Amyloid fibril proteins

Xing, Yanming; Higuchi, Kenichi

doi:10.1016/s0047-6374(02)00098-2

Cited by 59 publications

(50 citation statements)

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“…Several conditions might contribute to the progress of amyloidosis: (1) structures or mutations of amyloid proteins, 18 (2) levels of the amyloid proteins in the blood or local environment in each tissue, (3) transmission of amyloidogenic materials and (4) other environmental conditions such as inflammation, nutrition and aging. In particular, many tissue factors that facilitate the metabolism, aggregation or stability of amyloid fibrils may contribute to a differential tissue distribution of amyloid deposition.…”

Section: Discussionmentioning

confidence: 99%

“…Transmission of amyloid fibrils from the environment may influence fibril formation as an important epigenetic factor. 18 The R1.P1-Apoa2 c strain has been a valuable model system for the investigation of genetic and epigenetic factors in amyloid deposition. However, at least 2-3 months are required to evaluate the degree of amyloid deposition even after the injection of AApoAII fibrils.…”

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confidence: 99%

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Amyloidosis in transgenic mice expressing murine amyloidogenic apolipoprotein A-II (Apoa2)

Yao

et al. 2007

Laboratory Investigation

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In mice, apolipoprotein A-II (apoA-II) self-associates to form amyloid fibrils (AApoAII) in an age-associated manner. We postulated that the two most important factors in apoA-II amyloidosis are the Apoa2 c allele, which codes for the amyloidogenic protein APOA2C (Gln5, Ala38) and transmission of amyloid fibrils. To characterize further the contribution of the Apoa2 c allele to amyloidogenesis and improve detection of amyloidogenic materials, we established transgenic mice that overexpress APOA2C protein under the cytomegalovirus (CMV) immediate early gene (CMV-IE) enhancer/ chicken b promoter. Compared to transgene negative (Tg À/À ) mice that express apoA-II protein mainly in the liver, mice homozygous (Tg þ / þ ) and heterozygous (Tg þ /À ) for the transgene express a high level of apoA-II protein in many tissues. They also have higher plasma concentrations of apoA-II, higher ratios of ApoA-II/apolipoprotein A-I (ApoA-I) and higher concentrations of high-density lipoprotein (HDL) cholesterol. Following injection of AApoAII fibrils into Tg þ / þ mice, amyloid deposition was observed in the testis, liver, kidney, heart, lungs, spleen, tongue, stomach and intestine but not in the brain. In Tg þ / þ mice, but not in Tg À/À mice, amyloid deposition was induced by injection of less than 10 À8 mg AApoAII fibrils. Furthermore, deposition in Tg þ / þ mice occurred more rapidly and to a greater extent than in Tg À/À mice. These studies indicate that increased levels of APOA2C protein lead to earlier and greater amyloid deposition and enhanced sensitivity to the transmission of amyloid fibrils in transgenic mice. This transgenic mouse model should prove valuable for studies of amyloidosis.

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Section: Discussionmentioning

confidence: 99%

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confidence: 99%

Amyloidosis in transgenic mice expressing murine amyloidogenic apolipoprotein A-II (Apoa2)

Yao

et al. 2007

Laboratory Investigation

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“…The polar/nonpolar binary pattern of SRC proteins is similar to that of amylodogenic proteins in which the occurrence of PPPPP and NNNNN pattern are ranked first and fourth (1). Amyloidogenic proteins are well known to self-assemble into amyloid fibrils from a partially unfolded state, which are pathological aggregates of protein in Alzheimer's and prion diseases (52). The diameter of the fibers formed by SRC8 was larger than that of amyloid fibrils, which are always 6 -13 nm in diameter independent of the amino acid sequence.…”

Section: Construction Of Recombinant Expression Plasmid Pet21a(ϩ)-srcn-mentioning

confidence: 97%

Cloning, Expression, and Assembly of Sericin-like Protein

Huang

Valluzzi

Bini

et al. 2003

Journal of Biological Chemistry

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Recombinant sericin proteins of different molecular masses (17.4, 31.9, and 46.5 kDa), based on the 38-amino acid repetitive motif of native sericin, were cloned, expressed, and purified. The recombinant sericin self-assembled during dialysis (starting concentration of 2.5 mg/ml) forming twisted fibers. Circular dichroism and Fourier transform infrared spectroscopy studies demonstrated protein conformational transitions occurred from random coil to ␤-sheets during the dialysis. Congo red-stained recombinant sericin fibrils exhibited applegreen birefringence, indicating long-range order in the array of ␤-sheets. Biosynthetic sericin has a high content of polar amino acids (e.g. Silk of Bombyx mori is composed of two kinds of proteins: the fibroin which is synthesized in the posterior silk gland and the sericins produced by the middle silk gland. The sericins bind two fibroin fibers together in the anterior region of the gland as the fibers are spun to form the cocoon. Sericins represent a family of proteins whose molecular mass ranges from 20 to 310 kDa (2, 3) and are characterized by an unusually high serine content, 38.1 mol % (4). Sericins are soluble in hot water, which makes it possible to degum the silk fibroin threads.Two genes encode sericins, Ser1 and Ser2 (5-8). The different molecular weight sericins are the products of different splicing events at the transcript level. Some conformation studies with sericins from the silk gland of B. mori or regenerated sericin from B. mori cocoons suggested random coil with some ␤ structure (9, 10). However, the samples used in these studies were mixtures of the various native sericin proteins, therefore the structure of the individual proteins is unknown and the contribution of specific sequences toward secondary structure is not confirmed. Sericin model peptides such as poly(L-serine) (11-16), poly(O-benzyl-L-serine) (12), and poly(O-acetyl-L-serine) (13,14) were synthesized for structural feature characterization. The ability of poly(L-serine) to fold into a ␤ conformation depended on molecular weight. Low molecular weight poly(L-serine) (molecular weight 650) was soluble and adopted a random coil conformation in aqueous solution, whereas high molecular weight poly(L-serine) (molecular weight 105,000) formed ␤-sheets and was insoluble in water (11). However, homopolypeptides like poly(L-serine) do not match native sericin in terms of amino acid composition, sequence, and molecular weight. Therefore, to better understand sericin structure, interactions between sericin and fibroin, and the biological relevance of sericin in fiber structure, high molecular weight pure sericin-like proteins are required.Sericin 1 encoded by Ser 1 consists of 70 repeats of the 38-amino acid motif (5): SSTGSSSNTDSNSNSVGSSTS-GGSSTYGYSSNSRDGSV. The molecular mass of sericin 1 proteins is 76 -284 kDa. The 38-amino acid repeat motif exhibits a high content of hydrophilic amino acids: 44.7% serine, 10.5% threonine, and 7.9% tyrosine, very close to the average amino acid composition of serici...

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“…In general, this disease is the result of longlasting inflammations in humans [2][3][4][5] and in animal species [6][7][8][9][10].…”

Section: Introductionmentioning

confidence: 99%

Increasing fatal AA amyloidosis in hunting falcons and how to identify the risk: a report from the United Arab Emirates

Hampel

Kinne

Wernery

et al. 2009

Amyloid

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Amyloid fibril proteins

Cited by 59 publications

References 70 publications

Amyloidosis in transgenic mice expressing murine amyloidogenic apolipoprotein A-II (Apoa2)

Amyloidosis in transgenic mice expressing murine amyloidogenic apolipoprotein A-II (Apoa2)

Cloning, Expression, and Assembly of Sericin-like Protein

Increasing fatal AA amyloidosis in hunting falcons and how to identify the risk: a report from the United Arab Emirates

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