Two Surgical Cases of Os Odontoideum in Spondyloepiphyseal Dysplasia Tarda.

In recent years, the number of individuals with dwarfism participating in sports and physical activities has increased. The Dwarf Athletic Association of America (DAAA) has grown from 30 athletes in 1985 to over 600 in 1994. This paper details the structural, intellectual, motor, orthopedic, and medical characteristics of six types of dwarfism (achondroplasia, hypochon-droplasia, cartilage-hair hypoplasia, diastrophic dysplasia, spondyloepiphyseal dysplasia tarda, and spondyloepiphyseal dysplasia congenita) seen in individuals currently participating in eight DAAA-sanctioned sports. Implications and modifications for participation in physical activity, physical education, and sport are included.

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A single nucleotide deletion of 293delT in SEDL gene causing spondyloepiphyseal dysplasia tarda in a four-generation Chinese family

Mutation Research/Fundamental and Molecular Mechanisms of Mutagenesis ◽

10.1016/s0027-5107(02)00315-9 ◽

2003 ◽

Vol 525 (1-2) ◽

pp. 61-65 ◽

Cited By ~ 5

Author(s):

Cuiying Xiao ◽

Sizhong Zhang ◽

Jun Wang ◽

Weimin Qiu ◽

Leiting Chi ◽

...

Keyword(s):

Chinese Family ◽

Single Nucleotide ◽

Single Nucleotide Deletion ◽

Nucleotide Deletion ◽

Spondyloepiphyseal Dysplasia ◽

Spondyloepiphyseal Dysplasia Tarda

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A novel deletion variant in TRAPPC2 causes spondyloepiphyseal dysplasia tarda in a five-generation Chinese family

BMC Medical Genetics ◽

10.1186/s12881-020-01052-8 ◽

2020 ◽

Vol 21 (1) ◽

Author(s):

Cai Zhang ◽

Caiqi Du ◽

Juan Ye ◽

Feng Ye ◽

Renfa Wang ◽

...

Keyword(s):

Chinese Family ◽

Deletion Variant ◽

Spondyloepiphyseal Dysplasia ◽

Spondyloepiphyseal Dysplasia Tarda

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Crystal Structure of SEDL and Its Implications for a Genetic Disease Spondyloepiphyseal Dysplasia Tarda

Journal of Biological Chemistry ◽

10.1074/jbc.m207436200 ◽

2002 ◽

Vol 277 (51) ◽

pp. 49863-49869 ◽

Cited By ~ 57

Author(s):

Se Bok Jang ◽

Yeon-Gil Kim ◽

Yong-Soon Cho ◽

Pann-Ghill Suh ◽

Kyung-Hwa Kim ◽

...

Keyword(s):

Protein Interactions ◽

Genetic Disease ◽

Point Mutations ◽

Missense Mutations ◽

Protein Protein Interactions ◽

Spondyloepiphyseal Dysplasia ◽

Multiple Protein ◽

Protein Particle ◽

Eukaryotic Organisms ◽

Spondyloepiphyseal Dysplasia Tarda

SEDL is an evolutionarily highly conserved protein in eukaryotic organisms. Deletions or point mutations in theSEDLgene are responsible for the genetic disease spondyloepiphyseal dysplasia tarda (SEDT), an X-linked skeletal disorder. SEDL has been identified as a component of the transport protein particle (TRAPP), critically involved in endoplasmic reticulum-to-Golgi vesicle transport. Herein, we report the 2.4 Å resolution structure of SEDL, which reveals an unexpected similarity to the structures of the N-terminal regulatory domain of two SNAREs, Ykt6p and Sec22b, despite no sequence homology to these proteins. The similarity and the presence of unusually many solvent-exposed apolar residues of SEDL suggest that it serves regulatory and/or adaptor functions through multiple protein-protein interactions. Of the four known missense mutations responsible for SEDT, three mutations (S73L, F83S, V130D) map to the protein interior, where the mutations would disrupt the structure, and the fourth (D47Y) on a surface at which the mutation may abrogate functional interactions with a partner protein.

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Corneal Changes in Spondyloepiphyseal Dysplasia Tarda

Japanese Journal of Ophthalmology ◽

10.1016/s0021-5155(99)00146-x ◽

2000 ◽

Vol 44 (1) ◽

pp. 29-32 ◽

Cited By ~ 3

Author(s):

Y Hirata

Keyword(s):

Spondyloepiphyseal Dysplasia ◽

Spondyloepiphyseal Dysplasia Tarda

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Biochemical consequences of sedlin mutations that cause spondyloepiphyseal dysplasia tarda

Biochemical Journal ◽

10.1042/bj20090541 ◽

2009 ◽

Vol 423 (2) ◽

pp. 233-242 ◽

Cited By ~ 14

Author(s):

Mei Y. Choi ◽

Caleb C. Y. Chan ◽

Danny Chan ◽

Keith D. K. Luk ◽

Kathryn S. E. Cheah ◽

...

Keyword(s):

Late Onset ◽

Transport Protein ◽

Missense Mutations ◽

Wild Type ◽

Spondyloepiphyseal Dysplasia ◽

Type Protein ◽

Wild Type Protein ◽

Protein Particle ◽

Spondyloepiphyseal Dysplasia Tarda

SEDT (spondyloepiphyseal dysplasia tarda) is a late-onset X-linked recessive skeletal dysplasia caused by mutations in the gene SEDL coding for sedlin. In the present paper, we investigated four missense mutations observed in SEDT and compare biochemical and cellular characteristics relative to the wild-type protein to address the mechanism of disease and to gain insight into the function of the sedlin protein. In situ hybridization and immunohistochemical experiments in mouse growth plates revealed sedlin to be predominantly expressed in proliferating and hypertrophic chondrocytes. Cell culture studies showed that the wild-type protein localized predominantly in the vicinity of the nucleus and the Golgi, with further localization around the cytoplasm, whereas mutation resulted in mislocalization. The D47Y mutant was expressed similarly to the wild-type, but the S73L, F83S and V130D mutants showed particularly low levels of expression that were rescued in the presence of the proteasome inhibitor MG132 (benzyloxycarbonyl-leucylleucylleucinal). Furthermore, whereas the D47Y mutant folded similarly and had similar stability to the wild-type sedlin as shown by CD and fluorescence, the S73L, F83S and V130D mutants all misfolded during expression. Two independent assays showed that the D47Y mutation resulted in an increased affinity for the transport protein particle component Bet3 compared with the wild-type sedlin. Our results suggest that the sedlin mutations S73L, F83S and V130D cause SEDT by sedlin misfolding, whereas the D47Y mutation may influence normal TRAPP (transport protein particle) dynamics.

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