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APOA1 – Primary Hypoalphalipoproteinemia Type 2

APOA1-related primary hypoalphalipoproteinemia type 2 is an autosomal recessive disorder characterized by severely reduced HDL-cholesterol due to biallelic loss-of-function variants. Three unrelated probands have been reported: a 69-year-old woman with a c.552del (p.Thr185ArgfsTer) frameshift and early stop, a patient with carboxyl-terminal truncation p.His186ProfsTer46, and a homozygous c.322C>T (p.Gln108Ter) nonsense variant, all leading to undetectable apoA-I levels and low HDL (PMID:11996960)(PMID:29396262)(PMID:1901417).

Functional studies in patient plasma, cell models and transgenic mice demonstrate that these truncating mutations abolish apoA-I secretion, impair HDL disc formation, reduce LCAT activation and accelerate apoA-I catabolism, consistent with a haploinsufficiency mechanism (PMID:1898657)(PMID:2111322). No segregation beyond the index cases has been documented, but extensive concordant experimental data support pathogenicity and inform diagnostic decision-making and potential therapeutic targeting.

Key take-home: Biallelic truncating APOA1 variants cause a clinically recognizable AR HDL-deficiency syndrome with robust functional evidence, enabling accurate molecular diagnosis and guiding future intervention trials.

References

  • Atherosclerosis | 2002 | Apolipoprotein A-I deficiency with accumulated risk for CHD but no symptoms of CHD. PMID:11996960
  • Journal of Clinical Lipidology | 2018 | A case of apolipoprotein A-I deficiency due to carboxyl-terminal truncation. PMID:29396262
  • Proceedings of the National Academy of Sciences of the United States of America | 1991 | Apolipoprotein A-I deficiency due to a codon 84 nonsense mutation of the apolipoprotein A-I gene. PMID:1901417
  • The Journal of Clinical Investigation | 1991 | A frameshift mutation in the human apolipoprotein A-I gene causes high density lipoprotein deficiency, partial lecithin: cholesterol-acyltransferase deficiency, and corneal opacities. PMID:1898657
  • The Journal of Biological Chemistry | 1990 | Structural analysis of human apolipoprotein A-I variants. Amino acid substitutions are nonrandomly distributed throughout the apolipoprotein A-I primary structure. PMID:2111322

Evidence Based Scoring (AI generated)

Gene–Disease Association

Limited

3 probands across unrelated families, no segregation, consistent truncating variants

Genetic Evidence

Limited

3 probands with biallelic truncating LoF variants leading to absent apoA-I levels

Functional Evidence

Moderate

In vitro and in vivo assays demonstrate impaired secretion, HDL formation, LCAT activation and accelerated catabolism