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

Endogenous substrates for epidermal transglutaminase.

H Hanigan, L A Goldsmith

    Biochimica Et Biophysica Acta
    |February 10, 1978
    PubMed
    Summary
    This summary is machine-generated.

    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 essential role of dermatology publications in enhancing professional diversity, equity, and inclusion.

    Clinics in dermatology·2022
    Same author

    The essential role of dermatology publications in enhancing professional diversity, equity and inclusion.

    The British journal of dermatology·2021
    Same author

    Dermatological education for the 21st century: prioritizing diversity.

    The British journal of dermatology·2020
    Same author

    Human epidermal transglutaminase.

    The Journal of investigative dermatology·2010
    Same author

    The polypeptide composition of epidermal prekeratin.

    Biochimica et biophysica acta·2009
    Same author

    What is the pathogenesis of acne?

    Experimental dermatology·2005
    Same journal

    Cumulative Contents.

    Biochimica et biophysica acta·2020
    Same journal

    Molecular Basis of Disease Cumulative Contents.

    Biochimica et biophysica acta·2020
    Same journal

    General Subjects Cumulative Contents.

    Biochimica et biophysica acta·2020
    Same journal

    Erratum to 'on the role of exchangeable hydrogen bonds for the kinetics of P680<sup>+·</sup> Q<sub>A</sub> <sup>-·</sup> formation and P680<sup>+·</sup> Pheo<sup>-·</sup> recombination in photosystem II' [Biochim. Biophys. Acta 1276 (1996) 35-44].

    Biochimica et biophysica acta·2019
    Same journal

    Oligomeric state of the light-harvesting complexes B800-850 and B875 from purple bacterium Rubrivivax gelatinosus in detergent solution.

    Biochimica et biophysica acta·2019
    Same journal

    Regulation of pigment content and enzyme activity in the cyanobacterium Nostoc sp. Mac grown in continuous light, a light-dark photoperiod, or darkness.

    Biochimica et biophysica acta·2019
    See all related articles

    Researchers identified high molecular weight epidermal proteins that act as substrates for epidermal transglutaminase. These proteins, rich in specific amino acids, become cross-linked and insoluble, a process inhibited by putrescine.

    Area of Science:

    • Biochemistry
    • Dermatology
    • Proteomics

    Background:

    • Epidermal transglutaminase (eTG) plays a crucial role in skin barrier formation and protein cross-linking.
    • Identifying specific substrates for eTG is essential for understanding epidermal structure and function.

    Purpose of the Study:

    • To isolate and characterize potential in vivo substrates for epidermal transglutaminase in human and rat epidermis.
    • To investigate the role of these substrates in protein cross-linking and insolubilization.

    Main Methods:

    • In vitro incorporation of radiolabeled putrescine and dansylcadaverine into epidermal proteins.
    • Analysis of protein incorporation using SDS-PAGE.
    • Amino acid composition analysis of labeled proteins.
    • In vivo labeling with [14C]glycine, [14C]histidine, and [4C]proline in newborn rats.

    Related Experiment Videos

    Main Results:

    • Two high molecular weight proteins were identified as major substrates for epidermal transglutaminase in both human and rat epidermis.
    • These proteins incorporated labels and became progressively insoluble upon transglutaminase incubation.
    • The amino acid composition of these proteins showed similarities to alpha-keratin.
    • Putrescine incorporation and subsequent cross-linking were time-dependent and inhibited by known eTG inhibitors.

    Conclusions:

    • Specific high molecular weight proteins in the epidermis serve as substrates for epidermal transglutaminase.
    • eTG-mediated cross-linking contributes to epidermal protein insolubilization and structural integrity.
    • The identified substrates share characteristics with alpha-keratins, suggesting a role in epidermal structure formation.