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

Enkephalin-degrading activity in arthropode hemolymphe.

M A Coletti-Previero, H Mattras, R Zwilling

    Neuropeptides
    |September 1, 1985
    PubMed
    Summary

    Opioid peptides like enkephalin are quickly broken down in the hemolymph of invertebrates such as Astacus fluviatilis and Limulus polyphemus. This rapid inactivation by multiple enzymes suggests a metabolic barrier limiting peptide activity in invertebrates.

    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

    Activation of pro-astacin. Immunological and model peptide studies on the processing of immature astacin, a zinc-endopeptidase from the crayfish Astacus astacus.

    European journal of biochemistry·2001
    Same author

    Steroidal affinity labels of the estrogen receptor alpha. 4. Electrophilic 11beta-aryl derivatives of estradiol.

    Journal of medicinal chemistry·2000
    Same author

    cDNA cloning, bacterial expression, in vitro renaturation and affinity purification of the zinc endopeptidase astacin.

    The Biochemical journal·1999
    Same author

    Cysteine 530 of the human estrogen receptor alpha is the main covalent attachment site of 11beta-(aziridinylalkoxyphenyl)estradiols.

    Biochemistry·1999
    Same author

    Aspartyl proteases in Caenorhabditis elegans. Isolation, identification and characterization by a combined use of affinity chromatography, two-dimensional gel electrophoresis, microsequencing and databank analysis.

    European journal of biochemistry·1999
    Same author

    Proteoglycan distribution pattern during aging in the nematode Caenorhabditis elegans: an ultrastructural histochemical study.

    The Histochemical journal·1999

    Area of Science:

    • Biochemistry
    • Comparative Physiology
    • Enzymology

    Background:

    • Opioid peptides, such as enkephalins, play crucial roles in vertebrate systems.
    • Understanding the fate of these peptides in invertebrates provides insights into evolutionary adaptations.
    • Hemolymph serves as a circulatory fluid in invertebrates, analogous to blood in vertebrates.

    Purpose of the Study:

    • To investigate the stability and inactivation mechanisms of opioid peptides in invertebrate hemolymph.
    • To identify and characterize the enzymes responsible for opioid peptide degradation in Astacus fluviatilis and Limulus polyphemus.
    • To compare the enzymatic inactivation of opioid peptides in invertebrates with that in vertebrates.

    Main Methods:

    • Incubation of enkephalin and related peptides with hemolymph from Astacus fluviatilis and Limulus polyphemus.

    Related Experiment Videos

  • Identification and characterization of enzymatic activities (aminopeptidase, carboxypeptidase, peptidyl-dipeptidase) in the hemolymph.
  • Comparative analysis of enzyme properties between invertebrate and vertebrate systems.

    • Main Results:

    • Enkephalin and related peptides were found to be rapidly inactivated in the hemolymph of both Astacus fluviatilis and Limulus polyphemus.
    • At least three distinct enzymes—an aminopeptidase, a carboxypeptidase, and a peptidyl-dipeptidase—were identified acting on these peptide substrates.
    • The characterized enzymes showed properties that were compared to their vertebrate counterparts, revealing potential differences in their mechanisms or efficiency.

    Conclusions:

    • Opioid peptides are extremely short-lived in invertebrate hemolymph due to rapid enzymatic degradation.
    • The identified enzymatic system in invertebrate hemolymph acts as a significant metabolic barrier, potentially limiting the potency and duration of action of these peptides compared to vertebrate blood.
    • This study highlights a key difference in peptide metabolism between invertebrates and vertebrates, with implications for understanding neuropeptide signaling across phyla.