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Structure-function relationship in the evolution of elastin

H Sage

    The Journal of Investigative Dermatology
    |July 1, 1982
    PubMed
    Summary
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    Elastin, a key protein in connective tissues, evolved with increasing hydrophobicity and crosslinking in higher vertebrates. This adaptation supports efficient circulatory systems in mammals and birds.

    Area of Science:

    • Biochemistry
    • Evolutionary Biology
    • Biophysics

    Background:

    • Elastin is a crucial rubber-like protein in connective tissues, providing elasticity under physiological stress.
    • Its structure, distribution, and properties are vital for tissue function, particularly in the cardiovascular system.

    Purpose of the Study:

    • To investigate the evolutionary trajectory of elastin structure across diverse species.
    • To correlate elastin's biochemical and morphological changes with vertebrate evolution and circulatory system development.

    Main Methods:

    • Phylogenetic analysis of elastin distribution in vertebrate and invertebrate tissues.
    • Histological examination of fiber morphology and arrangement.
    • Biochemical assays for amino acid composition, crosslinking (desmosine/isodesmosine), and hydrophobicity.

    Related Experiment Videos

  • Microcalorimetry to assess elastin's mechanical response to deformation.

    • Main Results:

    • Elastin was found in all vertebrates except jawless fish, and absent in examined invertebrates.
    • Significant differences in aortic elastin fiber morphology were observed across vertebrate families.
    • Higher vertebrates (mammals, birds) exhibited increased elastin crosslinking and hydrophobicity compared to bony fish.
    • Mammalian elastin showed enhanced coacervation at 37°C and distinct mechanical behavior under tensile stress.

    Conclusions:

    • Elastin's evolution, marked by increased hydrophobicity, parallels the development of high-pressure circulatory systems in homeotherms.
    • The data suggest distinct elastin types may have evolved from a common ancestral gene, rather than a shared origin with other connective tissue proteins.