アミロイド前駆体蛋白質
WordNet
- a substance from which another substance is formed (especially by a metabolic reaction)
- a person who goes before or announces the coming of another (同)forerunner
- any of a large group of nitrogenous organic compounds that are essential constituents of living cells; consist of polymers of amino acids; essential in the diet of animals for growth and for repair of tissues; can be obtained from meat and eggs and milk and legumes; "a diet high in protein"
- (pathology) a waxy translucent complex protein resembling starch that results from degeneration of tissue
- a non-nitrogenous food substance consisting chiefly of starch; any substance resembling starch
PrepTutorEJDIC
- (…の)前朕,前触れ《+『of』+『名』》
- 蛋白(たんばく)質
UpToDate Contents
全文を閲覧するには購読必要です。 To read the full text you will need to subscribe.
English Journal
- Glycosaminoglycans promote fibril formation by amyloidogenic immunoglobulin light chains through a transient interaction.
- Martin DJ, Ramirez-Alvarado M.AbstractAmyloid formation occurs when a precursor protein misfolds and aggregates, forming a fibril nucleus that serves as a template for fibril growth. Glycosaminoglycans are highly charged polymers known to associate with tissue amyloid deposits that have been shown to accelerate amyloidogenesis in vitro. We studied two immunoglobulin light chain variable domains from light chain amyloidosis patients with 90% sequence identity, analyzing their fibril formation kinetics and binding properties with different glycosaminoglycan molecules. We find that the less amyloidogenic of the proteins shows a weak dependence on glycosaminoglycan size and charge, while the more amyloidogenic protein responds only minimally to changes in the glycosaminoglycan. These glycosaminoglycan effects on fibril formation do not depend on a stable interaction between the two species but still show characteristic traits of an interaction-dependent mechanism. We propose that transient, predominantly electrostatic interactions between glycosaminoglycans and the precursor proteins mediate the acceleration of fibril formation in vitro.
- Biophysical chemistry.Biophys Chem.2011 Sep;158(1):81-9. Epub 2011 May 18.
- Amyloid formation occurs when a precursor protein misfolds and aggregates, forming a fibril nucleus that serves as a template for fibril growth. Glycosaminoglycans are highly charged polymers known to associate with tissue amyloid deposits that have been shown to accelerate amyloidogenesis in vitro.
- PMID 21640469
- Mislocalization of CDK11/PITSLRE, a regulator of the G2/M phase of the cell cycle, in Alzheimer disease.
- Baji? VP, Su B, Lee HG, Kudo W, Siedlak SL, Zivkovi? L, Spremo-Potparevi? B, Djelic N, Milicevic Z, Singh AK, Fahmy LM, Wang X, Smith MA, Zhu X.SourceInstitute of Biomedical Research, Galenika a.d., 11000, Belgrade, Serbia, vladanbajic@yahoo.com.
- Cellular & molecular biology letters.Cell Mol Biol Lett.2011 Sep;16(3):359-72. Epub 2011 Apr 3.
- Post-mitotic neurons are typically terminally differentiated and in a quiescent status. However, in Alzheimer disease (AD), many neurons display ectopic re-expression of cell cycle-related proteins. Cyclin-dependent kinase 11 (CDK11) mRNA produces a 110-kDa protein (CDK11(p110)) throughout the cell
- PMID 21461981
Japanese Journal
- Amyloid Precursor Protein Binding Protein Fe65 Is Cleaved by Caspases during DNA Damage-Induced Apoptosis
- Saeki Kazunori,Nose Yasuyo,Hirao Nobukuni,Takasawa Ryoko,Tanuma Sei-ichi
- Biological & Pharmaceutical Bulletin 34(2), 290-294, 2011
- … Caspases cleave several cellular proteins to execute cell death by apoptosis. … In this study, we tested whether an amyloid precursor protein (APP) binding protein Fe65 is proteolytically degraded in neuronal cell death by apoptosis, using a neuron-like cell line, human neuroblastoma SH-SY5Y cells. …
- NAID 130000402205
- Correlation Between Decrease in Protein Levels of Ubiquitin Ligase HRD1 and Amyloid-β Production
- Saito Ryo,Kaneko Masayuki,Okuma Yasunobu,Nomura Yasuyuki
- Journal of Pharmacological Sciences advpub(0), 1006300412, 2010
- … Endoplasmic reticulum–associated degradation (ERAD) is a quality control mechanism in which unfolded proteins are retro-translocated to the cytosol for degradation. … Our recent study showed that suppression of expression of ubiquitin ligase HRD1, which is involved in ERAD, caused amyloid precursor protein (APP) accumulation and amyloid-β (Aβ) production. …
- NAID 130000301202
Related Links
- Amyloid precursor protein (APP) is an integral membrane protein expressed in many tissues and concentrated in the synapses of neurons. Its primary function is not known, though it has been implicated as a regulator of synapse formation, ...
★リンクテーブル★
[★]
- 英
- amyloid precursor protein, amyloid precursor proteins, APP
- 同
- アミロイドβ蛋白質前駆体 amyloid β-protein precursor β-APP
[show details]
[★]
[★]
- 関
- progenitor
[★]
アミロイド
- 関
- amyloid fibril、amyloid protein