scholarly journals Soluble EMMPRIN levels discriminate aortic ectasia in Marfan syndrome patients

Theranostics ◽  
2019 ◽  
Vol 9 (8) ◽  
pp. 2224-2234 ◽  
Author(s):  
Erica Rurali ◽  
Gianluca L. Perrucci ◽  
Raffaella Gaetano ◽  
Alessandro Pini ◽  
Donato Moschetta ◽  
...  
Keyword(s):  
Marfan Syndrome ◽  
Aortic Ectasia

scholarly journals The borohydride-reducible compounds of human aortic elastin. Demonstration of a new cyclic amino acid in alkali hydrolysate, and changes with age and in patients with annulo-aortic ectasia including one with Marfan syndrome

1985 ◽  
Vol 232 (1) ◽  
pp. 169-175 ◽  
Author(s):  
T Halme ◽  
M Jutila ◽  
T Vihersaari ◽  
P Oksman ◽  
N D Light ◽  
...  
Keyword(s):  
Acid Hydrolysis ◽  
Marfan Syndrome ◽  
Aldol Condensation ◽  
Condensation Product ◽  
Hydrolysis Product ◽  
Exchange Chromatography ◽  
Spectrometric Analysis ◽  
Cross Link ◽  
Aortic Ectasia ◽  
And Control

Human aortic elastin reduced with [3H]borohydride was analysed by ion-exchange chromatography after alkali or acid hydrolysis. Alkali hydrolysates of elastins contained a radioactive peak that was eluted between proline and leucine. This peak was not present in foetal elastin, but its proportion increased steadily during aging. Aortic samples from patients with annulo-aortic ectasia (aneurysm of the ascending aorta), including one with classical Marfan syndrome, contained less elastin (CNBr-insoluble material) than did the age-matched controls. The proportion of radioactivity in the new peak of all these aortas was low when compared with age-matched controls. Gas-chromatographic/mass-spectrometric analysis suggested that it contained a cyclic derivative of a hydrated aldol-condensation product. The concentration of the cross-link precursors, lysine aldehyde and aldol-condensation product (estimated from the acid-hydrolysis product 6-chloronorleucine and the acid-degradation product of reduced aldol-condensation product) was high in very young aortas but remained quite stable after childhood. No differences were observed in cross-link profiles of acid hydrolysates between pathological and control aortas. A low proportion of radioactivity in the new peak may indicate the presence of young or immature elastin in the pathological aortas.

Annulo-aortic ectasia — with special reference to total repair of patients with Marfan syndrome

1995 ◽  
pp. 83-89
Author(s):  
M. V. Inberg ◽  
J. Niinikoski ◽  
V. Rantakokko ◽  
T. Savunen ◽  
E. Vänttinen
Keyword(s):  
Special Reference ◽  
Marfan Syndrome ◽  
Aortic Ectasia

P5487Thoracic aortic ectasia in Marfan syndrome patients is discriminated by soluble EMMPRIN levels

2018 ◽  
Vol 39 (suppl_1) ◽  
Author(s):  
E Rurali ◽  
G L Perrucci ◽  
R Gaetano ◽  
A Pini ◽  
D Moschetta ◽  
...  
Keyword(s):  
Marfan Syndrome ◽  
Aortic Ectasia

Two stage radical surgery for type I dissecting aneurysm with annulo-aortic ectasia (AAE) in Marfan syndrome

1995 ◽  
Vol 3 ◽  
pp. 144-144
Author(s):  
K KOJA ◽  
Y KUSABA ◽  
Y KUNIYOSHI ◽  
K IHA ◽  
M AKASAKI ◽  
...  
Keyword(s):  
Marfan Syndrome ◽  
Radical Surgery ◽  
Dissecting Aneurysm ◽  
Type I ◽  
Two Stage ◽  
Aortic Ectasia

Banded aggregates containing fibrillin are present in the cartilage matrix adjacent to chondrocytes in individuals affected with scoliosis

1992 ◽  
Vol 50 (1) ◽  
pp. 892-893
Author(s):  
Douglas R. Keene ◽  
Magaret Fairhurst ◽  
Catherine C. Ridgway ◽  
Lynn Y. Sakai
Keyword(s):  
Connective Tissue ◽  
Marfan Syndrome ◽  
Cross Section ◽  
Immunoelectron Microscopy ◽  
Cartilage Matrix ◽  
Negative Stain ◽  
Gene Coding ◽  
Rotary Shadowing

Matrix microfibrils are present in the connective tissue matrices of all tissues. Following standard TEM processing, they appear in cross section as cylindrical fibrils 8-10 nm in diameter, often associated with amorphous elastin. They are also seen in the absence of amorphous elastin, for example in the shallow papillary layer of skin, and also in cartilage matrix (Figure 1). Negative stain and rotary shadowing studies suggest that microfibrils are composed of laterally associated globular structures connected by fine filamentous strands (“ beaded strings”), and that they are extendable. Immunoelectron microscopy has demonstrated that fibrillin, a 350 Kd glycoprotein, is distributed along all microfibrils with a relaxed periodicity of about 54 nm The gene coding for fibrillin has recently been identified and is defective in the Marfan syndrome.

Marfan Syndrome Update

2011 ◽  
Vol 44 (8) ◽  
pp. 54-55
Author(s):  
HOWARD P. LEVY
Keyword(s):  
Marfan Syndrome
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