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TRPV4 – Spondylometaphyseal Dysplasia, Kozlowski Type

Spondylometaphyseal dysplasia, Kozlowski type (SMDK) is an autosomal dominant skeletal dysplasia characterized by short stature, metaphyseal abnormalities, platyspondyly, and variable neurologic features. Radiographically, patients display thickened hyaline cartilage at ossification centers, metaphyseal cupping, and notochordal remnants within vertebrae and discs. Clinical diagnosis is confirmed by identification of pathogenic variants in TRPV4, which encodes a calcium-permeable cation channel. TRPV4 and Spondylometaphyseal Dysplasia, Kozlowski type have a well-established gene-disease relationship.

Multiple independent case reports have described heterozygous missense variants in TRPV4 in SMDK probands. A de novo c.2389G>A (p.Glu797Lys) was identified in a 9-year-old male with progressive kyphoscoliosis and compressive myelopathy (PMID:38721578). A c.1781G>A (p.Arg594His) substitution was reported in a 2-year-old patient with typical metaphyseal changes and notochordal remnants (PMID:28687525). In a cohort of 20 SMDK probands, 19 carried TRPV4 mutations, including a recurrent R594H hotspot in 12 subjects and seven novel alleles (PMID:20577006). An additional nine unrelated SMDK patients from 21 families all harbored heterozygous TRPV4 variants, underscoring replication across multiple centers (PMID:21658220).

Although formal segregation counts are limited, the recurrent R594H allele in unrelated families and de novo occurrence of p.Glu797Lys support pathogenicity. No large multi-generation pedigrees with detailed co-segregation have been published, but heterozygous alleles consistently track with disease in simplex and familial cases.

The variant spectrum in SMDK is dominated by missense substitutions clustered in cytoplasmic and pore-lining domains. Recurrent codon 594 substitutions (c.1781G>A (p.Arg594His)) and exon 15 variants such as c.2389G>A (p.Glu797Lys) illustrate hotspots. All reported SMDK alleles are single nucleotide changes predicting amino acid substitutions; loss-of-function and splice variants have not been linked to this phenotype.

Functional studies demonstrate a gain-of-function mechanism concordant with human phenotype. Disruption of the L596–W733 bond (e.g., p.Leu596Pro) elevates basal open probability and reduces agonist responsiveness, leading to constitutive channel activation (PMID:25737550). Moreover, mutations adjacent to the calmodulin binding domain (p.Glu797Lys) abolish CaM-mediated autoinhibition, further increasing constitutive Ca2+ influx (PMID:26170305). These data are consistent across electrophysiological and biophysical assays.

Collectively, over 30 unrelated SMDK probands, including de novo occurrences and multiple recurrent alleles, combined with robust gain-of-function evidence, firmly establish TRPV4 as a strong gene-disease association. Key take-home: TRPV4 gain-of-function missense variants should be considered diagnostic for SMDK in patients with characteristic radiographic features.

References

  • European journal of medical genetics • 2017 • SMD Kozlowski type caused by p.Arg594His substitution in TRPV4 reveals abnormal ossification and notochordal remnants in discs and vertebrae. PMID:28687525
  • Journal of pediatric genetics • 2024 • Compressive Myelopathy Secondary to TRPV4 Skeletal Dysplasia: Spondylometaphyseal Dysplasia, Kozlowski Type. PMID:38721578
  • Journal of medical genetics • 2010 • Novel and recurrent TRPV4 mutations and their association with distinct phenotypes within the TRPV4 dysplasia family. PMID:20577006
  • Orphanet journal of rare diseases • 2011 • TRPV4 related skeletal dysplasias: a phenotypic spectrum highlighted by clinical, radiographic, and molecular studies in 21 new families. PMID:21658220
  • Proceedings of the National Academy of Sciences of the United States of America • 2015 • L596-W733 bond between the start of the S4-S5 linker and the TRP box stabilizes the closed state of TRPV4 channel. PMID:25737550
  • Proceedings of the National Academy of Sciences of the United States of America • 2015 • A channelopathy mechanism revealed by direct calmodulin activation of TrpV4. PMID:26170305

Evidence Based Scoring (AI generated)

Gene–Disease Association

Strong

~30 probands across multiple unrelated families with replication and de novo events; consistent phenotype–genotype correlation and functional data

Genetic Evidence

Strong

30 affected individuals including 2 de novo variants and recurrent Arg594 hotspot across independent cohorts ([PMID:28687525]; [PMID:38721578]; [PMID:20577006]; [PMID:21658220])

Functional Evidence

Moderate

In vitro electrophysiology and structural studies show gain-of-function via disrupted TRPV4 gating and loss of autoinhibition ([PMID:25737550]; [PMID:26170305])