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CRABP1 in Non-Canonical Activities of Retinoic Acid in Health and Diseases

Jennifer Nhieu1, Yu-Lung Lin1, Li-Na Wei1

  • 1Department of Pharmacology, University of Minnesota, Minneapolis, MN 55455, USA.

Nutrients
|April 12, 2022
PubMed

Insights

Cellular Retinoic Acid Binding Protein 1 (CRABP1) mediates non-canonical retinoic acid (RA) activities, impacting stem cells, cancer, and neurological disorders. Targeting CRABP1 offers therapeutic potential for various human diseases.

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Cellular Retinoic Acid Binding Protein 1 (CRABP1) traditionally binds retinoic acid (RA).
  • Emerging evidence suggests CRABP1 mediates non-canonical RA activities.
  • These activities are relevant to various human diseases.

Purpose of the Study:

  • To review the non-canonical roles of CRABP1.
  • To explore CRABP1's involvement in regulating MAPK and CaMKII signaling pathways.
  • To discuss the implications of CRABP1 in human diseases and potential therapeutic strategies.

Main Methods:

  • Review of molecular and genetic studies, including Crabp1 knockout (CKO) mouse models.
  • Analysis of cell culture models.
  • Examination of gene expression data and CRABP1 gene single nucleotide polymorphisms (SNPs) in patient cohorts.

Main Results:

  • CRABP1 regulates MAPK activities, influencing stem cell proliferation, cancers, adipocyte health, and neuro-immune regulation.
  • CRABP1 also regulates CaMKII activities, impacting heart and motor neuron diseases.
  • CRABP1 forms RA-regulated signalsomes in a cell context-dependent manner.

Conclusions:

  • CRABP1 plays a significant role in diverse cellular processes beyond canonical RA signaling.
  • Abnormalities in CRABP1 are implicated in human diseases like cancer, neurodegeneration, and immune disorders.
  • Targeting CRABP1 presents a promising therapeutic avenue for managing these conditions.
Keywords:
CAMKIICRABP1MAPKcancerhuman diseaseinflammationmetabolismneurodegenerationnon-canonicalretinoic acid

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