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Vol. 123 No. 10, October 1988 |
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PAPERS READ BEFORE THE 14TH ANNUAL MEETING OF THE NEW ENGLAND SOCIETY FOR VASCULAR SURGERY, BRETTON WOODS, NH, SEPT 10 TO SEPT 11, 1987 |
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Molecular Diversity in the Abdominal Aortic Aneurysm Phenotype
M. David Tilson, MD;
Michael P. Roberts, MS
Arch Surg. 1988;123(10):1202-1206.
Abstract
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Abnormalities of collagenous peptides were detected among a group of 20 patients with abdominal aortic aneurysms, studied by high-performance liquid chromatography/NaDodSO4-PAGE (sodium dodecyl sulfate-polyacrylamide gel electrophoresis) analysis of the cyanogen bromide (CB) cleavage products of insoluble skin protein. Three abnormal patterns were identified as follows: (1) relative deficiency of a peptide with a relative molecular mass of approximately 58 kilodaltons (four patients); (2) relative decrease in the ratio of -2 to -1 (I) CB peptides (seven patients); and (3) decreased detection of all collagenous CB and pepsin cleavage products (one patient, who was also heterozygous for the Z allele of 1-antitrypsin). The "minimal hypothesis" to explain these findings is that most of the observed abnormalities can be explained by collagenolysis in vitro, although a mutation in the primary structure of collagen has not been ruled out in all patients. Molecular heterogeneity appears to occur within the aneurysm phenotype, and the findings in the patient in group 3 allow identification of one possible risk factor in abdominal aortic aneurysmal disease that has a genomic assignment.
(Arch Surg 1988;123:1202-1206)
Author Affiliations
From the Departments of Surgery (Dr Tilson) and Biology (Mr Roberts), Yale University, New Haven, Conn.
Footnotes
Accepted for publication Dec 30, 1987.
Read before the 14th Annual Meeting of the New England Society for Vascular Surgery, Bretton Woods, NH, Sept 11, 1987.
Reprint requests to Department of Surgery, Yale University School of Medicine, 333 Cedar St, New Haven, CT 06510 (Dr Tilson).
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