Variant Synonymizer: Platform to identify mutations defined in different ways is available now!

VarSy

Over 2,000 gene–disease validation summaries are now available—no login required!

Browse Summaries

GGCX – Body Skin Hyperlaxity due to Vitamin K-dependent Coagulation Factor Deficiency

The γ-glutamyl carboxylase encoded by GGCX catalyzes the post-translational γ-carboxylation of vitamin K-dependent proteins essential for coagulation and extracellular matrix mineralization. Loss‐of‐function variants in GGCX underlie hereditary combined vitamin K-dependent coagulation factor deficiency type 1 (VKCFD1), manifesting with bleeding diathesis and skin hyperlaxity classified as body skin hyperlaxity due to vitamin K-dependent coagulation factor deficiency.

Clinical Validity

Inheritance is autosomal recessive. Four unrelated probands in two distinct families with biallelic GGCX variants have been reported, including compound heterozygosity for a splice‐site change and a missense substitution, and uniparental disomy, confirming loss‐of‐function as the disease mechanism (4 probands total; 2 families) (PMID:15287948, PMID:27681307).

ClinGen classification: Moderate
a. 4 probands with molecularly confirmed biallelic GGCX variants; autosomal recessive inheritance; concordant functional data.

Genetic Evidence

VKCFD1 arises from homozygous or compound heterozygous GGCX variants. Reported variant classes include: 1 splice‐site mutation (c.215-1G>T) and multiple missense changes. Recurrent alleles or founder variants have not been observed. No additional segregation beyond probands has been documented.

Representative variant: c.1454G>C (p.Arg485Pro) (PMID:15287948).

Genetic evidence tier: Moderate (“3 probands with compound heterozygous variants; AR inheritance; functional concordance”).

Functional Evidence

Biochemical and cellular assays demonstrate that missense variants such as p.Arg485Pro impair γ-glutamyl carboxylase activity, leading to defective carboxylation of coagulation factors and matrix Gla protein. Rescue experiments with vitamin K only partially normalize activity, consistent with in vivo bleeding and cutaneous phenotypes. Complementary studies of Δ2GGCX splice‐isoform overexpression via uniparental disomy models confirm that loss of full‐length GGCX disrupts both hepatic and extra‐hepatic vitamin K-dependent proteins.

Functional evidence tier: Moderate (“Multiple in vitro assays and UPD model confirm loss of GGCX function; partial rescue with vitamin K”).

Integration and Conclusion

Biallelic GGCX loss‐of‐function variants cause an autosomal recessive syndrome of combined coagulation factor deficiency with marked skin hyperlaxity. Genetic findings are supported by concordant functional assays demonstrating impaired enzyme activity. This association informs molecular diagnosis, guides vitamin K supplementation strategies, and facilitates genetic counseling for VKCFD1 patients with cutaneous manifestations.

Key take‐home: AR GGCX mutations should be considered in patients with unexplained bleeding and skin hyperlaxity to enable targeted therapy and family screening.

References

  • British Journal of Haematology • 2004 • Compound heterozygous mutations in the gamma-glutamyl carboxylase gene cause combined deficiency of all vitamin K-dependent blood coagulation factors. PMID:15287948
  • Journal of Thrombosis and Haemostasis • 2016 • Uniparental disomy causes deficiencies of vitamin K-dependent proteins. PMID:27681307

Evidence Based Scoring (AI generated)

Gene–Disease Association

Moderate

4 probands in 2 families with biallelic GGCX variants; autosomal recessive inheritance; concordant functional data

Genetic Evidence

Moderate

3 probands with compound heterozygous variants; AR inheritance; functional concordance

Functional Evidence

Moderate

Multiple in vitro assays and UPD model confirm loss of GGCX function; partial rescue with vitamin K