Congenital stationary night blindness associated with morning glory disc malformation: a novel hemizygous mutation in CACNA1F

Abdelkader, Ehab; AlHilali, Sara; Neuhaus, Christine; Bergmann, Carsten; AlMurshed, Tahani; Schatz, Patrik

doi:10.1080/13816810.2018.1498526

Cited by 4 publications

(2 citation statements)

References 14 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…There are type 1A (CSNB1A) and type 1F (CSNB1F) (Tsang and Sharma 2018, review). CSNB1A is caused by the mutations of nyctalopin (Bech‐Hansen et al 2000; Pusch et al 2000; Zhou et al 2015; Leroy et al 2009; Dai et al 2015; Pradhan et al 2011; Wang et al 2012; Xiao et al 2006; Zeitz et al 2005; Sui et al 2008; Ivanova et al 2019) as well as CSNB1F by those of LRIT3 (Zeitz et al 2013, 2015; Dan et al 2017), CACNA1F, TRPM1 (Abdelkader et al 2018), RPM1 (AlTalbishi et al 2019), and GNAT1 (Marmor and Zeitz 2018).…”

Section: Human Diseases Associated With Mutationsmentioning

confidence: 99%

Sequence features, structure, ligand interaction, and diseases in small leucine rich repeat proteoglycans

Matsushima

Miyashita²,

Kretsinger

2021

J. Cell Commun. Signal.

View full text Add to dashboard Cite

Small leucine rich repeat proteoglycans (SLRPs) are a group of active components of the extracellular matrix in all tissues. SLRPs bind to collagens and regulate collagen fibril growth and fibril organization. SLRPs also interact with various cytokines and extracellular compounds, which lead to various biological functions such cell adhesion and signaling, proliferation, and differentiation. Mutations in SLRP genes are associated with human diseases. Now crystal structures of five SLRPs are available. We describe some features of amino acid sequence and structures of SLRPs. We also review ligand interactions and then discuss the interaction surfaces. Furthermore, we map mutations associated with human diseases and discuss possible effects on structures by the mutations.

show abstract

Section: Human Diseases Associated With Mutationsmentioning

confidence: 99%

Sequence features, structure, ligand interaction, and diseases in small leucine rich repeat proteoglycans

Matsushima

Miyashita²,

Kretsinger

2021

J. Cell Commun. Signal.

View full text Add to dashboard Cite

show abstract

“…The CACNA1F gene defect is also responsible for Aland Island eye disease (AIED, OMIM:300600) (Jalkanen et al, 2007) and incomplete congenital stationary night blindness (icCSNB, OMIM: 300071) (Bech‐Hansen et al, 1998; Strom et al, 1998). It comprises 48 exons and codes for the pore‐forming α 1F subunit of the L‐type voltage gated calcium channel (Cav1.4), which localized to rod and cone photoreceptor ribbon synapses and supported Ca 2+ influx under relatively depolarized conditions (Abdelkader et al, 2018; Koschak et al, 2021). Over 200 mutations in CACNA1F including missense, nonsense, splice‐site variants, and indels have been reported (Mahmood et al, 2021).…”

Section: Introductionmentioning

confidence: 99%

Identification of a novel CACNA1F mutation in a Chinese family with CORDX3

Du¹,

Li²,

Zheng³

et al. 2022

Molec Gen & Gen Med

View full text Add to dashboard Cite

Background: X-linked cone-rod dystrophy (CORDX) is one form of inherited retinal disorders (IRDs) characterized by progressive dysfunction of photoreceptor. Three types of CORDX were reported and CACNA1F gene defect can cause CORDX3. The aim of this study was to investigate the pathogenic variant in a Chinese family with IRD. Methods:The two affected subjects including the proband and his elder sister underwent ophthalmic examinations. Whole exome sequencing (WES) was performed in the proband at first, then co-segregation analysis was performed in the family by Sanger sequencing. Minigene approach was used to verify the effect of the mutation on the splicing of CACNA1F. X-chromosomal inactivation assay was performed to evaluate the inactivation patterns of the female carriers. Results: The ophthalmic examination results of the proband fit the clinical description of CORDX3, and the female patient presented with only mild symptoms due to mildly skewed X-chromosomal inactivation (ratio 67: 33). Molecular genetic testing identified a novel splice-site mutation c.3847-2A > G in CACNA1F (NM_005183.4) gene in the patients, which inherited from their asymptomatic mother. Minigene approach confirmed that c.3847-2A > G could affect the splicing of CACNA1F. Conclusion: Our study identified a novel splice-site mutation in the CACNA1F gene, which expanded the mutational spectrum of CACNA1F-releated diseases and demonstrated the importance of combining clinical and genetic testing in the diagnosis of IRDs.

show abstract

Cav1.4 dysfunction and congenital stationary night blindness type 2

Koschak

Fernández‐Quintero

Heigl

et al. 2021

Pflugers Arch - Eur J Physiol

View full text Add to dashboard Cite

Cav1.4 L-type Ca2+ channels are predominantly expressed in retinal neurons, particularly at the photoreceptor terminals where they mediate sustained Ca2+ entry needed for continuous neurotransmitter release at their ribbon synapses. Cav1.4 channel gating properties are controlled by accessory subunits, associated regulatory proteins, and also alternative splicing. In humans, mutations in the CACNA1F gene encoding for Cav1.4 channels are associated with X-linked retinal disorders such as congenital stationary night blindness type 2. Mutations in the Cav1.4 protein result in a spectrum of altered functional channel activity. Several mouse models broadened our understanding of the role of Cav1.4 channels not only as Ca2+ source at retinal synapses but also as synaptic organizers. In this review, we highlight different structural and functional phenotypes of Cav1.4 mutations that might also occur in patients with congenital stationary night blindness type 2. A further important yet mostly neglected aspect that we discuss is the influence of alternative splicing on channel dysfunction. We conclude that currently available functional phenotyping strategies should be refined and summarize potential specific therapeutic options for patients carrying Cav1.4 mutations. Importantly, the development of new therapeutic approaches will permit a deeper understanding of not only the disease pathophysiology but also the physiological function of Cav1.4 channels in the retina.

show abstract

Congenital stationary night blindness associated with morning glory disc malformation: a novel hemizygous mutation in CACNA1F

Cited by 4 publications

References 14 publications

Sequence features, structure, ligand interaction, and diseases in small leucine rich repeat proteoglycans

Sequence features, structure, ligand interaction, and diseases in small leucine rich repeat proteoglycans

Identification of a novel CACNA1F mutation in a Chinese family with CORDX3

Cav1.4 dysfunction and congenital stationary night blindness type 2

Contact Info

Product

Resources

About