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

Structure and characterization of AAT-1 isoforms.

Eiko Matsuda1, Ray Ishizaki, Takahiro Taira

  • 1Graduate School of Pharmaceutical Sciences, Hokkaido University, Sapporo 060-0812, Japan.

Biological & Pharmaceutical Bulletin
|May 3, 2005
PubMed
Summary

Researchers discovered new forms of the AAT-1 protein, AAT-1L, AAT-1M, and AAT-1S, which bind to AMY-1. These isoforms show differential tissue expression and distinct cellular localizations, suggesting varied roles in cellular functions beyond spermatogenesis.

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

Exploring the link between synesthesia and lucid dreaming through perceptual presence.

Frontiers in psychology·2026
Same author

Cultural Self-Construal and Sustainable Mental Health in Japan: The Role of Subjective, Objective, and Autonomous Selves.

International journal of environmental research and public health·2026
Same author

Subacute Thyroiditis Following COVID-19: A Case of Diagnostic Challenge in the Absence of Neck Pain.

Cureus·2024
Same author

Impacts of sleep disturbance and work-related life stress on depression among Japanese and Chinese workers.

PloS one·2024
Same author

Development of a Cell-Based Assay Using a Split-Luciferase Reporter for Compound Screening.

Biological & pharmaceutical bulletin·2023
Same author

BAY61-3606 Alters snRNP Composition and Enhances Usage of Suboptimal Splice Acceptor Site.

Biological & pharmaceutical bulletin·2023

Area of Science:

  • Molecular Biology
  • Genetics
  • Cell Biology

Background:

  • A novel protein, AAT-1, was identified as an AMY-1 binding protein with three initial splicing variants (AAT-1alpha, -beta, -gamma).
  • The known function of AAT-1 is linked to spermatogenesis.
  • The aat-1 gene comprises 20 exons.

Purpose of the Study:

  • To identify and characterize additional splicing isoforms of AAT-1.
  • To investigate the differential expression and cellular localization of AAT-1 isoforms.
  • To explore the functional implications of AAT-1 isoforms in human cells.

Main Methods:

  • Identification of novel AAT-1 splicing isoforms (AAT-1L, AAT-1M, AAT-1S) through gene analysis.
  • Analysis of promoter usage for different AAT-1 variant groups.

Related Experiment Videos

  • Examination of protein sequence homology across isoforms.
  • Assessment of tissue-specific expression patterns.
  • Investigation of protein-protein interactions and colocalization with AMY-1 using human cells.
  • Determination of subcellular localization of AAT-1 isoforms.
  • Main Results:

    • Three new AAT-1 isoforms (AAT-1L, AAT-1M, AAT-1S) with lengths of 767, 603, and 252 amino acids were identified.
    • AAT-1L, AAT-1M, and AAT-1S utilize a distinct promoter compared to AAT-1alpha, -beta, and -gamma.
    • A conserved C-terminal region (60 amino acids from exons 15-17) is shared among AAT-1L, AAT-1M, AAT-1S, and AAT-1alpha.
    • AAT-1alpha is testis-specific, while AAT-1L, AAT-1M, and AAT-1S exhibit differential expression across various human tissues.
    • All identified AAT-1 isoforms bind to and colocalize with AMY-1 in human cells.
    • AAT-1L and AAT-1M localize to the cytoplasm, whereas AAT-1S and AAT-1alpha are found in mitochondria-like structures.

    Conclusions:

    • The aat-1 gene generates multiple splicing isoforms with distinct regulatory mechanisms and expression patterns.
    • Differential localization of AAT-1 isoforms suggests specialized roles within cellular compartments.
    • The interaction and colocalization of all AAT-1 isoforms with AMY-1 highlight a conserved functional relationship.
    • Further research is warranted to elucidate the specific functions of each AAT-1 isoform in different cellular contexts.