Publication

Morphological and primary structural consistency of fibrils from different AA patients (common variant)

Liberta, F., Rennegarbe, M., Roesler, R., Bijzet, J., Wiese, S., Hazenberg, B. P. C. & Fandrich, M., 24-Jun-2019, In : Amyloid. 26, 3, p. 164-170 7 p.

Research output: Contribution to journalArticleAcademicpeer-review

APA

Liberta, F., Rennegarbe, M., Roesler, R., Bijzet, J., Wiese, S., Hazenberg, B. P. C., & Fandrich, M. (2019). Morphological and primary structural consistency of fibrils from different AA patients (common variant). Amyloid, 26(3), 164-170. https://doi.org/10.1080/13506129.2019.1628015

Author

Liberta, Falk ; Rennegarbe, Matthies ; Roesler, Reinhild ; Bijzet, Johan ; Wiese, Sebastian ; Hazenberg, Bouke P. C. ; Fandrich, Marcus. / Morphological and primary structural consistency of fibrils from different AA patients (common variant). In: Amyloid. 2019 ; Vol. 26, No. 3. pp. 164-170.

Harvard

Liberta, F, Rennegarbe, M, Roesler, R, Bijzet, J, Wiese, S, Hazenberg, BPC & Fandrich, M 2019, 'Morphological and primary structural consistency of fibrils from different AA patients (common variant)', Amyloid, vol. 26, no. 3, pp. 164-170. https://doi.org/10.1080/13506129.2019.1628015

Standard

Morphological and primary structural consistency of fibrils from different AA patients (common variant). / Liberta, Falk; Rennegarbe, Matthies; Roesler, Reinhild; Bijzet, Johan; Wiese, Sebastian; Hazenberg, Bouke P. C.; Fandrich, Marcus.

In: Amyloid, Vol. 26, No. 3, 24.06.2019, p. 164-170.

Research output: Contribution to journalArticleAcademicpeer-review

Vancouver

Liberta F, Rennegarbe M, Roesler R, Bijzet J, Wiese S, Hazenberg BPC et al. Morphological and primary structural consistency of fibrils from different AA patients (common variant). Amyloid. 2019 Jun 24;26(3):164-170. https://doi.org/10.1080/13506129.2019.1628015


BibTeX

@article{634d69ac699241c2a577996cd63ac044,
title = "Morphological and primary structural consistency of fibrils from different AA patients (common variant)",
abstract = "Aims: To test the hypothesis that the fibril morphology and the fibril protein primary structure are conserved across different patients suffering from the common variant of systemic Amyloid A (AA) amyloidosis. Methods: Amyloid fibrils were extracted from the renal tissue of four patients. The fibril morphology was analysed in negatively stained samples with transmission electron microscopy (TEM). The fibril protein identity and fragment length were determined by using mass spectrometry. Results: The fibrils show a consistent morphology in all four patients and exhibit an average width of similar to 9.6 nm and an average pitch of similar to 112 nm. All fibrils are composed of polypeptide chains that can be assigned to human serum amyloid A (SAA) 1.1 protein. All fragments lack the N-terminal arginine residue and are C-terminally truncated. Differences exist concerning the exact C-terminal cleavage site. The most prominent cleavage site occurs at residues 64-67. Conclusions: Our data demonstrate that AA amyloid fibrils are consistent at the level of the protein primary structure and fibril morphology in the four analysed patients.",
keywords = "Systemic amyloidosis, fibril structure, protein misfolding, SAA, AMINO-ACID-SEQUENCE, RISK-FACTORS, PROTEIN AA, AMYLOIDOSIS, COMPONENT, DEPOSITION",
author = "Falk Liberta and Matthies Rennegarbe and Reinhild Roesler and Johan Bijzet and Sebastian Wiese and Hazenberg, {Bouke P. C.} and Marcus Fandrich",
year = "2019",
month = "6",
day = "24",
doi = "10.1080/13506129.2019.1628015",
language = "English",
volume = "26",
pages = "164--170",
journal = "Amyloid",
issn = "1350-6129",
publisher = "Taylor & Francis Ltd",
number = "3",

}

RIS

TY - JOUR

T1 - Morphological and primary structural consistency of fibrils from different AA patients (common variant)

AU - Liberta, Falk

AU - Rennegarbe, Matthies

AU - Roesler, Reinhild

AU - Bijzet, Johan

AU - Wiese, Sebastian

AU - Hazenberg, Bouke P. C.

AU - Fandrich, Marcus

PY - 2019/6/24

Y1 - 2019/6/24

N2 - Aims: To test the hypothesis that the fibril morphology and the fibril protein primary structure are conserved across different patients suffering from the common variant of systemic Amyloid A (AA) amyloidosis. Methods: Amyloid fibrils were extracted from the renal tissue of four patients. The fibril morphology was analysed in negatively stained samples with transmission electron microscopy (TEM). The fibril protein identity and fragment length were determined by using mass spectrometry. Results: The fibrils show a consistent morphology in all four patients and exhibit an average width of similar to 9.6 nm and an average pitch of similar to 112 nm. All fibrils are composed of polypeptide chains that can be assigned to human serum amyloid A (SAA) 1.1 protein. All fragments lack the N-terminal arginine residue and are C-terminally truncated. Differences exist concerning the exact C-terminal cleavage site. The most prominent cleavage site occurs at residues 64-67. Conclusions: Our data demonstrate that AA amyloid fibrils are consistent at the level of the protein primary structure and fibril morphology in the four analysed patients.

AB - Aims: To test the hypothesis that the fibril morphology and the fibril protein primary structure are conserved across different patients suffering from the common variant of systemic Amyloid A (AA) amyloidosis. Methods: Amyloid fibrils were extracted from the renal tissue of four patients. The fibril morphology was analysed in negatively stained samples with transmission electron microscopy (TEM). The fibril protein identity and fragment length were determined by using mass spectrometry. Results: The fibrils show a consistent morphology in all four patients and exhibit an average width of similar to 9.6 nm and an average pitch of similar to 112 nm. All fibrils are composed of polypeptide chains that can be assigned to human serum amyloid A (SAA) 1.1 protein. All fragments lack the N-terminal arginine residue and are C-terminally truncated. Differences exist concerning the exact C-terminal cleavage site. The most prominent cleavage site occurs at residues 64-67. Conclusions: Our data demonstrate that AA amyloid fibrils are consistent at the level of the protein primary structure and fibril morphology in the four analysed patients.

KW - Systemic amyloidosis

KW - fibril structure

KW - protein misfolding

KW - SAA

KW - AMINO-ACID-SEQUENCE

KW - RISK-FACTORS

KW - PROTEIN AA

KW - AMYLOIDOSIS

KW - COMPONENT

KW - DEPOSITION

U2 - 10.1080/13506129.2019.1628015

DO - 10.1080/13506129.2019.1628015

M3 - Article

VL - 26

SP - 164

EP - 170

JO - Amyloid

JF - Amyloid

SN - 1350-6129

IS - 3

ER -

ID: 92534029