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

Aging, and crosslinking in mammlian collagen

D J Cannon, P F Davison

    Experimental Aging Research
    |March 1, 1977
    PubMed
    Summary

    Collagen

    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

    The moral foundations of a national medical service.

    Journal. Medical Association of Eire·2010
    Same author

    A British Medical Association Lecture on RECENT ADVANCES IN THE PHYSIOLOGY OF MENSTRUATION.

    British medical journal·2010
    Same author

    The wealth of a nation and the health of its workers and families.

    Journal. Medical Association of Eire·2010
    Same author

    Stress incontinence in women.

    Journal. Medical Association of Eire·2010
    Same author

    Traumatic rupture of the spleen.

    Irish journal of medical science·2010
    Same author

    Toxicology: past, present, and future.

    Annals of clinical and laboratory science·1999

    Area of Science:

    • Biochemistry
    • Biomaterials Science
    • Aging Research

    Background:

    • Collagen crosslinking is crucial for tissue integrity.
    • Borohydride-reducible crosslinks are key indicators of collagen maturation.
    • Changes in crosslinking patterns occur with aging.

    Purpose of the Study:

    • To investigate the changes in collagen crosslinks over animal age.
    • To determine tissue and species-specific variations in collagen crosslinking.
    • To correlate crosslink levels with growth cessation and tissue turnover.

    Main Methods:

    • Analysis of borohydride-reducible crosslinks in collagen.
    • Examination across different animal species (bovine, canine, human) and tissues.
    • Quantification of crosslink levels and ratios as a function of age.

    Main Results:

    • Reducible crosslink levels decrease with increasing animal age.
    • Significant tissue and species-specific differences in crosslink changes were observed.
    • Decreased reducible crosslinks correlate with the cessation of growth.

    Conclusions:

    • Reducible collagen crosslinks are converted into a stable, nonreducible form over time.
    • Low levels of reducible crosslinks may indicate reduced tissue turnover.
    • Observed ratio changes in reducible crosslinks likely stem from post-translational modifications.

    Related Experiment Videos