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Related Experiment Videos

Native collagen fibrils from echinoderms are molecularly bipolar

F A Thurmond1, J A Trotter

  • 1Department of Anatomy, University of New Mexico School of Medicine, Albuquerque 87131.

Journal of Molecular Biology
|January 7, 1994
PubMed
Summary

Collagen fibrils are not uniform cylinders and molecules do not share the same polarity. Echinoderm collagen fibrils are spindle-shaped and molecularly bipolar, challenging long-held assumptions in fibrillogenesis research.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Collagen fibrils are typically modeled as uniform cylinders with unidirectional molecular polarity.
  • These assumptions have remained largely untested due to the difficulty in isolating intact native fibrils.

Purpose of the Study:

  • To investigate the molecular structure and arrangement within intact native collagen fibrils.
  • To challenge and test the prevailing assumptions about collagen fibril uniformity and molecular polarity.

Main Methods:

  • Electron microscopy was employed to analyze the molecular structure of intact collagen fibrils.
  • Fibrils were extracted from echinoderms, a source known for yielding intact native structures.

Main Results:

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  • Echinoderm collagen fibrils are symmetrically spindle-shaped, not uniform cylinders.
  • These fibrils exhibit molecular bipolarity, with N-termini oriented towards fibril ends.
  • Constituent collagen molecules are arranged antiparallelly at the fibril center.

Conclusions:

  • The study refutes the long-standing assumptions of uniform diameter and unidirectional molecular polarity in collagen fibrils.
  • The bipolar molecular arrangement and spindle shape of echinoderm collagen fibrils offer new insights into fibrillogenesis.
  • Findings necessitate a re-evaluation of collagen fibril structure models and their formation processes.