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

Human arginase isozymes.

W W Grody, G J Dizikes, S D Cederbaum

    Isozymes
    |January 1, 1987
    PubMed
    Summary
    This summary is machine-generated.

    Two distinct arginase isozymes, AI and AII, exist in humans and animals. AI aids ammonia detoxification, while AII produces ornithine, with mutations in AI causing hyperargininemia.

    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

    Expanded carrier screening for inherited genetic disease using exome and genome sequencing.

    Journal of genetic counseling·2024
    Same author

    ECFS standards of care on CFTR-related disorders: Towards a comprehensive program for affected individuals.

    Journal of cystic fibrosis : official journal of the European Cystic Fibrosis Society·2024
    Same author

    Biochemical characteristics of newborns with carnitine transporter defect identified by newborn screening in California.

    Molecular genetics and metabolism·2017
    Same author

    AIDS and the heart: Review and consideration of pathogenetic mechanisms.

    Cardiovascular pathology : the official journal of the Society for Cardiovascular Pathology·2015
    Same author

    Minimal ureagenesis is necessary for survival in the murine model of hyperargininemia treated by AAV-based gene therapy.

    Gene therapy·2015
    Same author

    Minimal ureagenesis is necessary for survival in the murine model of hyperargininemia treated by AAV-based gene therapy.

    Gene therapy·2014
    Same journal

    Genetics, expression, and modification in the human alkaline phosphatases.

    Isozymes·1987
    Same journal

    Plant genetic resources: prediction by isozyme markers and ecology.

    Isozymes·1987
    Same journal

    Plant peroxidases.

    Isozymes·1987
    Same journal

    Regulation and structure of isozymes of sugar phosphate metabolism in plants.

    Isozymes·1987
    Same journal

    Human aldehyde dehydrogenase isozymes and alcohol sensitivity.

    Isozymes·1987
    Same journal

    The effect of heavy metals on isozyme gene expression in Silene cucubalus.

    Isozymes·1987
    See all related articles

    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Human Physiology

    Background:

    • Two arginase isozymes, AI (high pI, cytosolic) and AII (neutral pI, mitochondrial), have been identified in humans and experimental animals.
    • Arginase AI is predominantly found in the liver and is crucial for ammonia detoxification into urea.
    • Arginase AII is widely expressed and involved in ornithine production for proline and glutamate synthesis.

    Purpose of the Study:

    • To elucidate the distinct roles and characteristics of the two identified arginase isozymes.
    • To understand the genetic basis of hyperargininemia related to arginase AI.
    • To differentiate the immunological and genetic properties of arginase AI and AII.

    Main Methods:

    • Comparative analysis of arginase isozyme properties in experimental animals and humans.

    Related Experiment Videos

  • Investigation of the gene mutation responsible for human hyperargininemia.
  • Immunological assays to assess distinctness between isozymes.
  • DNA cross-hybridization studies to evaluate genetic differences.

    • Main Results:

    • Arginase AI is primarily involved in ammonia detoxification, with mutations causing hyperargininemia.
    • Arginase AII is implicated in ornithine production, serving as a precursor for proline and glutamate.
    • Both isozymes are encoded by separate genes and are immunologically distinct.
    • Despite kinetic similarities, significant compositional differences exist between AI and AII.

    Conclusions:

    • The human body possesses two distinct arginase isozymes with specialized functions: AI for ammonia detoxification and AII for ornithine production.
    • Genetic defects in arginase AI lead to hyperargininemia, highlighting its critical role in urea cycle.
    • The immunological and genetic distinctness of arginase AI and AII underscore their separate evolutionary and functional pathways.