Unique Amyloid Protein Subunit common to Different Types of Amyloid Fibril

Nature ◽  
1973 ◽  
Vol 244 (5415) ◽  
pp. 362-364 ◽  
Author(s):  
G. HUSBY ◽  
J. B. NATVIG ◽  
T. E. MICHAELSEN ◽  
K. SLETTEN ◽  
H. HÖST
Keyword(s):  
Amyloid Fibril ◽  
Amyloid Protein ◽  
Protein Subunit ◽  
Different Types

Immunocytochemical Localization of Amyloid Protein AA in the “Dense Fibrillar Inclusions” of the Reticuloendothelical Cells

1977 ◽  
Vol 35 ◽  
pp. 438-439
Author(s):  
T. Shirahama ◽  
M. Skinner ◽  
A.S. Cohen
Keyword(s):  
Amyloid Fibril ◽  
Close Association ◽  
Gel Filtration ◽  
Fibril Formation ◽  
Amyloid Protein ◽  
Electron Microscopic ◽  
Amyloid Deposits ◽  
Amyloid Fibril Formation ◽  
Electron Microscopic Technique ◽  
Lysosomal System

A1thought the mechanisms of amyloidogenesis have not been entirely clarified, proteolysis of the parent proteins may be one of the important steps in the amyloid fibril formation. Recently, we reported that "dense fibrillar inclusions" (DFI), which had the characteristics of lysosomes and contained organized fibrillar profiles as well, were observed in the reticuloendothelial cells in close association with the foci of new amyloid deposits. We considered the findings as evidence for the involvement of lysosomal system in amyloid fibril formation (l). In the present study, we attempted to determine the identity of the contents of the DFI by the use of antisera against the amyloid protein (AA) and an immuno-electron microscopic technique.Amyloidosis was induced in CBA/J mice by daily injections of casein (l). AA was isolated from amyloid-laden spleens by gel filtration and antibody to it was produced in rabbits (2). For immunocytochemistry, the unlabeled antibody enzyme method (3) was employed.

scholarly journals HUMAN AMYLOID PROTEIN: CHEMICAL VARIABILITY AND HOMOGENEITY

1971 ◽  
Vol 19 (1) ◽  
pp. 1-15 ◽  
Author(s):  
M. HARADA ◽  
C. ISERSKY ◽  
P. CUATRECASAS ◽  
D. PAGE ◽  
H. A. BLADEN ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amyloid Fibril ◽  
Gel Filtration ◽  
Protein S ◽  
Amyloid Protein ◽  
X Ray Diffraction ◽  
Amyloid Proteins ◽  
X Ray ◽  
Chemical Variability ◽  
Sepharose 4B

The morphology of the fibril of amyloid derived from different individuals is similar, but occasionally significant differences are noted. All human amyloid filaments have a "β-pleated sheet" conformation as revealed by x-ray diffraction, and those examined after orientation show a "cross-β" pattern. All amyloid fibril concentrates studied so far can be fractionated to obtain the major amyloid protein component(s) by sequential gel filtration with 5 M guanidine-HCl in 1 N acetic acid on Sepharose 4B and Sephadex G-100 or G-75 columns with the removal of over 28% of proteins representing minor constituents. The major amyloid protein(s) obtained from the spleen and/or liver of six patients is found to contain tryptophan, to be deficient in hydroxylysine and hydroxyproline and usually at least one commonly occurring amino acid and to have a high content of dicarboxylic acid and short chain amino acids and unreactive (blocked) NH2-terminal groups or aspartic acid-asparagine (Asx). However, the amyloid protein(s) from each individual differs from that of the others in molecular weight, in amino acid composition and in the presence or absence of specific tryptic peptides. Amyloid protein(s) from the liver and spleen of the same individual is identical. No chemical characteristics distinguish amyloid proteins derived from cases classified clinically as "primary" from those classified as "secondary." There is a striking chemical similarity between amyloid proteins and the NH2-terminal variable fragment of the light and heavy chain of immumoglobulin proteins.

scholarly journals Gold nanocolloid–protein interactions and their impact on β-sheet amyloid fibril formation

RSC Advances ◽  
2018 ◽  
Vol 8 (2) ◽  
pp. 980-986 ◽  
Author(s):  
Heloise R. Barros ◽  
Maria Kokkinopoulou ◽  
Izabel C. Riegel-Vidotti ◽  
Katharina Landfester ◽  
Héloïse Thérien-Aubin
Keyword(s):  
Protein Interactions ◽  
Amyloid Fibril ◽  
Interaction Mechanism ◽  
Fibril Formation ◽  
Amyloid Protein ◽  
Degenerative Diseases ◽  
Amyloid Fibril Formation ◽  
Protein Fibrils ◽  
Β Sheet

Formation of amyloid protein fibrils is associated with degenerative diseases. Here, the interaction mechanism between globular and fibrillar proteins with AuNPs were investigated in order to potentially control and reverse the fibrillation process.

scholarly journals Isolation and spectral characterization of phycobiliproteins

1970 ◽  
Vol 116 (2) ◽  
pp. 161-169 ◽  
Author(s):  
F. W. J. Teale ◽  
R. E. Dale
Keyword(s):  
Energy Transfer ◽  
Ionic Strength ◽  
Aqueous Medium ◽  
Fluorescence Emission ◽  
Protein Subunit ◽  
Fluorescence Excitation ◽  
Different Types ◽  
Single Protein ◽  
Polarization Spectra

Several phycobiliproteins were prepared chromatographically pure and their absorption, fluorescence-emission, fluorescence-excitation and fluorescence-excitation polarization spectra determined. Changes in these spectra with ionic strength of the aqueous medium and chromoprotein concentration were interpreted in terms of interchromophore energy transfer and protein subunit equilibria. The complexity of the polarization spectra confirms the presence of different types of chromophore, designated sensitizing (‘s’) and fluorescing (‘f’), in a single protein.

Structure of a Functional Amyloid Protein Subunit Computed Using Sequence Variation

2014 ◽  
Vol 137 (1) ◽  
pp. 22-25 ◽  
Author(s):  
Pengfei Tian ◽  
Wouter Boomsma ◽  
Yong Wang ◽  
Daniel E. Otzen ◽  
Mogens H. Jensen ◽  
...  
Keyword(s):  
Sequence Variation ◽  
Amyloid Protein ◽  
Protein Subunit ◽  
Functional Amyloid

scholarly journals Accumulation of pro-apolipoprotein A-II in mouse senile amyloid fibrils

1997 ◽  
Vol 325 (3) ◽  
pp. 653-659 ◽  
Author(s):  
Keiichi HIGUCHI ◽  
Kumiko KOGISHI ◽  
Jing WANG ◽  
Chen XIA ◽  
Takuya CHIBA ◽  
...  
Keyword(s):  
Amino Acid ◽  
High Density Lipoprotein ◽  
Relative Abundance ◽  
Mouse Liver ◽  
Amyloid Fibrils ◽  
Amyloid Fibril ◽  
Density Lipoprotein ◽  
Amyloid Protein ◽  
Amino Acid Residues ◽  
Apolipoprotein A

Apolipoprotein A-II (apoA-II), the major apoprotein of serum high-density lipoprotein, is deposited as amyloid fibrils (AApoAII) in murine senile amyloidosis. We have identified and purified a more basic amyloid protein from old-mouse liver. N-terminal sequencing of the protein revealed that the pro-segment of five amino acid residues (Ala-Leu-Val-Lys-Arg) extended from the N-terminal glutamine residue of mature apoA-II protein. MS analysis revealed the deposit of intact pro-apoA-II protein (molecular mass 9319 Da). Antiserum was prepared for staining of the AApoAII amyloid deposition. The relative abundance of pro-apoA-II to mature apoA-II in the amyloid-fibril fraction isolated from livers of mice with severe amyloidosis was 14.1%. The similar abundance of pro-apoA-II in the amyloid fibril fraction from the spleen (16.3%) suggested that deposited pro-apoA-II originated from the blood. The concentration of pro-apoA-II was much lower in the serum (1.5% of mature apoA-II) than in the amyloid-fibril fraction. There was no difference in the content of pro-apoA-II between the amyloidogenetic R1.P1-Apoa2c and amyloid-resistant SAMR1 strains at the age of 3 months. The abundance of pro-apoA-II in the amyloid-fibril fraction compared with the serum suggested that it plays a key role in the initialization of mouse senile amyloidosis.

scholarly journals MURINE AMYLOID FIBRIL PROTEIN: ISOLATION, PURIFICATION AND CHARACTERIZATION

1971 ◽  
Vol 19 (1) ◽  
pp. 16-28 ◽  
Author(s):  
G. G. GLENNER ◽  
D. PAGE ◽  
C. ISERSKY ◽  
M. HARADA ◽  
P. CUATRECASAS ◽  
...  
Keyword(s):  
Amyloid Fibrils ◽  
Amyloid Fibril ◽  
Sodium Dodecyl ◽  
Gel Filtration ◽  
Disc Electrophoresis ◽  
Structure Identification ◽  
Major Protein ◽  
Amyloid Protein ◽  
Molecular Weights ◽  
Sepharose 4B

Murine amyloid has been produced by four different induction methods ( Mycobacterium butyricum, casein, casein plus Freund's adjuvant and endotoxin-induced mouse amyloidosis) in several strains and obtained from mice with "spontaneous" amyloidosis. The amyloid fibrils have been concentrated from spleen and liver. Electron microscopy of all of these preparations reveals the amyloid fibril to be 100 Å in width and composed of two parallel filaments, each measuring 35-40 Å in width and having the appearance of a twisted ribbon. X-ray diffraction of all preparations reveals a "backbone" spacing at 4.75 Å and a "side chain" spacing at 11 Å indicating a "β-pleated sheet" structure. Identification of the major protein component of amyloid fibril concentrates was made by combined use of sodium dodecyl sulfate polyacrylamide disc electrophoresis, labeling of the protein with 3H-tryptophan and Sepharose 4B gel filtration. Purification of the amyloid protein from spontaneous amyloidosis liver was accomplished by sequential gel filtration with 5 M guanidine in 1 N acetic acid on Sepharose 4B and Sephadex G-100 or G-75 columns. The material is a unique glycoprotein with a molecular weight of 7200, a high content of dicarboxylic and short chain amino acids, a significant amount of tryptophan and an unreactive NH2-terminal amino acid, tentatively identified as pyrrolid-2-one-5-carboxylic acid. There are no methionine, half-cystine, hydroxylysine or hydroxyproline residues. Murine amyloid protein, therefore, has striking similarities to many human amyloid protein preparations. It differs from the human proteins in the similarity of molecular weights of different preparations.

scholarly journals Selective vulnerability of different types of commissural neurons for amyloid  -protein-induced neurodegeneration in APP23 mice correlates with dendritic tree morphology

Brain ◽  
2006 ◽  
Vol 129 (11) ◽  
pp. 2992-3005 ◽  
Author(s):  
E. Capetillo-Zarate ◽  
M. Staufenbiel ◽  
D. Abramowski ◽  
C. Haass ◽  
A. Escher ◽  
...  
Keyword(s):  
Dendritic Tree ◽  
Selective Vulnerability ◽  
Amyloid Protein ◽  
Commissural Neurons ◽  
Tree Morphology ◽  
Different Types
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