Multiple Defects in Type III Collagen Synthesis Are Associated with the Pathogenesis of Abdominal Aortic Aneurysms a

@article{Anderson1996MultipleDI,
  title={Multiple Defects in Type III Collagen Synthesis Are Associated with the Pathogenesis of Abdominal Aortic Aneurysms a},
  author={David W. Anderson and Troy K. Edwards and Michael H. Ricketts and Helena Kuivaniemi and Gerard Tromp and Catherine A. Stolle and Susan B. Deak and Charles D. Boyd},
  journal={Annals of the New York Academy of Sciences},
  year={1996},
  volume={800},
  url={https://api.semanticscholar.org/CorpusID:27075556}
}
It is clear from this study that aberrant synthesis oftype III collagen, as a consequence of both a coding sequence mutation and other factors contributing to reduced secretion of type III procollagen, will result in the development of an aortic aneurysm in a significant percentage of patients with this disease.
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40 Citations
Background Citations
11
Methods Citations
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Results Citations
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40 Citations

The role of type III collagen in family members of patients with abdominal aortic aneurysms.

Type III collagen deficiency does not appear to be an aetiological factor in the development of AAA, and type III collagen was normal in all family members.

Increased amount of type III pN-collagen in human abdominal aortic aneurysms: evidence for impaired type III collagen fibrillogenesis.

The results strongly suggest that the metabolism of type III collagen is enhanced in AAAs, suggesting that type I collagen synthesis is a fibroproliferative response related to the atherosclerotic process.

Type III collagen (COL3A1): Gene and protein structure, tissue distribution, and associated diseases.

Impaired balance of type I and type III procollagen mRNA in cultured fibroblasts of patients with incisional hernia.

The altered synthesis of type I and type III collagen in cultured skin fibroblasts suggests a disorder of collagen metabolism, at least in patients with recurrent hernia, possibly contributing to the unsatisfactory results of incisional hernia repair.

Characterization of type I and type III collagens in human tissues

The amount of type III pN-collagen was increased in malignant ovarian tumors, whereas no such tendency was seen in colon cancer, and a wide variety of changes in the metabolism of type I and III collagens in diseases are suggested.

Increased amount of type III pN-collagen in AAA when compared with AOD.

The larger amount oftype III pN-collagen suggests an alteration in the metabolism of type III collagen in AAAs, which may partially explain the decreased tensile strength of the aortic tissue.

Familial abdominal aortic aneurysm: a systematic review of a genetic background.

These studies give insight in the pathology but do not lead to the specific genetic factor(s) responsible for (familial) AAA.

Type I/type III collagen ratio associated with diverticulitis of the colon in young patients.

Decreased collagen ratio type I/III in association with hemorrhoidal disease

Quality of collagen formation in the corpus cavernosum recti in patients with hemorrhoids degree III and IV in comparison to persons without showed a significant disorder in collagen metabolism, and pathophysiological process of hemorrhoidal disease seems to be associated with this.

Abdominal Aortic Aneurysm Is a Specific Antigen‐Driven T Cell Disease

The results demonstrate that oligoclonal αβ T CR+ and γδ TCR+T cells are present in AAA lesions, and it appears that AAA is a specific antigen‐driven T cell disease.

17 References

Abnormalities in the biosynthesis of type III procollagen in cultured skin fibroblasts from two patients with multiple aneurysms.

A mutation in the gene for type III procollagen (COL3A1) in a family with aortic aneurysms.

Results demonstrated that mutations in the type III procollagen gene can cause familial aortic aneurysms and that DNA tests for such mutations can identify individuals at risk for aneurYSms.

Exclusion of mutations in the gene for type III collagen (COL3A1) as a common cause of intracranial aneurysms or cervical artery dissections

The results indicated that mutations in the gene for type III procollagen (COL3A1) are not a common cause of either intracranial artery aneurysms or cervical artery dissections.

Mutations in collagen genes: causes of rare and some common diseases in humans

The results suggest that mutations in procollagen genes may cause a wide spectrum of both rare and common human diseases.

Sequencing of cDNA from 50 unrelated patients reveals that mutations in the triple-helical domain of type III procollagen are an infrequent cause of aortic aneurysms.

Detailed DNA sequencing of the triple-helical domain of type III procollagen was carried out on cDNA prepared from 54 patients with aortic aneurysms, revealing only two nucleotide changes that altered the structure of the protein.

A Gly1127Ser mutation in an EGF-like domain of the fibrillin-1 gene is a risk factor for ascending aortic aneurysm and dissection.

The Gly1127Ser FBN1 mutation produces a mild form of autosomal dominantly inherited weakness of elastic tissue, which predisposes to ascending aortic aneurysm and dissection later in life.

Increases in Type III Collagen Gene Expression and Protein Synthesis in Patients with Inguinal Hernias

This study represents the first attempt to define individuals with an abnormality in collagen production that may be specifically related to herniation, and suggests a constitutive and systemic increase in type III collagen synthesis may result in reduced collagen fibril assembly in the abdominal wall, eventually leading to the development of hernia.

SOME PATIENTS WITH CEREBRAL ANEURYSMS ARE DEFICIENT IN TYPE III COLLAGEN

Familial tendency for abdominal aortic aneurysms.

It is suggested that the relatives of patients with AAA may themselves be at significantly increased risk for the development of aneurysmal degeneration, and noninvasive screening to detect early AAA formation may be warranted in relatives.

Structure of cDNA clones coding for the entire prepro alpha 1 (III) chain of human type III procollagen. Differences in protein structure from type I procollagen and conservation of codon preferences.

Two overlapping cDNA clones that cover the complete length of the mRNA for human type III procollagen and two tripeptide sequences of -Gly-Xaa-Yaa- were identified that were not detected previously by amino acid sequencing of humantype III collagen establish that the alpha 1 (III) chain is 15 amino acids longer than either thealpha 1 (I) or alpha 2 ( I) chains of type I collagen.