elastin has been researched along with Scoliosis* in 8 studies
1 review(s) available for elastin and Scoliosis
Article | Year |
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The pathogenesis of idiopathic scoliosis: uncoupled neuro-osseous growth?
This paper examines the following speculative hypothesis: "that in some patients with scoliosis there is disproportionate neuro-osseous growth--the longitudinal growth of the spinal cord fails to keep pace with the growth of the vertebral column and, as a consequence, the spine buckles into a scoliosis deformity". A literature review of the morphology and neurology of scoliosis does not deny the hypothesis. Several mechanisms are suggested as to why the spinal cord growth could become uncoupled from osseous growth. Topics: Calmodulin; Child; Elastin; Free Radicals; Growth Substances; Humans; Melatonin; Scoliosis; Spinal Cord; Spine | 2001 |
7 other study(ies) available for elastin and Scoliosis
Article | Year |
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Qualitative and quantitative assessment of collagen and elastin in annulus fibrosus of the physiologic and scoliotic intervertebral discs.
The biophysical properties of the annulus fibrosus of the intervertebral disc are determined by collagen and elastin fibres. The progression of scoliosis is accompanied by a number of pathological changes concerning these structural proteins. This is a major cause of dysfunction of the intervertebral disc. The object of the study were annulus fibrosus samples excised from intervertebral discs of healthy subjects and patients treated surgically for scoliosis in the thoracolumbar or lumbar spine. The research material was subjected to structural analysis by light microscopy and quantitative analysis of the content of collagen types I, II, III and IV as well as elastin by immunoenzymatic test (ELISA). A statistical analysis was conducted to assess the impact of the sampling site (Mann-Whitney test, α=0.05) and scoliosis (Wilcoxon matched pairs test, α=0.05) on the obtained results. The microscopic studies conducted on scoliotic annulus fibrosus showed a significant architectural distortion of collagen and elastin fibres. Quantitative biochemical assays demonstrated region-dependent distribution of only collagen types I and II in the case of healthy intervertebral discs whereas in the case of scoliotic discs region-dependent distribution concerned all examined proteins of the extracellular matrix. Comparison of scoliotic and healthy annulus fibrosus revealed a significant decrease in the content of collagen type I and elastin as well as a slight increase in the proportion of collagen types III and IV. The content of collagen type II did not differ significantly between both groups. The observed anomalies are a manifestation of degenerative changes affecting annulus fibrosus of the intervertebral disc in patients suffering from scoliosis. Topics: Annulus Fibrosus; Collagen; Elastin; Humans; Intervertebral Disc; Scoliosis | 2016 |
Prevalence of scoliosis in Williams-Beuren syndrome patients treated at a regional reference center.
This study assessed the prevalence of scoliosis and the patterns of scoliotic curves in patients with Williams-Beuren syndrome. Williams-Beuren syndrome is caused by a chromosome 7q11.23 deletion in a region containing 28 genes, with the gene encoding elastin situated approximately at the midpoint of the deletion. Mutation of the elastin gene leads to phenotypic changes in patients, including neurodevelopmental impairment of varying degrees, characteristic facies, cardiovascular abnormalities, hypercalcemia, urological dysfunctions, and bone and joint dysfunctions.. A total of 41 patients diagnosed with Williams-Beuren syndrome, who were followed up at the genetics ambulatory center of a large referral hospital, were included in the study. There were 25 male subjects. The patients were examined and submitted to radiographic investigation for Cobb angle calculation.. It was observed that 14 patients had scoliosis; of these 14 patients, 10 were male. The pattern of deformity in younger patients was that of flexible and simple curves, although adults presented with double and triple curves. Statistical analysis showed no relationships between scoliosis and age or sex.. This study revealed a prevalence of scoliosis in patients with Williams-Beuren syndrome of 34.1%; however, age and sex were not significantly associated with scoliosis or with the severity of the curves. Topics: Adolescent; Adult; Age Factors; Brazil; Child; Child, Preschool; Chromosome Deletion; Cross-Sectional Studies; Elastin; Female; Humans; Male; Multivariate Analysis; Prevalence; Scoliosis; Sex Factors; Williams Syndrome; Young Adult | 2014 |
Ultrastructural immunolocalization of alpha-elastin and keratan sulfate proteoglycan in normal and scoliotic lumbar disc.
Comparative ultrastructural study of intervertebral discs from normal subjects and patients with scoliosis.. To identify ultrastructural relations among keratan sulfate (KS) proteoglycan, alpha-elastin, collagen fibers, and elastic fibers in normal and scoliotic discs.. KS proteoglycans, elastic fibers, and collagen fibers play important mechanical roles in the intervertebral disc, but the distributions of KS proteoglycans and elastin in this tissue have received little attention.. Tissues were fixed in 4% paraformaldehyde. Monoclonal antibody 5-D-4 (which recognizes a KS epitope on aggrecan, fibromodulin, and lumican) and polyclonal anti-alpha-elastin were visualized with a 10-nm immunogold-conjugated secondary antibody.. In a normal disc, a regular pattern of KS labeling occurred around collagen fibers, in the cell cytoplasm, and in the rough endoplasmic reticulum; the nucleus pulposus was more densely labeled for KS than was the anulus fibrosus. In scoliotic disc anulus fibrosus, KS labeling was weak throughout the matrix and pericellularly but abundant in lysosomes and on electron-dense material in degenerate cells. Degenerate collagen fibers in scoliotic tissue bore less KS than did normal fibers. KS labeling of the microfibrillar region of elastic fibers was strong in normal disc but weak in scoliotic disc. Elastin labeling of elastic fibers was weaker in scoliotic than in normal tissue.. KS proteoglycans and elastic fibers are closely associated with the lamellar organization of the collagen fibers in a normal disc. In scoliosis, impaired regulation of collagen fibrillogenesis by lumican or fibromodulin may result in disruption of the lamellar structure. Topics: Adolescent; Adult; Chondroitin Sulfate Proteoglycans; Elastin; Female; Humans; Immunohistochemistry; Intervertebral Disc; Keratan Sulfate; Lumbar Vertebrae; Lumican; Male; Scoliosis | 2005 |
Genetic analysis of structural elastic fiber and collagen genes in familial adolescent idiopathic scoliosis.
Adolescent idiopathic scoliosis is a genetic disorder of unknown etiology. Scoliosis is a clinical feature of inherited connective-tissue disorders including Marfan syndrome. Mutations within the gene of FBN1 (fibrillin 15), a component of the extracellular matrix, are now linked to Marfan syndrome and similar clinical phenotypes. This study investigated the potential association of structural genes encoding for extracellular matrix components of FBN1, elastin, and one of the polypeptides of type-I collagen (COL1A2) with familial adolescent idiopathic scoliosis. Eleven pedigrees, including 96 individuals, were identified in which adolescent idiopathic scoliosis segregated in an apparent autosomal dominant pattern. Fifty-two individuals were determined to be affected with scoliosis. Genomic DNA was analyzed by genetic linkage utilizing four intragenic markers for the structural genes of FBN1, elastin, and COL1A2. Collectively, our results exclude the structural genes of FBN1, elastin, and COL1A2 as candidate genes within these families. However, when viewed individually, specific markers cannot be excluded within all of the families. This information complements previously reported data that fibrillin production and matrix incorporation from scoliotic fibroblasts in vitro are normal in more than 80% of patients studied. Topics: Adolescent; Collagen; Elastic Tissue; Elastin; Female; Fibronectins; Genes; Genotype; Humans; Lod Score; Male; Pedigree; Scoliosis | 1996 |
Clinical, ultrastructural and biochemical studies in two sibs with Ehlers-Danlos syndrome type VI-B-like features.
Two Turkish sibs with clinical features of Ehlers-Danlos syndrome type VI-B are presented. The hydroxylysine contents of dermis and gel electrophoresis of type I and type III collagen produced by fibroblasts were normal. Ultrastructural studies of skin collagen and elastic fibers showed discrete abnormalities. Other syndromes with similar clinical, biochemical and ultrastructural features are discussed. Topics: Child, Preschool; Collagen; Diagnosis, Differential; Ehlers-Danlos Syndrome; Elastin; Eye Abnormalities; Female; Fibroblasts; Humans; Hydroxylysine; Infant; Joint Instability; Male; Pedigree; Sclera; Scoliosis; Skin | 1994 |
The potential role of the elastic fiber system in adolescent idiopathic scoliosis.
To assess its possible role in the etiology of adolescent idiopathic scoliosis, the elastic fiber system of the ligamentum flavum was examined in twenty-three patients who had scoliosis and in five age-matched individuals who did not. Elastic fibers are composed of two components: the amorphous core of elastin and microfibrils, of which fibrillin is the primary element. Fresh-frozen histological specimens of ligamentum flavum removed at the time of an operation were examined by Verhoeff staining for elastic fibers and by immunohistochemical staining with use of a monoclonal antibody to fibrillin. Additionally, cultures of fibroblast cells from the ligamentum flavum were used to study the biosynthesis and secretion of fibrillin and its incorporation into the extracellular matrix in vitro. The specimens from one patient did not provide sufficient material for the histological studies; however, fibroblasts were harvested from this specimen. In five (23 percent) of the remaining twenty-two specimens from patients who had adolescent idiopathic scoliosis, Verhoeff staining of elastic fibers showed a marked decrease in fiber density (the number of fibers per unit area) and a non-uniform distribution of fibers throughout the ligament. Eighteen specimens (82 percent) exhibited abnormalities on immunohistochemical staining, including a marked disarrangement of the fibers and a difference in the density of staining, when compared with the control specimens from individuals who did not have adolescent idiopathic scoliosis. Studies of the biosynthesis and secretion of fibrillin and its incorporation into the extracellular matrix in vitro demonstrated that fibroblasts from four (17 percent) of the twenty-three specimens produced normal amounts of fibrillin and secreted it from the cell, but the fibrillin failed to bind to other macromolecules, to form a sedimentable complex, and to incorporate into the extracellular matrix. Collectively, the results suggest the potential role of the elastic fiber system as a component in the pathogenesis of adolescent idiopathic scoliosis in some individuals. Topics: Adolescent; Adult; Child; Culture Techniques; Elastin; Extracellular Matrix; Female; Fibrillins; Fibroblasts; Humans; Immunohistochemistry; Ligamentum Flavum; Male; Microfilament Proteins; Scoliosis | 1994 |
Characterisation of collagen from normal and scoliotic human spinal ligament.
Acid-soluble and pepsin-soluble collagens have been isolated from spinal ligaments of normal and scoliotic individuals. Polyacrylamide gel electrophoresis of native and cyanogen bromide-treated collagens, and amino acid analysis, showed that the ligament collagen is almost all of the Type I variety with only trace amounts of Type III present. There was no evidence for abnormal ratios of collagen alpha-chains, or underhydroxylation of proline and lysine in the scoliotic ligament. These results indicate that collagen biochemistry is normal with respect to type, post-translational modification and cross-linking in spinal ligaments of patients with idiopathic scoliosis. Elastin and proteoglycan were only minor components of the ligaments. The nature of the non-collagenous part of the ligament is unknown, although it contains some proteins with a hydrophobic nature. Topics: Amino Acids; Animals; Collagen; Cyanogen Bromide; Elastin; Electrophoresis, Polyacrylamide Gel; Hexuronic Acids; Humans; Pepsin A; Rats; Scoliosis; Spinal Cord | 1983 |