Segmental Absence of Intestinal Musculature in a Child with Type IV Ehlers–Danlos Syndrome

Patients with vascular Ehlers–Danlos syndrome (vEDS) have a defect in the formation of type III collagen. This defect puts patients at risk of vascular rupture, uterine rupture, and bowel perforations. The segmental absence of intestinal musculature is a rare histopathologic finding, wherein there is a lack of a muscularis propria layer in the intestinal wall. Although typically documented in the literature in neonates or adults, it can be seen in children of other ages. This is a case report of a patient who exhibits both rare entities, which has not been described in the literature to date.

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Multiple Vascular and Bowel Ruptures in an Adolescent Male with Sporadic Ehlers-Danlos Syndrome Type IV

Pediatric and Developmental Pathology ◽

10.1007/s100249900095 ◽

1999 ◽

Vol 2 (1) ◽

pp. 86-93 ◽

Cited By ~ 19

Author(s):

Margaret H. Collins ◽

Ulrike Schwarze ◽

David F. Carpentieri ◽

Paige Kaplan ◽

Katherine Nathanson ◽

...

Keyword(s):

Clinical Manifestations ◽

Muscularis Propria ◽

Adolescent Male ◽

Type Iii Collagen ◽

Elastic Tissue ◽

Ehlers Danlos Syndrome ◽

Type Iii ◽

Type Iv ◽

Col3a1 Gene ◽

Danlos Syndrome

Ehlers-Danlos syndrome (EDS) type IV is a heritable disorder resulting from mutations in the COL3A1 gene that cause deficient production of type III collagen. Clinical manifestations of EDS type IV include hypermobility of small joints, excessive bruisability, thin translucent skin, poor wound healing, bowel rupture, and vascular rupture that is often fatal. A 14-year-old male without a family history of EDS died following multiple bowel and abdominal blood vessel ruptures. Even in areas apart from rupture sites, the bowel wall was thin because of diminished submucosa and muscularis propria. Similarly, the walls of blood vessels in bowel submucosa and elsewhere in the abdomen varied in thickness, and contained frayed and fragmented elastic tissue fibers. Fibroblasts cultured from the patient's skin secreted reduced quantities of type III collagen that was explained by a point mutation in one copy of the COL3A1 gene. EDS type IV should be strongly suspected in any patient with otherwise unexplainable bowel and/or vessel rupture.

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A single base mutation in the gene for type III collagen (COL3A1) converts glycine 847 to glutamic acid in a family with Ehlers-Danlos syndrome type IV. An unaffected family member is mosaic for the mutation

Human Genetics ◽

10.1007/bf00194313 ◽

1992 ◽

Vol 89 (4) ◽

Cited By ~ 22

Author(s):

A.J. Richards ◽

P.N. Ward ◽

P. Narcisi ◽

A.C. Nicholls ◽

J.C. Lloyd ◽

...

Keyword(s):

Glutamic Acid ◽

Family Member ◽

Type Iii Collagen ◽

Syndrome Type ◽

Unaffected Family Member ◽

Ehlers Danlos Syndrome ◽

Single Base ◽

Type Iii ◽

Type Iv ◽

Danlos Syndrome

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Percutaneous Embolization of an Inferior Mesenteric Artery Aneurysm in a Patient With Type IV Ehlers-Danlos Syndrome

Vascular and Endovascular Surgery ◽

10.1177/1538574418824185 ◽

2019 ◽

Vol 53 (4) ◽

pp. 343-347 ◽

Cited By ~ 1

Author(s):

Qasim Rahman ◽

Sailen G. Naidu ◽

Brian W. Chong ◽

William M. Stone

Keyword(s):

Mesenteric Artery ◽

Inferior Mesenteric Artery ◽

Artery Aneurysm ◽

Aortic Aneurysms ◽

Type Iii Collagen ◽

Cyanoacrylate Glue ◽

Ehlers Danlos Syndrome ◽

Percutaneous Embolization ◽

Type Iv ◽

Danlos Syndrome

Ehlers-Danlos syndrome (EDS) refers to a group of genetic disorders involving the connective tissues. Type IV EDS impairs type III collagen that is responsible for vessel integrity. Patients with type IV EDS are susceptible to vascular and visceral complications, including aortic aneurysms, pseudoaneurysms, dissections, and spontaneous rupture of internal organs. Treating aneurysms with open surgery versus endovascular techniques each carry a unique risk-to-benefit ratio that must be applied to each individual carefully. We present a patient with type IV EDS who presented with a rapidly growing inferior mesenteric artery aneurysm. The patient was treated with a percutaneous endovascular technique using coils and n-butyl-cyanoacrylate glue.

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Abnormal type III collagen produced by an exon-17-skipping mutation of the COL3A1 gene in Ehlers-Danlos syndrome type IV is not incorporated into the extracellular matrix

Biochemical Journal ◽

10.1042/bj3110939 ◽

1995 ◽

Vol 311 (3) ◽

pp. 939-943 ◽

Cited By ~ 5

Author(s):

A A Chiodo ◽

D O Sillence ◽

W G Cole ◽

J F Bateman

Keyword(s):

Extracellular Matrix ◽

Triple Helix ◽

Type Iii Collagen ◽

Syndrome Type ◽

Ehlers Danlos Syndrome ◽

Type Iii ◽

Type Iv ◽

Col3a1 Gene ◽

Collagen Molecules ◽

Danlos Syndrome

A novel heterozygous mutation of the COL3A1 gene that encodes the alpha 1(III) chains of type III collagen was identified in a family with the acrogeric form of Ehlers-Danlos syndrome type IV (EDS-IV). Cultured dermal fibroblasts produced normal and shortened alpha 1(III) chains. The triple helix of the latter chain was shortened owing to a 33 amino acid deletion of Gly-184 to Pro-216. The corresponding region of cDNA lacked 99 base pairs from nucleotides 1051 to 1149. The deletions corresponded exactly to the normal sequence encoded by exon 17 of the COL3A1 gene. The proband was heterozygous for a T to G transversion at position +2 of intron 17, which resulted in skipping of exon 17. The splicing defect was not corrected by growing the fibroblasts at 33 degrees C and no other splicing variants were identified at 33 or 37 degrees C. The affected brother had the same mutation but his unaffected mother did not. Heterotrimeric type III collagen molecules containing normal and mutant chains were retained within the cell. The mutant homotrimeric molecules were modified and secreted normally and were thermally stable. These normal characteristics of the mutant homotrimers suggested that the loss of ten Gly-Xaa-Yaa triplets (where Gly-Xaa-Yaa is a repetitive amino acid triplet structure in which Xaa and Yaa are other amino acids, proline and hydroxyproline being more common in the Yaa position) did not adversely affect the formation and stability of the triple helix or the structural requirements for secretion. However, the mutant homotrimers were not incorporated into the extracellular matrix of an in vitro model of EDS-IV dermis. The EDS-IV phenotype in this family was probably due to a deficiency in the amount of normal type III collagen available for formation of the heterotypic collagen fibrils of the extracellular matrix. Intracellular and extracellular quality-control mechanisms prevented the incorporation of heterotrimeric and homotrimeric mutant type III collagen molecules into the cross-linked extracellular matrix.

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