Cutis laxa. Ultrastructural and biochemical studies

Hashimoto, Ken

doi:10.1001/archderm.111.7.861

Cited by 53 publications

(39 citation statements)

References 9 publications

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“…There are some previous descriptions of electrondense bundles in elastic fibers (Ross et al 1969;Varadi 1972;Hashimoto et al 1975). Some workers interpret the electron-dense bundles as dark-staining microfibrils (Ross et al 1969;Varadi 1972).…”

Section: Discussionmentioning

confidence: 99%

Ultrastructural Distribution of 36-kD Microfibril-associated Glycoprotein (MAGP-36) in Human and Bovine Tissues

Toyoshima

Yamashita

Furuichi

et al. 1999

J Histochem Cytochem.

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SUMMARYWe observed the ultrastructural distribution of MAGP-36 by immunoelectron microscopy in human and bovine tissues. MAGP-36 was present in microfibrils associated with tropoelastin in skin, aorta, and spleen. It was not detected in microfibrils from the ocular zonule and kidney mesangium that were not associated with tropoelastin. In skin, MAGP-36 was present in both early immature elastic fibers and mature elastic fibers. In mature elastic fibers, MAGP-36 was localized around amorphous elastic cores at the elastinmicrofibril interface and in electron-dense bundles. Localization of MAGP-36 in elastic fibers coincided with the distribution of lysyl oxidase, an enzyme that plays a pivotal role in the deposition of tropoelastin. These findings suggest that MAGP-36 may be involved in elastogenesis.

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Section: Discussionmentioning

confidence: 99%

Ultrastructural Distribution of 36-kD Microfibril-associated Glycoprotein (MAGP-36) in Human and Bovine Tissues

Toyoshima

Yamashita

Furuichi

et al. 1999

J Histochem Cytochem.

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“…1,5,6 A highly variable spectrum of associated features 7 -11 has been reported. The skin histology characteristically demonstrates abnormal elastic fiber structure with a significantly decreased amount of elastin.…”

Section: Introductionmentioning

confidence: 99%

“…The skin histology characteristically demonstrates abnormal elastic fiber structure with a significantly decreased amount of elastin. 5,6,12 The most common forms are inherited in an autosomal recessive or dominant fashion (MIM 219200, MIM 219100, MIM 123700, MIM 150240). Two distinct clinical types of autosomal recessive cutis laxa (ARCL) have been described in detail.…”

Section: Introductionmentioning

confidence: 99%

Defective protein glycosylation in patients with cutis laxa syndrome

et al. 2005

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Congenital cutis laxa is a genetically heterogeneous condition presenting with loose and redundant skin folds, decreased elasticity of the skin, connective tissue involvement and a highly variable spectrum of associated features. The most common forms are inherited in an autosomal recessive or dominant fashion. Fibulin 5 and elastin mutations were detected in a limited number of patients, but in most cases the etiology is not known. Based on a previous observation of an abnormal transferrin isoelectric focusing pattern in a patient with cutis laxa indicating an N-glycosylation defect, we performed a screening for disorders of protein glycosylation in unrelated children with cutis laxa syndrome, including a recently developed test for defective O-glycosylation. Here, we describe five patients from consanguineous marriages with a cutis laxa syndrome with skeletal and joint involvement, developmental delay and neurological findings. Three of these five children have an inborn error of glycan biosynthesis affecting the synthesis of both N-and O-linked glycans. Two patients had normal glycosylation patterns. All known causes of secondary glycosylation disorders were excluded in the children. No mutations were found in the FBLN5 gene. In conclusion, we have identified a new combined glycosylation defect with a distinct clinical phenotype. Our results suggest that a combined defect of glycosylation might be a causative factor in congenital cutis laxa. This is the first report where abnormal N-and O-linked glycosylation is implicated in the etiology of cutis laxa syndrome.

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“…Investigations of the elastic fibers in cutis laxa have confirmed the morphological structural abnormalities. There is a reduction of elastic structures, and, in many cases, elastic fibers are fragmented [4, 5, 6]. Electron-microscopic examination of cutis laxa has shown a decrease in elastin expression, a structural component of elastic fibers, making microfibrils visible [4].…”

Section: Discussionmentioning

confidence: 99%

“…Loose skin is localized to the hands, feet and neck as opposed to generalized cutis laxa. In cutis laxa, morphological studies showed a reduction of elastic structures and fragmentation of elastic fibers [4, 5, 6]. Elastin mRNA levels are also reduced in several fibroblast strains of cutis laxa [7, 8, 9].…”

Section: Introductionmentioning

confidence: 99%

Costello Syndrome with Decreased Gene Expression of Elastin in Cultured Dermal Fibroblasts

et al. 2000

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We report a case of Costello syndrome. A 2-year-old Japanese boy presented with a ‘coarse‘ face, curly hair and loose skin of the dorsal aspect of the hands and feet with dark pigmentation. A skin biopsy of the dorsal aspect of the left hand revealed hyperkeratosis and papillomatosis of the epidermis, hyperpigmentation of the basal layer, and shortening and rupture of elastic fibers of the dermis. Electron microscopy of dermal elastic fibers showed a decreased amount of elastin with an exposed appearance of microfibrils. In Northern blot analysis of cultured dermal fibroblasts, elastin mRNA levels were reduced, suggesting a decrease in elastin production at the lesions of loose skin.

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Cutis laxa. Ultrastructural and biochemical studies

Cited by 53 publications

References 9 publications

Ultrastructural Distribution of 36-kD Microfibril-associated Glycoprotein (MAGP-36) in Human and Bovine Tissues

Ultrastructural Distribution of 36-kD Microfibril-associated Glycoprotein (MAGP-36) in Human and Bovine Tissues

Defective protein glycosylation in patients with cutis laxa syndrome

Costello Syndrome with Decreased Gene Expression of Elastin in Cultured Dermal Fibroblasts

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