Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Collagen fibril structure in lamprey

B Brodsky1, K C BelBruno, T A Hardt

  • 1Department of Biochemistry, UMDNJ-Robert Wood Johnson Medical School, Piscataway 08854.

Journal of Molecular Biology
|October 14, 1994
PubMed
Summary

Collagen fibril structures in lampreys reveal ancient molecular packing conserved since early vertebrate evolution. Higher-level organization, however, diversified alongside vertebrates, except in notochord tissues.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Novel peptides as potential treatment of systemic lupus erythematosus.

Lupus·2011
Same author

Synchrotron radiation hardness studies of PILATUS II.

Journal of synchrotron radiation·2009
Same author

Does the genetic type of collagen determine fibril structure?

Biophysical journal·2009
Same author

Determinants of collagen fibril structure.

Biophysical journal·2009
Same author

Performance of single-photon-counting PILATUS detector modules.

Journal of synchrotron radiation·2009
Same author

A spatially resolving x-ray crystal spectrometer for measurement of ion-temperature and rotation-velocity profiles on the Alcator C-Mod tokamak.

The Review of scientific instruments·2008

Area of Science:

  • Biochemistry
  • Evolutionary Biology
  • Structural Biology

Background:

  • Collagen fibrils are essential structural components in vertebrates.
  • Lampreys possess five distinct genetic types of fibrillar collagen.
  • Understanding collagen structure in primitive vertebrates like lampreys offers insights into evolutionary conservation.

Purpose of the Study:

  • To compare the molecular and higher-order structure of collagen fibrils in three lamprey tissues (dermis, perinotochord, notochord sheath).
  • To investigate the evolutionary conservation of collagen fibril packing motifs.
  • To explore differences in fibril diameter and spatial orientation between lamprey and mammalian tissues.

Main Methods:

  • X-ray diffraction analysis of collagen fibril structure.

Related Experiment Videos

  • Electron microscopy for higher-order structural comparison.
  • Comparative analysis of lamprey collagen with higher vertebrate collagen.

    • Main Results:

    • Lamprey collagen fibrils exhibit the three major axial and lateral packing motifs found in higher vertebrates.
    • A decreased D period in lamprey dermis, attributed to molecular tilt, mirrors findings in higher vertebrate skins.
    • Fibril diameters and spatial orientation in most lamprey tissues differ from mammalian tissues, with notable similarity in lamprey notochord to type II collagen tissues.

    Conclusions:

    • The fundamental molecular packing of collagen fibrils was established early in vertebrate evolution and has remained conserved.
    • Higher-level organization of collagen fibrils evolved with vertebrate diversification, with exceptions like the lamprey notochord.
    • These findings highlight conserved molecular mechanisms and evolving structural adaptations in vertebrate collagen.