β-Amyloid (1-42)由 42 个氨基酸组成的肽,其在阿尔茨海默病的发病机制中起关键作用。
编号:114789
CAS号:107761-42-2
单字母:H2N-DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA-OH
β-Amyloid (1-42)由 42 个氨基酸组成的肽,其在阿尔茨海默病的发病机制中起关键作用。
淀粉样β-肽(1-42)(Aβ42)是一种42个氨基酸的肽,在阿尔茨海默病(AD)的发病机制中起着关键作用。
发病机制中的主要有害作用可能由Aβ42调节,Aβ42作为基因转录的阻遏物或激活物,导致进一步的突触功能损伤和神经元变性。
当Aβ42升高到2.5μM时,SH-SY5Y细胞的活力降低到65%。使用染色质免疫沉淀(ChIP)和qRT-PCR分析,用具有LRP1和KAI1启动子的Aβ42相关肽处理SH-SY5Y细胞并增加APP mRNA水平,而无毒的Aβ42G33A肽作为大量存在于细胞核中的对照组,对mRNA表达没有任何影响。与几种不同长度的肽相比,Aβ42处理后其前体基因APP的转录和表达独家增加。
β42被认为是调节细胞功能的重要作用。
Amyloid β-Peptide (1-42) (Aβ42) human is a 42-amino acid peptide that plays a key role in the pathogenesis of Alzheimer disease (AD).
The main deleterious effects in the pathogenesis are probably regulated by Aβ42, which acts as a repressor or activator of gene transcription causing further synaptic function damage and neuronal degeneration .
Aβ42 reduced the viability of SH-SY5Y cells to 65% when it rose to 2.5 μM. Using the chromatin immunoprecipitation (ChIP) and qRT-PCR assays, treatment of SH-SY5Y cells with Aβ42 associated peptide with both LRP1 and KAI1 promoters and increased APP mRNA levels, while the nontoxic Aβ42 G33A peptide, as a control group which presents in the nucleus abundantly, did not have any influence on mRNA expression. The exclusive increase of transcription and expression of its precursor gene APP was found with the treatment of Aβ42, compared with several different lengths of peptides .
Aβ42 is regarded as an important role in modulating the function of voltage-gated Ca2+- and K+-channels of the surface neuronal membranes. Application of Aβ42 with desired concentrations (1 to 10 μM) in the perfusing medium had no impact on delayed rectifier K+-current and leakage current, while enhanced inactivation of Ca2+-current and blocked Ca2+-dependent K+-current .
β1-42,淀粉样前体蛋白的42个残基片段,已被发现是阿尔茨海默病和晚期唐氏综合征患者大脑中形成的老年斑的主要成分。Aβ1-42在生理pH值下容易形成神经毒性低聚物。另一方面,该肽具有抗菌活性。该肽的序列对应于人、牛、犬、猫、绵羊、豚鼠和兔Aβ42的序列。该肽已被用于通过荧光相关光谱检测阿尔茨海默病患者脑脊液中的淀粉样β蛋白多聚体。关于Aβ1-42单体和原纤维制备的详细描述,请参阅Jan、Hartley和Lashuel、Stine等人(2011)以及Broersen及其同事的论文。Ryan等人的研究结果表明,10%的氨比HFIP更有效地分解Aβ42。
Aβ 1-42, 42-residue fragment of amyloid precursor protein, has been found to be a major constituent of the senile plaques formed in the brains of patients with Alzheimer’s disease and late Down’s syndrome. Aβ 1-42 readily forms neurotoxic oligomers at physiological pH. On the other hand, the peptide shows antimicrobial activity. The sequence of this peptide corresponds to the sequence of human, bovine, canine, feline, ovine, guinea pig, and rabbit Aβ42. The peptide has been used to detect amyloid β-protein multimers in the cerebrospinal fluid of Alzheimer’s disease patients through fluorescence correlation spectroscopy. For detailed descriptions of the preparation of Aβ 1-42 monomers and protofibrils please see the papers of Jan, Hartley, and Lashuel, Stine et al. (2011), and of Broersen and colleagues. The findings of Ryan et al. indicate that 10% ammonia disaggregates Aβ42 more efficiently than HFIP.
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