| 1. |
- Granfeldt, Hans, et al.
(författare)
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Experience with the Impella (R) recovery axial-flow system for acute heart failure at three cardiothoracic centers in Sweden
- 2009
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Ingår i: Scandinavian Cardiovascular Journal. - : Informa UK Limited. - 1401-7431 .- 1651-2006. ; 43:4, s. 233-239
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Tidskriftsartikel (refereegranskat)abstract
- Objectives. The Impella (R) recovery axial-flow system is a mechanical assist system for use in acute heart failure. This retrospective study reports the use of the device at three cardiothoracic units in Sweden. Design. Fifty patients (35 men, mean age 55.8 years, range 26 to 84 years) underwent implantation of 26 Impella (R) LP 2.5/5.0 (support-time 0.1 to 14 days), 16 Impella (R) LD (support-time 1 to 7 days) and 8 Impella (R) RD (support-time 0.1 to 8 days) between 2003 and 2007. Implantation was performed because of postcardiotomy heart failure (surgical group, n=33) or for various states of heart failure in cardiological patients (non-surgical group, n=17). The intention for the treatments was mainly to use the pump as a obridge-to-recoveryo. Results. Early mortality in the surgical and non-surgical groups was 45% and 23%, respectively. Complications included infection, 36% and right ventricular failure, 28%. Cardiac output and cardiac power output postoperatively were significantly higher among survivors than non-survivors. Conclusions. The Impella (R) recovery axial-flow system facilitates treatment in acute heart failure. Early intervention in patients with acute heart failure and optimized hemodynamics in the post-implantation period seem to be of importance for long-term survival. Insufficient early response to therapy should urge to consider further treatment options.
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| 2. |
- Larsson, Annika, et al.
(författare)
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Lactadherin binds to elastin -a starting point for medin amyloid formation?
- 2006
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Ingår i: Amyloid. - : Informa UK Limited. - 1350-6129 .- 1744-2818. ; 13:2, s. 78-85
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Tidskriftsartikel (refereegranskat)abstract
- Medin amyloid is found in the medial layer of the aorta in almost 100% of the Caucasian population over 50 years of age. The medin fragment is 5.5 kDa and derives from the C2-like domain of the precursor protein lactadherin. We have previously reported immunohistochemical findings showing that medin amyloid co-localizes with elastic fibers of arteries and herein we show that lactadherin also is associated with elastic structures of human aortic material. In addition, results from in vitro binding assays demonstrate that both medin and lactadherin bind to tropoelastin in a concentration-dependent fashion, suggesting that the lactadherin-tropoelastin interaction is mediated via the medin domain. It is possible that lactadherin, which is a cell adhesion protein, in this way connects smooth muscle cells to the elastic fibers of arteries. Given that both medin and lactadherin interact with elastic fibers, elastin is probably an important component in the formation of medin amyloid.
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| 3. |
- Peng, Siwei, et al.
(författare)
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Role of aggregated medin in the pathogenesis of thoracic aortic aneurysm and dissection
- 2007
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Ingår i: Laboratory Investigation. - : Elsevier BV. - 0023-6837 .- 1530-0307. ; 87:12, s. 1195-1205
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Tidskriftsartikel (refereegranskat)abstract
- 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 mm2, 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.
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