Abstract
Atomic force microscopy was employed to study ex vivo amyloid material isolated from the transplanted hearts of two patients affected by systemic amyloidosis caused by the Leu174Ser apolipoprotein A-I variant. The purified material consists of fibrils and globular aggregates. For both patients the same morphological patterns are observed; in addition, fibril diameters obtained for the two patients turn out to be compatible, both in air (2.00±0.02 and 2.04±0.04 nm) and under liquid (10.7±0.4 and 11.3±0.5 nm). Fibrils display heterogeneous morphologies, occasionally showing a left-handed twist. Inspection of fibril ends, the study of fibril contour shape and the analysis of partially unfolded fibrils yield independent evidences suggesting that most twisted fibrils are composed of three protofilaments. The size of globular aggregates is the same for both patients (4.4±0.4 and 5.1±0.5 nm, measured under liquid) and is compatible with the protofilament expected diameter, suggesting that globules may represent protofilament precursors.
| Original language | English |
|---|---|
| Pages (from-to) | 33-41 |
| Number of pages | 9 |
| Journal | Biochimica et Biophysica Acta - Molecular Basis of Disease |
| Volume | 1690 |
| Issue number | 1 |
| DOIs | |
| Publication status | Published - Sep 6 2004 |
Fingerprint
Keywords
- Amyloid
- Apolipoprotein A-I
- Atomic force microscopy
ASJC Scopus subject areas
- Molecular Biology
- Molecular Medicine
- Biophysics
Cite this
Ultrastructural organization of ex vivo amyloid fibrils formed by the apolipoprotein A-I Leu174Ser variant : An atomic force microscopy study. / Relini, Annalisa; Rolandi, Ranieri; Bolognesi, Martino; Aboudan, Manuela; Merlini, Giampaolo; Bellotti, Vittorio; Gliozzi, Alessandra.
In: Biochimica et Biophysica Acta - Molecular Basis of Disease, Vol. 1690, No. 1, 06.09.2004, p. 33-41.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Ultrastructural organization of ex vivo amyloid fibrils formed by the apolipoprotein A-I Leu174Ser variant
T2 - An atomic force microscopy study
AU - Relini, Annalisa
AU - Rolandi, Ranieri
AU - Bolognesi, Martino
AU - Aboudan, Manuela
AU - Merlini, Giampaolo
AU - Bellotti, Vittorio
AU - Gliozzi, Alessandra
PY - 2004/9/6
Y1 - 2004/9/6
N2 - Atomic force microscopy was employed to study ex vivo amyloid material isolated from the transplanted hearts of two patients affected by systemic amyloidosis caused by the Leu174Ser apolipoprotein A-I variant. The purified material consists of fibrils and globular aggregates. For both patients the same morphological patterns are observed; in addition, fibril diameters obtained for the two patients turn out to be compatible, both in air (2.00±0.02 and 2.04±0.04 nm) and under liquid (10.7±0.4 and 11.3±0.5 nm). Fibrils display heterogeneous morphologies, occasionally showing a left-handed twist. Inspection of fibril ends, the study of fibril contour shape and the analysis of partially unfolded fibrils yield independent evidences suggesting that most twisted fibrils are composed of three protofilaments. The size of globular aggregates is the same for both patients (4.4±0.4 and 5.1±0.5 nm, measured under liquid) and is compatible with the protofilament expected diameter, suggesting that globules may represent protofilament precursors.
AB - Atomic force microscopy was employed to study ex vivo amyloid material isolated from the transplanted hearts of two patients affected by systemic amyloidosis caused by the Leu174Ser apolipoprotein A-I variant. The purified material consists of fibrils and globular aggregates. For both patients the same morphological patterns are observed; in addition, fibril diameters obtained for the two patients turn out to be compatible, both in air (2.00±0.02 and 2.04±0.04 nm) and under liquid (10.7±0.4 and 11.3±0.5 nm). Fibrils display heterogeneous morphologies, occasionally showing a left-handed twist. Inspection of fibril ends, the study of fibril contour shape and the analysis of partially unfolded fibrils yield independent evidences suggesting that most twisted fibrils are composed of three protofilaments. The size of globular aggregates is the same for both patients (4.4±0.4 and 5.1±0.5 nm, measured under liquid) and is compatible with the protofilament expected diameter, suggesting that globules may represent protofilament precursors.
KW - Amyloid
KW - Apolipoprotein A-I
KW - Atomic force microscopy
UR - http://www.scopus.com/inward/record.url?scp=4344678675&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=4344678675&partnerID=8YFLogxK
U2 - 10.1016/j.bbadis.2004.04.007
DO - 10.1016/j.bbadis.2004.04.007
M3 - Article
C2 - 15337168
AN - SCOPUS:4344678675
VL - 1690
SP - 33
EP - 41
JO - Biochimica et Biophysica Acta - Molecular Basis of Disease
JF - Biochimica et Biophysica Acta - Molecular Basis of Disease
SN - 0925-4439
IS - 1
ER -