Journal of Amino Acids最新文献_第9页

Protein modification by dicarbonyl molecular species in neurodegenerative diseases. 二羰基分子物种在神经退行性疾病中的蛋白质修饰。

Journal of Amino Acids Pub Date : 2011-01-01 Epub Date: 2011-03-14 DOI: 10.4061/2011/461216

Wesley M Williams, Aaron Weinberg, Mark A Smith

{"title":"Protein modification by dicarbonyl molecular species in neurodegenerative diseases.","authors":"Wesley M Williams, Aaron Weinberg, Mark A Smith","doi":"10.4061/2011/461216","DOIUrl":"https://doi.org/10.4061/2011/461216","url":null,"abstract":"Neurodegeneration results from abnormalities in cerebral metabolism and energy balance within neurons, astrocytes, microglia, or microvascular endothelial cells of the blood-brain barrier. In Alzheimer's disease, β-amyloid is considered the primary contributor to neuropathology and neurodegeneration. It now is believed that certain systemic diseases, such as diabetes mellitus, can contribute to neurodegeneration through the effects of chronic hyperglycemia/insulin resistance resulting in protein glycation, oxidative stress and inflammation within susceptible brain regions. Here, we present an overview of research focusing on the role of protein glycation, oxidative stress, and inflammation in the neurodegenerative process. Of special interest in this paper is the effect of methylglyoxal (MGO), a cytotoxic byproduct of glucose metabolism, elevated in neurodegenerative disease, and diabetes mellitus, on cerebral protein function and oxidative stress. How MGO interacts with amino acid residues within β-amyloid, and small peptides within the brain, is also discussed in terms of the affect on protein function.","PeriodicalId":14901,"journal":{"name":"Journal of Amino Acids","volume":"2011 ","pages":"461216"},"PeriodicalIF":0.0,"publicationDate":"2011-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.4061/2011/461216","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"30458578","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 17

Serpin Inhibition Mechanism: A Delicate Balance between Native Metastable State and Polymerization. 丝氨酸蛋白酶抑制机制:原生亚稳态和聚合之间的微妙平衡。

Journal of Amino Acids Pub Date : 2011-01-01 Epub Date: 2011-05-24 DOI: 10.4061/2011/606797

Mohammad Sazzad Khan, Poonam Singh, Asim Azhar, Asma Naseem, Qudsia Rashid, Mohammad Anaul Kabir, Mohamad Aman Jairajpuri

{"title":"Serpin Inhibition Mechanism: A Delicate Balance between Native Metastable State and Polymerization.","authors":"Mohammad Sazzad Khan, Poonam Singh, Asim Azhar, Asma Naseem, Qudsia Rashid, Mohammad Anaul Kabir, Mohamad Aman Jairajpuri","doi":"10.4061/2011/606797","DOIUrl":"https://doi.org/10.4061/2011/606797","url":null,"abstract":"The serpins (serine proteinase inhibitors) are structurally similar but functionally diverse proteins that fold into a conserved structure and employ a unique suicide substrate-like inhibitory mechanism. Serpins play absolutely critical role in the control of proteases involved in the inflammatory, complement, coagulation and fibrinolytic pathways and are associated with many conformational diseases. Serpin's native state is a metastable state which transforms to a more stable state during its inhibitory mechanism. Serpin in the native form is in the stressed (S) conformation that undergoes a transition to a relaxed (R) conformation for the protease inhibition. During this transition the region called as reactive center loop which interacts with target proteases, inserts itself into the center of β-sheet A to form an extra strand. Serpin is delicately balanced to perform its function with many critical residues involved in maintaining metastability. However due to its typical mechanism of inhibition, naturally occurring serpin variants produces conformational instability that allows insertion of RCL of one molecule into the β-sheet A of another to form a loop-sheet linkage leading to its polymerization and aggregation. Thus understanding the molecular basis and amino acid involved in serpin polymerization mechanism is critical to devising strategies for its cure.","PeriodicalId":14901,"journal":{"name":"Journal of Amino Acids","volume":" ","pages":"606797"},"PeriodicalIF":0.0,"publicationDate":"2011-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.4061/2011/606797","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39968369","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 74

Formation of the 42-mer Amyloid β Radical and the Therapeutic Role of Superoxide Dismutase in Alzheimer's Disease. 42-mer 淀粉样β自由基的形成和超氧化物歧化酶在阿尔茨海默病中的治疗作用。

Journal of Amino Acids Pub Date : 2011-01-01 Epub Date: 2011-01-16 DOI: 10.4061/2011/654207

Kazuma Murakami, Takahiko Shimizu, Kazuhiro Irie

引用次数: 0

Functional Subunits of Eukaryotic Chaperonin CCT/TRiC in Protein Folding. 真核伴侣蛋白CCT/TRiC在蛋白质折叠中的功能亚基。

Journal of Amino Acids Pub Date : 2011-01-01 Epub Date: 2011-07-02 DOI: 10.4061/2011/843206

M Anaul Kabir, Wasim Uddin, Aswathy Narayanan, Praveen Kumar Reddy, M Aman Jairajpuri, Fred Sherman, Zulfiqar Ahmad

{"title":"Functional Subunits of Eukaryotic Chaperonin CCT/TRiC in Protein Folding.","authors":"M Anaul Kabir, Wasim Uddin, Aswathy Narayanan, Praveen Kumar Reddy, M Aman Jairajpuri, Fred Sherman, Zulfiqar Ahmad","doi":"10.4061/2011/843206","DOIUrl":"https://doi.org/10.4061/2011/843206","url":null,"abstract":"Molecular chaperones are a class of proteins responsible for proper folding of a large number of polypeptides in both prokaryotic and eukaryotic cells. Newly synthesized polypeptides are prone to nonspecific interactions, and many of them make toxic aggregates in absence of chaperones. The eukaryotic chaperonin CCT is a large, multisubunit, cylindrical structure having two identical rings stacked back to back. Each ring is composed of eight different but similar subunits and each subunit has three distinct domains. CCT assists folding of actin, tubulin, and numerous other cellular proteins in an ATP-dependent manner. The catalytic cooperativity of ATP binding/hydrolysis in CCT occurs in a sequential manner different from concerted cooperativity as shown for GroEL. Unlike GroEL, CCT does not have GroES-like cofactor, rather it has a built-in lid structure responsible for closing the central cavity. The CCT complex recognizes its substrates through diverse mechanisms involving hydrophobic or electrostatic interactions. Upstream factors like Hsp70 and Hsp90 also work in a concerted manner to transfer the substrate to CCT. Moreover, prefoldin, phosducin-like proteins, and Bag3 protein interact with CCT and modulate its function for the fine-tuning of protein folding process. Any misregulation of protein folding process leads to the formation of misfolded proteins or toxic aggregates which are linked to multiple pathological disorders.","PeriodicalId":14901,"journal":{"name":"Journal of Amino Acids","volume":" ","pages":"843206"},"PeriodicalIF":0.0,"publicationDate":"2011-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.4061/2011/843206","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39968139","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 39

The Aggregation Inhibitor Peptide QBP1 as a Therapeutic Molecule for the Polyglutamine Neurodegenerative Diseases. 聚集抑制肽QBP1作为多谷氨酰胺性神经退行性疾病的治疗分子。

Journal of Amino Acids Pub Date : 2011-01-01 Epub Date: 2011-06-30 DOI: 10.4061/2011/265084

H Akiko Popiel, James R Burke, Warren J Strittmatter, Shinya Oishi, Nobutaka Fujii, Toshihide Takeuchi, Tatsushi Toda, Keiji Wada, Yoshitaka Nagai

{"title":"The Aggregation Inhibitor Peptide QBP1 as a Therapeutic Molecule for the Polyglutamine Neurodegenerative Diseases.","authors":"H Akiko Popiel, James R Burke, Warren J Strittmatter, Shinya Oishi, Nobutaka Fujii, Toshihide Takeuchi, Tatsushi Toda, Keiji Wada, Yoshitaka Nagai","doi":"10.4061/2011/265084","DOIUrl":"10.4061/2011/265084","url":null,"abstract":"Misfolding and abnormal aggregation of proteins in the brain are implicated in the pathogenesis of various neurodegenerative diseases including Alzheimer's, Parkinson's, and the polyglutamine (polyQ) diseases. In the polyQ diseases, an abnormally expanded polyQ stretch triggers misfolding and aggregation of the disease-causing proteins, eventually resulting in neurodegeneration. In this paper, we introduce our therapeutic strategy against the polyQ diseases using polyQ binding peptide 1 (QBP1), a peptide that we identified by phage display screening. We showed that QBP1 specifically binds to the expanded polyQ stretch and inhibits its misfolding and aggregation, resulting in suppression of neurodegeneration in cell culture and animal models of the polyQ diseases. We further demonstrated the potential of protein transduction domains (PTDs) for in vivo delivery of QBP1. We hope that in the near future, chemical analogues of aggregation inhibitor peptides including QBP1 will be developed against protein misfolding-associated neurodegenerative diseases.","PeriodicalId":14901,"journal":{"name":"Journal of Amino Acids","volume":" ","pages":"265084"},"PeriodicalIF":0.0,"publicationDate":"2011-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.4061/2011/265084","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39968914","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 24

Intracisternally injected L-proline activates hypothalamic supraoptic, but not paraventricular, vasopressin-expressing neurons in conscious rats. 脑内注射l -脯氨酸激活清醒大鼠下丘脑视上表达抗利尿激素的神经元，但不激活室旁表达抗利尿激素的神经元。

Journal of Amino Acids Pub Date : 2011-01-01 Epub Date: 2011-10-16 DOI: 10.4061/2011/230613

Yumi Takemoto

{"title":"Intracisternally injected L-proline activates hypothalamic supraoptic, but not paraventricular, vasopressin-expressing neurons in conscious rats.","authors":"Yumi Takemoto","doi":"10.4061/2011/230613","DOIUrl":"https://doi.org/10.4061/2011/230613","url":null,"abstract":"When injected into specific rat brain regions, the neurotransmitter candidate L-proline produces various cardiovascular changes through ionotropic excitatory amino acid receptors. The present study used an immunohistochemical double-labeling approach to determine whether intracisternally injected L-proline in freely moving rats, which increases blood pressure, activates hypothalamic vasopressin-expressing neurons and ventral medullary tyrosine-hydroxylase- (TH-) containing neurons. Following injection of L-proline, the number of activated hypothalamic neurons that coexpressed vasopressin and c-Fos was much greater in the supraoptic nucleus (SON) than in the paraventricular nucleus (PVN) of rats with increased blood pressure. The number of activated TH-containing neurons was significantly greater following L-proline treatment than following control injections of artificial cerebrospinal fluid (ACSF). These results clearly demonstrate that intracisternally injected L-proline activates hypothalamic supraoptic, but not paraventricular, vasopressin-expressing neurons and medullary TH-containing (A1/C1) neurons in freely moving rats.","PeriodicalId":14901,"journal":{"name":"Journal of Amino Acids","volume":" ","pages":"230613"},"PeriodicalIF":0.0,"publicationDate":"2011-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.4061/2011/230613","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39968438","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 7

Signal protein-derived peptides as functional probes and regulators of intracellular signaling. 信号蛋白衍生肽作为细胞内信号传导的功能探针和调节剂。

Journal of Amino Acids Pub Date : 2011-01-01 Epub Date: 2011-08-23 DOI: 10.4061/2011/656051

Alexander O Shpakov

引用次数: 22

Synthesis and Characterization of New Optically Active Poly (ethyl L-lysinamide)s and Poly (ethyl L-lysinimide)s. 新型光学活性聚（乙基 L-赖氨酰胺）和聚（乙基 L-赖氨酰亚胺）的合成与表征。

Journal of Amino Acids Pub Date : 2010-01-01 Epub Date: 2010-07-13 DOI: 10.4061/2010/910906

Saeed Zahmatkesh, Mohammad Reza Vakili

引用次数: 0

Fluorine-tagged 5-hydroxytryptophan to investigate amino Acid metabolism in vivo. 氟标记的5-羟色氨酸研究体内氨基酸代谢。

Journal of Amino Acids Pub Date : 2010-01-01 Epub Date: 2010-05-19 DOI: 10.4061/2010/265069

Zofia E Gagnon, Sherry Dingman, Rhys N Thomas

引用次数: 0

Effects of (L)-cystine and (L)-theanine supplementation on the common cold: a randomized, double-blind, and placebo-controlled trial. 补充(L)-胱氨酸和(L)-茶氨酸对普通感冒的影响：随机、双盲和安慰剂对照试验。

Journal of Amino Acids Pub Date : 2010-01-01 Epub Date: 2010-05-12 DOI: 10.4061/2010/307475

Shigekazu Kurihara, Takenori Hiraoka, Masahisa Akutsu, Eiji Sukegawa, Makoto Bannai, Susumu Shibahara

引用次数: 0