells to physically organize their 3D environment, as well as to sense and respond to various types of mechanical stress.

Widespread distribution of collagens and collagen-associated domains in eukaryotes

It is found that collagen domains are ubiquitous in choanoflagellates, the sister group of metazoans, and widespread across many other major eukaryotic taxa, suggesting that their ability to assemble into superstructures may have contributed to the origin of metazoan multicellularity.

Collagens and cartilage matrix homeostasis.

  • D. Eyre
  • Biology, Engineering
    Clinical orthopaedics and related research
  • 2004
Valuable insights and predictions on the function of the individual collagen types in cartilage continue to come from the study of skeletal dysplasia syndromes caused by mutations in genes for collagens and associated matrix proteins.

Basic Structure, Physiology, and Biochemistry of Connective Tissues and Extracellular Matrix Collagens.

This chapter discusses how the structures of the molecules, fibrils, and fibers contribute to connective tissue physiology in health, and in pathology with injury and repair, and how biochemistry plays a role in each of the processes involved in collagen synthesis and assembly.

Equine Collagen | Encyclopedia

The post-translational hydroxylation of the 11%–14% of proline residues by the enzyme proxyl-4-hydroxylase (PH4) (EC 1.11.2) is a process that gives to collagen a unique characteristic attributable only to type I collagen, important both for its recognition and quantification.

Invertebrate Data Predict an Early Emergence of Vertebrate Fibrillar Collagen Clades and an Anti-incest Model*

The modular structure of the fibrillar collagen chains present in different invertebrates from the protostome Anopheles gambiae to the chordate Ciona intestinalis indicates that all the key steps required for the formation of fibrils of variable structure and functionality arose step by step during invertebrate evolution.



The evolution of fibrillar collagens: a sea-pen collagen shares common features with vertebrate type V collagen.

Evolution of metazoan collagens.

  • R. Garrone
  • Biology
    Progress in molecular and subcellular biology
  • 1998
The development of electron microscopy and the improvement of biochemical analyses led to the clear localization of collagen in both vertebrates and invertebrates, but most studies focused on the easily recognizable collagen fibrils.

Collagen family of proteins

  • M. E. van der RestR. Garrone
  • Biology, Chemistry
    FASEB journal : official publication of the Federation of American Societies for Experimental Biology
  • 1991
Collagen molecules are structural macromolecules of the extracellular matrix that include in their structure one or several domains that have a characteristic triple helical conformation and play the role of connecting elements between these major structures and other tissue components.

Collagens and collagen-related diseases

The collagen superfamily of proteins plays a dominant role in maintaining the integrity of various tissues and also has a number of other important functions. The superfamily now includes more than

Type IV collagen in sponges, the missing link in basement membrane ubiquity *

Characterization of Hydra Type IV Collagen

Exposure of adult hydra to 15 mm glucose resulted in up-regulation of type IV collagen mRNA levels within 48 h and significant thickening of the mesoglea within 14 days, suggesting that basement membrane thickening seen in diabetes may be, in evolutionary terms, an ancient glucose-mediated response.

Hydra and Niccolo Paganini (1782–1840)—two peas in a pod? The molecular basis of extracellular matrix structure in the invertebrate, Hydra

  • M. SarrasR. Deutzmann
  • Biology
    BioEssays : news and reviews in molecular, cellular and developmental biology
  • 2001
This review will focus on structure–function relationships of the ECM of Hydra, and some aspects of the structural features of Hydra collagens mimic what is seen in Ehlers‐Danlos syndrome, an inherited condition in humans that results in an abnormally flexible ECM that can be debilitating in extreme cases.

Cloning of an annelid fibrillar-collagen gene and phylogenetic analysis of vertebrate and invertebrate collagens.

Phylogenetic studies indicate that the fibrillar collagen 1alpha chain of A. marina is homologous to the R. pachyptila interstitial collagen and that the FAm1alpha gene evolved independently from the other alpha-chain genes.

Cuticle collagen genes. Expression in Caenorhabditis elegans.

Stimulation of protein (collagen) synthesis in sponge cells by a cardiac myotrophin‐related molecule from Suberites domuncula

It is shown that a myotrophinlike polypeptide from the sponge Suberites domuncula causes the expression of collagen in cells from the same sponge in vitro, and it is concluded that the sponge myOTrophin causes in homologous cells the same/similar effect as the cardiac myotrophic effect in mammalian cells, where it is involved in initiation of cardial ventricular hypertrophy.