Elastin in Diseases

Uitto, Jouni; Ryhänen, Lasse; Abraham, Pathrapankal A.; Perejda, Andrea J.

doi:10.1038/jid.1982.29

Cited by 38 publications

(15 citation statements)

References 46 publications

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“…With aging there was a decreased collagen content in the fascias, as well as decreased extractability of collagen with pepsin (Pans et al 17 ). This is in accordance with the data of the literature reported for skin (Uitto et al 18 ) and our previous data for the diaphragm (Rodrigues et al 13 ). …”

Section: Discussionsupporting

confidence: 94%

Quantitative analysis of collagen and elastic fibers in the transversalis fascia in direct and indirect inguinal hernia

Rodrigues

Cunha

et al. 2002

Rev. Hosp. Clin.

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PURPOSE:Our previous studies demonstrated structural and quantitative age-related changes of the elastic fibers in transversalis fascia, which may play a role in inguinal hernia formation. To verify whether there were differences in the extracellular matrix between direct and indirect inguinal hernia, we studied the amount of collagen and elastic fibers in the transversalis fascia of 36 male patients with indirect inguinal hernia and 21 with direct inguinal hernia. MATERIAL AND METHODS:Transversalis fascia fragments were obtained during surgical intervention and underwent histological quantitative analysis of collagen by colorimetry and analysis of elastic fibers by histomorphometry. RESULTS:We demonstrated significantly lower amounts of collagen and higher amounts of elastic fibers in transversalis fascia from patients with direct inguinal hernia compared to indirect inguinal hernia patients. The transversalis fascia from direct inguinal hernia patients showed structural changes of the mature and elaunin elastic fibers, which are responsible for elasticity, and lower density of oxytalan elastic fibers, which are responsible for resistance. These changes promoted loss of resiliency of the transversalis fascia.CONCLUSION: These results improve our understanding of the participation of the extracellular matrix in the genesis of direct inguinal hernia, suggesting a relationship with genetic defects of the elastic fiber and collagen synthesis. DESCRIPTORS: Inguinal hernia. Transversalis fascia. Elastin. Collagen. Extracellular matrix.

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Section: Discussionsupporting

confidence: 94%

Quantitative analysis of collagen and elastic fibers in the transversalis fascia in direct and indirect inguinal hernia

Rodrigues

Cunha

et al. 2002

Rev. Hosp. Clin.

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“…The microfibrillar component is mostly composed of fibrillin and microfibril-associated glycoprotein. 14 The ELN gene is a single-copy gene of 34 exons localized in humans at 7q11.2. Its product, tropoelastin, is a 72-kDa polypeptide with a primary structure of alternating hydrophobic and lysine-rich sequences.…”

Section: Commentmentioning

confidence: 99%

A Novel Elastin Gene Mutation Resulting in an Autosomal Dominant Form of Cutis Laxa

Rodríguez‐Revenga¹,

Iranzo²,

Badenas³

et al. 2004

Arch Dermatol

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Background: Cutis laxa is an extremely rare disorder characterized by marked skin laxity. Few cases of cutis laxa have been described worldwide. Clinical presentation and mode of inheritance show considerable heterogeneity; autosomal dominant, autosomal recessive, and X-linked recessive forms have been reported. Only 3 mutations in the elastin gene have been described as the genetic cause of the autosomal dominant form of cutis laxa.Observations: A 45-year-old woman and her 19-yearold son presented with inelastic, loose-hanging, and wrinkled skin that appeared prematurely aged and were clinically diagnosed as having cutis laxa. Mutational analy-sis of the elastin gene evidenced a novel mutation (2292delC) that predicts a frameshift in the coding region and causes translation to proceed into the 3Јuntranslated region. This would replace the C-terminal amino acid of the normal elastin protein with a novel sequence. Conclusion:This article is the fourth report of autosomal dominant cutis laxa to appear in the literature in which a mutation in the elastin gene has been correlated with the disease.

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“…E lastic fibers are the principal components of connective tissue that impart resilience and elasticity to the skin. [1][2][3][4][5] Mature elastic fibers in the reticular dermis are composed of microfibrils (15% by weight, containing fibrillins and microfibrilassociated glycoproteins) that surround a core of amorphous elastin (85% by weight, a single polypeptide chain of 800 amino acids); the immature fibers seen in children have a higher percentage of microfibrils (50% by weight). 6 By 30 years of age, the concentration of microfibrils has dropped significantly; by age 60, elastic fibers are predominantly elastin.…”

mentioning

confidence: 99%

Acquired disorders of elastic tissue: part I. increased elastic tissue and solar elastotic syndromes

Lewis

Bercovitch

Dill

et al. 2004

Journal of the American Academy of Dermatology

171

178

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Elastin in Diseases

Cited by 38 publications

References 46 publications

Quantitative analysis of collagen and elastic fibers in the transversalis fascia in direct and indirect inguinal hernia

Quantitative analysis of collagen and elastic fibers in the transversalis fascia in direct and indirect inguinal hernia

A Novel Elastin Gene Mutation Resulting in an Autosomal Dominant Form of Cutis Laxa

Acquired disorders of elastic tissue: part I. increased elastic tissue and solar elastotic syndromes

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