Search results for "Osteochondrodysplasias"

showing 10 items of 18 documents

Skeletal Dysplasia Mutations Effect on Human Filamins’ Structure and Mechanosensing

2016

AbstractCells’ ability to sense mechanical cues in their environment is crucial for fundamental cellular processes, leading defects in mechanosensing to be linked to many diseases. The actin cross-linking protein Filamin has an important role in the conversion of mechanical forces into biochemical signals. Here, we reveal how mutations in Filamin genes known to cause Larsen syndrome and Frontometaphyseal dysplasia can affect the structure and therefore function of Filamin domains 16 and 17. Employing X-ray crystallography, the structure of these domains was first solved for the human Filamin B. The interaction seen between domains 16 and 17 is broken by shear force as revealed by steered mo…

0301 basic medicineFilaminsScienceProtein domainPeptide bindingPlasma protein bindingmacromolecular substancesBiologyMolecular Dynamics SimulationFilaminmedicine.disease_causeBioinformaticsCrystallography X-RayOsteochondrodysplasiasMechanotransduction CellularArticlecomputational biophysics03 medical and health sciences0302 clinical medicineProtein DomainsmedicineHumansLarsen syndromeForeheadMechanotransductionNMR-spektroskopiaActinMutationMultidisciplinaryBinding SitesQRSAXSmedicine.diseasecytoskeletal proteinsActinsCell biologybody regions030104 developmental biologyMutationMedicine030217 neurology & neurosurgeryröntgenkristallografiaProtein Binding
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Preselection of cases through expert clinical and radiological review significantly increases mutation detection rate in multiple epiphyseal dysplasia

2006

Skeletal dysplasias are difficult to diagnose for the nonexpert. In a previous study of patients with multiple epiphyseal dysplasia (MED), we identified cartilage oligomeric matrix protein (COMP) mutations in only 36% of cases and suspected that the low-mutation detection rate was partially due to misdiagnosis. We therefore instituted a clinical–radiographic review system, whereby all cases were evaluated by a panel of skeletal dysplasia experts (European Skeletal Dysplasia Network). Only those patients in whom the diagnosis of MED was confirmed by the panel were screened for mutations. Under this regimen the mutation detection rate increased to 81%. When clinical–radiological diagnostic cr…

AdultMaleMutation ratemedicine.medical_specialtyDNA Mutational AnalysisCartilage Oligomeric Matrix ProteinOsteochondrodysplasiasArticleMultiple epiphyseal dysplasiaGeneticsmedicineHumansMatrilin ProteinsGenetic TestingGenetics (clinical)Genetic testingGlycoproteinsCartilage oligomeric matrix proteinExtracellular Matrix Proteinsmedicine.diagnostic_testbiologybusiness.industryCartilageMiddle Agedmedicine.diseaseRadiographyRegimenmedicine.anatomical_structureDysplasiaChild PreschoolMutation (genetic algorithm)Mutationbiology.proteinFemaleRadiologybusiness
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Recessive multiple epiphyseal dysplasia (rMED): phenotype delineation in eighteen homozygotes for DTDST mutation R279W.

2003

Multiple epiphyseal dysplasia (MED) is a generalised skeletal dysplasia that although relatively mild is associated with significant morbidity. Joint pain, joint deformity, waddling gait, and short stature are the main clinical signs and symptoms. In the past, the disorder was subdivided into the milder Ribbing type, usually with flattened epiphyses,1 and the more severe Fairbank type with round epiphyses,2 but many cases were not classifiable as clearly either type.3 MED can be caused by mutations in at least six separate genes: COMP ,4–7 collagen IX ( COL9A1 , COL9A2 , and COL9A3 ),8–13 matrilin 3 ( MATN3 ),15 and the sulphate transporter, DTDST ( DTDST/SLC26A2 ). We have previously repor…

AdultMalePathologymedicine.medical_specialtyAdolescentAnion Transport ProteinsGenes RecessiveBiologySLC26A2ArginineOsteochondrodysplasiasShort statureMultiple epiphyseal dysplasiaGeneticsmedicineHumansChildGenetics (clinical)GeneticsAchondrogenesisSulfatesPoint mutationHomozygoteTryptophanChromosome MappingMembrane Transport ProteinsBiological TransportMiddle Agedmedicine.diseasePhenotypeGenetic defects of metabolism [UMCN 5.1]Amino Acid SubstitutionDysplasiaSulfate TransportersMutation (genetic algorithm)MutationMutation testingbiology.proteinFemalemedicine.symptomCarrier ProteinsLetter to JMGJournal of medical genetics
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Genotypic and phenotypic spectrum in tricho-rhino-phalangeal syndrome types I and III

2000

Tricho-rhino-phalangeal syndrome (TRPS) is characterized by craniofacial and skeletal abnormalities. Three subtypes have been described: TRPS I, caused by mutations in the TRPS1 gene on chromosome 8; TRPS II, a microdeletion syndrome affecting the TRPS1 and EXT1 genes; and TRPS III, a form with severe brachydactyly, due to short metacarpals, and severe short stature, but without exostoses. To investigate whether TRPS III is caused by TRPS1 mutations and to establish a genotype-phenotype correlation in TRPS, we performed extensive mutation analysis and evaluated the height and degree of brachydactyly in patients with TRPS I or TRPS III. We found 35 different mutations in 44 of 51 unrelated p…

AdultMaleanimal structuresAdolescentGenotypeDNA Mutational AnalysisMolecular Sequence DataLimb Deformities CongenitalBiologyOsteochondrodysplasiasPolymorphism Single NucleotideShort statureLanger–Giedion syndromeGeneticsmedicineHumansMissense mutationTricho–rhino–phalangeal syndromeGenetics(clinical)Amino Acid SequenceChildGenetics (clinical)GeneticsAnthropometryBase SequenceBrachydactylyInfantZinc FingersExonsSyndromeArticlesMiddle AgedMicrodeletion syndromemedicine.diseasePenetranceBody HeightPedigreeDNA-Binding ProteinsRadiographyPhenotypeChild PreschoolMutationTrichorhinophalangeal Syndrome Type IErythroid-Specific DNA-Binding FactorsFemalemedicine.symptomChromosomes Human Pair 8Transcription Factors
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Profilin 1 is required for abscission during late cytokinesis of chondrocytes

2009

Profilins are key factors for dynamic rearrangements of the actin cytoskeleton. However, the functions of profilins in differentiated mammalian cells are uncertain because profilin deficiency is early embryonic lethal for higher eukaryotes. To examine profilin function in chondrocytes, we disrupted the profilin 1 gene in cartilage (Col2pfn1). Homozygous Col2pfn1 mice develop progressive chondrodysplasia caused by disorganization of the growth plate and defective chondrocyte cytokinesis, indicated by the appearance of binucleated cells. Surprisingly, Col2pfn1 chondrocytes assemble and contract actomyosin rings normally during cell division; however, they display defects during late cytokines…

Cell divisionMice Transgenicmacromolecular substancesBiologyMyosinsOsteochondrodysplasiasGeneral Biochemistry Genetics and Molecular BiologyChondrocyteArticleBone and BonesMiceProfilinsChondrocytesMyosinmedicineAnimalsMolecular BiologyActinCytokinesisGeneral Immunology and MicrobiologyGeneral NeuroscienceActin cytoskeletonActinsCell biologymedicine.anatomical_structureCartilageProfilinGene Targetingbiology.proteinLamellipodiumCytokinesis
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A novel mutation in FGFR-3 disrupts a putative N-glycosylation site and results in hypochondroplasia

2000

Winterpacht, Andreas, Katja Hilbert, Christiane Stelzer, Thorsten Schweikardt, Heinz Decker, Hugo Segerer, Jürgen Spranger, and Bernhard Zabel. A novel mutation in FGFR-3 disrupts a putative N-glycosylation site and results in hypochondroplasia. Physiol. Genomics 2: 9–12, 2000.—Fibroblast growth factor receptor 3 (FGFR3) is a glycoprotein that belongs to the family of tyrosine kinase receptors. Specific mutations in the FGFR3 gene are associated with autosomal dominant human skeletal disorders such as hypochondroplasia, achondroplasia, and thanatophoric dysplasia. Hypochondroplasia (HCH), the mildest form of this group of short-limbed dwarfism disorders, results in ∼60% of cases from a mut…

GlycosylationGlycosylationPhysiologyDNA Mutational AnalysisHypochondroplasiaOsteochondrodysplasiasReceptor tyrosine kinaseMicechemistry.chemical_compoundGeneticsmedicineAnimalsHumansPoint MutationReceptor Fibroblast Growth Factor Type 3N-Glycosylation SiteGeneticschemistry.chemical_classificationBinding SitesBase SequencebiologyInfantDNAProtein-Tyrosine Kinasesmedicine.diseaseReceptors Fibroblast Growth FactorMolecular biologyProtein Structure TertiaryMice Inbred C57BLAmino Acid SubstitutionchemistryFibroblast growth factor receptorMutationbiology.proteinFemaleGlycoproteinNovel mutationPhysiological Genomics
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Identification of Novel pro-α2(IX) Collagen Gene Mutations in Two Families with Distinctive Oligo-Epiphyseal Forms of Multiple Epiphyseal Dysplasia

1999

Multiple epiphyseal dysplasia (MED) is a genetically heterogeneous disorder with marked clinical and radiographic variability. Traditionally, the mild "Ribbing" and severe "Fairbank" types have been used to define a broad phenotypic spectrum. Mutations in the gene encoding cartilage oligomeric-matrix protein have been shown to result in several types of MED, whereas mutations in the gene encoding the alpha2 chain of type IX collagen (COL9A2) have so far been found only in two families with the Fairbank type of MED. Type IX collagen is a heterotrimer of pro-alpha chains derived from three distinct genes-COL9A1, COL9A2, and COL9A3. In this article, we describe two families with distinctive ol…

MaleAdolescentRNA SplicingMutantGene mutationBiologyOsteochondrodysplasiasmedicine.disease_causeMultiple epiphyseal dysplasia03 medical and health sciencesExon0302 clinical medicineOsteoarthritismedicineGeneticsHumansGenetics(clinical)Genetic TestingOsteochondrodysplasiaMultiple epiphyseal dysplasiaGene mutationAlleleChildPolymorphism Single-Stranded ConformationalGenetics (clinical)030304 developmental biologyGenetics0303 health sciencesMutationType IX collagenGenetic heterogeneitymedicine.diseaseOsteochondrodysplasiaPedigreeRadiographyCartilageChild PreschoolMutationFemaleEpiphysesProcollagen030217 neurology & neurosurgeryResearch ArticleThe American Journal of Human Genetics
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The spondylometaphyseal dysplasias. A tentative classification.

1991

The spondylometaphyseal dysplasias constitute a very complex group of disorders. In addition to the Kozlowski type, three subgroups can be distinguished by the appearance of the femoral neck. In the first group (A) the changes are severe with absent ossification of the femoral neck and coxa vara. In the second group (B) the changes of the femoral neck are moderate and in the third (C) mild metaphyseal irregularities are only visible. This classification is not definitive but tries to put order in this confusing section of constitutional bone diseases.

MaleBone diseaseAdolescentCoxa varaOsteochondrodysplasiasmedicineHumansRadiology Nuclear Medicine and imagingChildFemoral neckbusiness.industryOssificationFemur NeckInfantAnatomymedicine.diseaseHandmedicine.anatomical_structureSpondylometaphyseal dysplasiaDysplasiaChild PreschoolPediatrics Perinatology and Child HealthFemaleSpinal Diseasesmedicine.symptombusinessPediatric radiology
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The deletion of six amino acids at the C-terminus of the alpha 1 (II) chain causes overmodification of type II and type XI collagen: further evidence…

1996

We have identified an 18 bp deletion in exon 49 of the type II procollagen gene (COL2A1) in a patient with Kniest dysplasia. The deletion is located at the very C-terminus of the helical domain and removes two of three Gly-Pro-Pro triplets at positions 1007-1012, which are thought to be involved in helix formation and stability. Morphological investigation of an iliac crest biopsy showed large inclusions in the endoplasmic reticulum of chondrocytes, reflecting impaired secretion of type II collagen. Electrophoretic analysis of collagens extracted from cartilage or synthesised by cultured chondrocytes showed that type II and also type XI procollagen molecules containing mutant alpha 1 (II) c…

MaleDNA Mutational AnalysisMolecular Sequence DataMutantType II collagenBiologyOsteochondrodysplasiasChondrocyteIliumExonKniest dysplasiaGeneticsmedicineHumansAmino Acid SequencePeptide sequenceCells CulturedGenetics (clinical)Sequence DeletionInclusion BodiesGeneticsBase SequenceC-terminusExonsmedicine.diseaseMolecular biologyProcollagen peptidaseCartilagemedicine.anatomical_structureGenesChild PreschoolCollagenEndoplasmic Reticulum RoughProcollagenResearch ArticleJournal of Medical Genetics
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Sedaghatian congenital lethal metaphyseal chondrodysplasia—observations in a second Iranian family and histopathological studies

1987

In 1980, Sedaghatian described in two brothers and one sister a neonatally lethal disorder associated with slight rhizomelic limb shortness, mild platyspondyly, and severe metaphyseal dysplasia. Here data are presented on another Iranian infant with the Sedaghatian syndrome who died on day 4 and was found to have histologic evidence of severe epimetaphyseal dysplasia. The occurrence in children of both sexes in one instance, born to normal parents who were first cousins, and currently apparent confinement of the disorder to Iranians suggests that the Sedaghatian syndrome is an autosomal recessive trait with high gene frequency in Iranians. This may be a more complexly pleiotropic syndrome t…

MaleGeneticsmedicine.medical_specialtyDepressed nasal bridgeMetaphyseal chondrodysplasiabusiness.industryInfant NewbornShort neckConsanguinityIranOsteochondrodysplasiasmedicine.diseaseMetaphyseal dysplasiaDermatologyMicrophthalmiaBone and BonesAutosomal recessive traitCartilageDysplasiaotorhinolaryngologic diseasesmedicineHumansbusinessGenetics (clinical)American Journal of Medical Genetics
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