The morphology of ascending aortic aneurysms

Klima, Tomas; Spjut, Harland J.; Coelho, Aldemir; Gray, Albert G.; Wukasch, Don C.; Reul, George J.; Cooley, Denton A.

doi:10.1016/s0046-8177(83)80303-7

Cited by 73 publications

(48 citation statements)

References 12 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Smooth muscle cells and a rich extracellular matrix, principally composed of collagen and elastin fibers, are the most important components of this layer. These proteins are directly implicated in the aneurismal development and are modified, structurally and quantitatively, during the advent of this aortic pathology [13][14][15].…”

Section: Resultsmentioning

confidence: 99%

FTIR protein secondary structure analysis of human ascending aortic tissues

Bonnier

Rubin

Debelle

et al. 2008

Journal of Biophotonics

View full text Add to dashboard Cite

Journal of BIOPHOTONICSThe advent of moderate dilatations in ascending aortas is often accompanied by structural modifications of the main components of the aortic tissue, elastin and collagen. In this study, we have undertaken an approach based on FTIR microscopy coupled to a curve-fitting procedure to analyze secondary structure modifications in these proteins in human normal and pathological aortic tissues. We found that the outcome of the aortic pathology is strongly influenced by these proteins, which are abundant in the media of the aortic wall, and that the advent of an aortic dilatation is generally accompanied by a decrease of parallel b-sheet structures. Elastin, essentially composed of b-sheet structures, seems to be directly related to these changes and therefore indicative of the elastic alteration of the aortic wall. Conventional microscopy and confocal fluorescence microscopy were used to compare FTIR microscopy results with the organization of the elastic fibers present in the tissues. This in-vitro study on 6 patients (three normal and three pathologic), suggests that such a spectroscopic marker, specific to aneurismal tissue characterization, could be important information for surgeons who face the dilemma of moderate aortic tissue dilatation of the ascending aortas.Infrared spectroscopy and imaging was applied to analyse Human thoracic ascending aortas with the aim to highlight the protein secondary structure reorganisation after an aneurism outcome. We used a curve-fitting procedure to visualise modifications in the protein spectral profile where alteration of b structures in pathological aortas could be detected. Our spectroscopic observations on tissue sections corroborated with confocal fluorescence microscopy clearly demonstrating that elastic fibres of aortic wall are strongly altered. Elastin appears as the privileged target during the pathological process.

show abstract

Section: Resultsmentioning

confidence: 99%

FTIR protein secondary structure analysis of human ascending aortic tissues

Bonnier

Rubin

Debelle

et al. 2008

Journal of Biophotonics

View full text Add to dashboard Cite

show abstract

“…Degeneration of elastic structures and extracellular deposits of glycosaminoglycan-rich material, the latter often referred to as cystic medial necrosis, are typical histopathologic findings. 1,2 Increased production or presence of certain matrix metalloproteinases (MMPs), particularly MMP-1, MMP-2 and MMP-9, has been found in both thoracic aortic aneurysms and dissections. [3][4][5][6] The resulting proteolysis leads to weakening of the aortic wall and appears to be a direct cause of the lesions.…”

mentioning

confidence: 99%

Role of aggregated medin in the pathogenesis of thoracic aortic aneurysm and dissection

Peng

Larsson

Wassberg

et al. 2007

Laboratory Investigation

View full text Add to dashboard Cite

The pathogenesis of sporadic thoracic aortic aneurysm and dissection, which may lead to rupture of the aorta, remains largely unknown. Amyloid deposits, formed from the medin peptide, are very prevalent in the media of the thoracic aorta. We have studied the occurrence of medin-derived amyloid in specimens from patients with thoracic aortic aneurysm, aortic dissection type A and normal dimensioned aorta. Surprisingly, the amount of amyloid was significantly lower in the aneurysm and dissection groups (0.63±0.13 and 0.36±0.24 amyloid particles per mm 2 , respectively) compared to the control material (2.37 ± 0.58). However, focal medin immunoreactivity not associated with amyloid was found more conspicuously in the media of the two diseased groups. Recent amyloid research indicates that prefibrillar oligomeric aggregates, rather than mature amyloid fibrils, are toxic to the surrounding cells. The non-amyloid medin immunoreactivity observed may represent such toxic oligomers. This is supported by the fact that aggregated medin induced death of aortic smooth muscle cells in vitro. In addition, cells incubated together with medin increased the production of matrix metalloproteinase-2, a protease that degrades elastin and collagen and subsequently weakens the vessel wall. We therefore propose that medin oligomers are involved in the degeneration process of sporadic thoracic aortic aneurysm and dissection.

show abstract

“…Причиной, по которой пациент, перенесший операцию по поводу острого расслоения ВА, появляется в поле зрения хирурга, является прогрессиро-вание дилатации Ао в различных сегментах и, как след-ствие, появление аортальной регургитации, развитие сер-дечной недостаточности, а также риск разрыва или рас-слоения, что обусловливает высокую частоту летальных исходов среди наблюдаемых пациентов [2,4,6]. В основе всего происходящего лежит «тканевая недостаточность» среднего слоя Ао [5], которая приводит к фатальному де-фекту целостности стенки Ао. В нашем случае мы встре-тили комплекс всех основных проблем у подобной катего-рии пациентов.…”

Section: Discussionunclassified