Critical Reviews in Biochemistry and Molecular Biology最新文献_第9页

Elastases and elastokines: elastin degradation and its significance in health and disease. 弹性蛋白酶和弹性因子:弹性蛋白降解及其在健康和疾病中的意义。

IF 6.5 2区生物学

Critical Reviews in Biochemistry and Molecular Biology Pub Date : 2020-06-01 Epub Date: 2020-06-12 DOI: 10.1080/10409238.2020.1768208

Andrea Heinz

{"title":"Elastases and elastokines: elastin degradation and its significance in health and disease.","authors":"Andrea Heinz","doi":"10.1080/10409238.2020.1768208","DOIUrl":"https://doi.org/10.1080/10409238.2020.1768208","url":null,"abstract":"Elastin is an important protein of the extracellular matrix of higher vertebrates, which confers elasticity and resilience to various tissues and organs including lungs, skin, large blood vessels and ligaments. Owing to its unique structure, extensive cross-linking and durability, it does not undergo significant turnover in healthy tissues and has a half-life of more than 70 years. Elastin is not only a structural protein, influencing the architecture and biomechanical properties of the extracellular matrix, but also plays a vital role in various physiological processes. Bioactive elastin peptides termed elastokines - in particular those of the GXXPG motif - occur as a result of proteolytic degradation of elastin and its non-cross-linked precursor tropoelastin and display several biological activities. For instance, they promote angiogenesis or stimulate cell adhesion, chemotaxis, proliferation, protease activation and apoptosis. Elastin-degrading enzymes such as matrix metalloproteinases, serine proteases and cysteine proteases slowly damage elastin over the lifetime of an organism. The destruction of elastin and the biological processes triggered by elastokines favor the development and progression of various pathological conditions including emphysema, chronic obstructive pulmonary disease, atherosclerosis, metabolic syndrome and cancer. This review gives an overview on types of human elastases and their action on human elastin, including the formation, structure and biological activities of elastokines and their role in common biological processes and severe pathological conditions.","PeriodicalId":10794,"journal":{"name":"Critical Reviews in Biochemistry and Molecular Biology","volume":"55 3","pages":"252-273"},"PeriodicalIF":6.5,"publicationDate":"2020-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/10409238.2020.1768208","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"38037537","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 71

Substrate specificity of polyphenol oxidase. 多酚氧化酶的底物特异性。

IF 6.5 2区生物学

Critical Reviews in Biochemistry and Molecular Biology Pub Date : 2020-06-01 Epub Date: 2020-05-22 DOI: 10.1080/10409238.2020.1768209

Mark-Anthony McLarin, Ivanhoe K H Leung

{"title":"Substrate specificity of polyphenol oxidase.","authors":"Mark-Anthony McLarin, Ivanhoe K H Leung","doi":"10.1080/10409238.2020.1768209","DOIUrl":"https://doi.org/10.1080/10409238.2020.1768209","url":null,"abstract":"The ubiquitous type-3 copper enzyme polyphenol oxidase (PPO) has found itself the subject of profound inhibitor research due to its role in fruit and vegetable browning and mammalian pigmentation. The enzyme itself has also been applied in the fields of bioremediation, biocatalysis and biosensing. However, the nature of PPO substrate specificity has remained elusive despite years of study. Numerous theories have been proposed to account for the difference in tyrosinase and catechol oxidase activity. The \"blocker residue\" theory suggests that bulky residues near the active site cover CuA, preventing monophenol coordination. The \"second shell\" theory suggests that residues distant (∼8 Å) from the active site, guide and position substrates within the active site based on their properties e.g., hydrophobic, electrostatic. It is also hypothesized that binding specificity is related to oxidation mechanisms of the catalytic cycle, conferred by coordination of a conserved water molecule by other conserved residues. In this review, we highlight recent developments in the structural and mechanistic studies of PPOs and consolidate key concepts in our understanding toward the substrate specificity of PPOs.","PeriodicalId":10794,"journal":{"name":"Critical Reviews in Biochemistry and Molecular Biology","volume":"55 3","pages":"274-308"},"PeriodicalIF":6.5,"publicationDate":"2020-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/10409238.2020.1768209","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"37965260","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 31

Mechanisms of mutagenesis induced by DNA lesions: multiple factors affect mutations in translesion DNA synthesis. DNA损伤诱导突变的机制:多种因素影响翻译DNA合成中的突变。

IF 6.5 2区生物学

Critical Reviews in Biochemistry and Molecular Biology Pub Date : 2020-06-01 Epub Date: 2020-05-24 DOI: 10.1080/10409238.2020.1768205

Huidong Zhang

{"title":"Mechanisms of mutagenesis induced by DNA lesions: multiple factors affect mutations in translesion DNA synthesis.","authors":"Huidong Zhang","doi":"10.1080/10409238.2020.1768205","DOIUrl":"https://doi.org/10.1080/10409238.2020.1768205","url":null,"abstract":"Environmental mutagens lead to mutagenesis. However, the mechanisms are very complicated and not fully understood. Environmental mutagens produce various DNA lesions, including base-damaged or sugar-modified DNA lesions, as well as epigenetically modified DNA. DNA polymerases produce mutation spectra in translesion DNA synthesis (TLS) through misincorporation of incorrect nucleotides, frameshift deletions, blockage of DNA replication, imbalance of leading- and lagging-strand DNA synthesis, and genome instability. Motif or subunit in DNA polymerases further affects the mutations in TLS. Moreover, protein interactions and accessory proteins in DNA replisome also alter mutations in TLS, demonstrated by several representative DNA replisomes. Finally, in cells, multiple DNA polymerases or cellular proteins collaborate in TLS and reduce in vivo mutagenesis. Summaries and perspectives were listed. This review shows mechanisms of mutagenesis induced by DNA lesions and the effects of multiple factors on mutations in TLS in vitro and in vivo.","PeriodicalId":10794,"journal":{"name":"Critical Reviews in Biochemistry and Molecular Biology","volume":"55 3","pages":"219-251"},"PeriodicalIF":6.5,"publicationDate":"2020-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/10409238.2020.1768205","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"37968252","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 5

Retinol-binding protein 2 (RBP2): biology and pathobiology. 视黄醇结合蛋白2 (RBP2):生物学和病理生物学。

IF 6.5 2区生物学

Critical Reviews in Biochemistry and Molecular Biology Pub Date : 2020-04-01 Epub Date: 2020-05-28 DOI: 10.1080/10409238.2020.1768207

William S Blaner, Pierre-Jacques Brun, Rossana M Calderon, Marcin Golczak

{"title":"Retinol-binding protein 2 (RBP2): biology and pathobiology.","authors":"William S Blaner, Pierre-Jacques Brun, Rossana M Calderon, Marcin Golczak","doi":"10.1080/10409238.2020.1768207","DOIUrl":"https://doi.org/10.1080/10409238.2020.1768207","url":null,"abstract":"Retinol-binding protein 2 (RBP2; originally cellular retinol-binding protein, type II (CRBPII)) is a 16 kDa cytosolic protein that in the adult is localized predominantly to absorptive cells of the proximal small intestine. It is well established that RBP2 plays a central role in facilitating uptake of dietary retinoid, retinoid metabolism in enterocytes, and retinoid actions locally within the intestine. Studies of mice lacking Rbp2 establish that Rbp2 is not required in times of dietary retinoid-sufficiency. However, in times of dietary retinoid-insufficiency, the complete lack of Rbp2 gives rise to perinatal lethality owing to RBP2 absence in both placental (maternal) and neonatal tissues. Moreover, when maintained on a high-fat diet, Rbp2-knockout mice develop obesity, glucose intolerance and a fatty liver. Unexpectedly, recent investigations have demonstrated that RBP2 binds long-chain 2-monoacylglycerols (2-MAGs), including the canonical endocannabinoid 2-arachidonoylglycerol, with very high affinity, equivalent to that of retinol binding. Crystallographic studies establish that 2-MAGs bind to a site within RBP2 that fully overlaps with the retinol binding site. When challenged orally with fat, mucosal levels of 2-MAGs in Rbp2 null mice are significantly greater than those of matched controls establishing that RBP2 is a physiologically relevant MAG-binding protein. The rise in MAG levels is accompanied by elevations in circulating levels of the hormone glucose-dependent insulinotropic polypeptide (GIP). It is not understood how retinoid and/or MAG binding to RBP2 affects the functions of this protein, nor is it presently understood how these contribute to the metabolic and hormonal phenotypes observed for Rbp2-deficient mice.","PeriodicalId":10794,"journal":{"name":"Critical Reviews in Biochemistry and Molecular Biology","volume":"55 2","pages":"197-218"},"PeriodicalIF":6.5,"publicationDate":"2020-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/10409238.2020.1768207","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"37986193","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 17

Phosphatidylserine exposure in living cells. 活细胞中的磷脂酰丝氨酸暴露。

IF 6.5 2区生物学

Critical Reviews in Biochemistry and Molecular Biology Pub Date : 2020-04-01 Epub Date: 2020-05-14 DOI: 10.1080/10409238.2020.1758624

Hye-Won Shin, Hiroyuki Takatsu

引用次数: 35

Protease propeptide structures, mechanisms of activation, and functions. 蛋白酶前肽的结构、活化机制和功能。

IF 6.5 2区生物学

Critical Reviews in Biochemistry and Molecular Biology Pub Date : 2020-04-01 Epub Date: 2020-04-14 DOI: 10.1080/10409238.2020.1742090

Lise Boon, Estefania Ugarte-Berzal, Jennifer Vandooren, Ghislain Opdenakker

{"title":"Protease propeptide structures, mechanisms of activation, and functions.","authors":"Lise Boon, Estefania Ugarte-Berzal, Jennifer Vandooren, Ghislain Opdenakker","doi":"10.1080/10409238.2020.1742090","DOIUrl":"https://doi.org/10.1080/10409238.2020.1742090","url":null,"abstract":"Proteases are a diverse group of hydrolytic enzymes, ranging from single-domain catalytic molecules to sophisticated multi-functional macromolecules. Human proteases are divided into five mechanistic classes: aspartate, cysteine, metallo, serine and threonine proteases, based on the catalytic mechanism of hydrolysis. As a protective mechanism against uncontrolled proteolysis, proteases are often produced and secreted as inactive precursors, called zymogens, containing inhibitory N-terminal propeptides. Protease propeptide structures vary considerably in length, ranging from dipeptides and propeptides of about 10 amino acids to complex multifunctional prodomains with hundreds of residues. Interestingly, sequence analysis of the different protease domains has demonstrated that propeptide sequences present higher heterogeneity compared with their catalytic domains. Therefore, we suggest that protease inhibition targeting propeptides might be more specific and have less off-target effects than classical inhibitors. The roles of propeptides, besides keeping protease latency, include correct folding of proteases, compartmentalization, liganding, and functional modulation. Changes in the propeptide sequence, thus, have a tremendous impact on the cognate enzymes. Small modifications of the propeptide sequences modulate the activity of the enzymes, which may be useful as a therapeutic strategy. This review provides an overview of known human proteases, with a focus on the role of their propeptides. We review propeptide functions, activation mechanisms, and possible therapeutic applications.","PeriodicalId":10794,"journal":{"name":"Critical Reviews in Biochemistry and Molecular Biology","volume":"55 2","pages":"111-165"},"PeriodicalIF":6.5,"publicationDate":"2020-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/10409238.2020.1742090","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"37836293","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 32

Architecture of the IFT ciliary trafficking machinery and interplay between its components. IFT辅助贩运机制的体系结构及其组成部分之间的相互作用。

IF 6.5 2区生物学

Critical Reviews in Biochemistry and Molecular Biology Pub Date : 2020-04-01 Epub Date: 2020-05-26 DOI: 10.1080/10409238.2020.1768206

Kazuhisa Nakayama, Yohei Katoh

{"title":"Architecture of the IFT ciliary trafficking machinery and interplay between its components.","authors":"Kazuhisa Nakayama, Yohei Katoh","doi":"10.1080/10409238.2020.1768206","DOIUrl":"https://doi.org/10.1080/10409238.2020.1768206","url":null,"abstract":"Cilia and flagella serve as cellular antennae and propellers in various eukaryotic cells, and contain specific receptors and ion channels as well as components of axonemal microtubules and molecular motors to achieve their sensory and motile functions. Not only the bidirectional trafficking of specific proteins within cilia but also their selective entry and exit across the ciliary gate is mediated by the intraflagellar transport (IFT) machinery with the aid of motor proteins. The IFT-B complex, which is powered by the kinesin-2 motor, mediates anterograde protein trafficking from the base to the tip of cilia, whereas the IFT-A complex together with the dynein-2 complex mediates retrograde protein trafficking. The BBSome complex connects ciliary membrane proteins to the IFT machinery. Defects in any component of this trafficking machinery lead to abnormal ciliogenesis and ciliary functions, and results in a broad spectrum of disorders, collectively called the ciliopathies. In this review article, we provide an overview of the architectures of the components of the IFT machinery and their functional interplay in ciliary protein trafficking.","PeriodicalId":10794,"journal":{"name":"Critical Reviews in Biochemistry and Molecular Biology","volume":"55 2","pages":"179-196"},"PeriodicalIF":6.5,"publicationDate":"2020-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/10409238.2020.1768206","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"37978007","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 42

The implication of the SUMOylation pathway in breast cancer pathogenesis and treatment. SUMOylation通路在乳腺癌发病和治疗中的意义。

IF 6.5 2区生物学

Critical Reviews in Biochemistry and Molecular Biology Pub Date : 2020-02-01 Epub Date: 2020-03-18 DOI: 10.1080/10409238.2020.1738332

Andrea Rabellino, Kum Kum Khanna

{"title":"The implication of the SUMOylation pathway in breast cancer pathogenesis and treatment.","authors":"Andrea Rabellino, Kum Kum Khanna","doi":"10.1080/10409238.2020.1738332","DOIUrl":"https://doi.org/10.1080/10409238.2020.1738332","url":null,"abstract":"Breast cancer is the most commonly diagnosed malignancy in woman worldwide, and is the second most common cause of death in developed countries. The transformation of a normal cell into a malignant derivate requires the acquisition of diverse genomic and proteomic changes, including enzymatic post-translational modifications (PTMs) on key proteins encompassing critical cell signaling events. PTMs occur on proteins after translation, and regulate several aspects of proteins activity, including their localization, activation and turnover. Deregulation of PTMs can potentially lead to tumorigenesis, and several de-regulated PTM pathways contribute to abnormal cell proliferation during breast tumorigenesis. SUMOylation is a PTM that plays a pivotal role in numerous aspects of cell physiology, including cell cycle regulation, protein trafficking and turnover, and DNA damage repair. Consistently with this, the deregulation of the SUMO pathway is observed in different human pathologies, including breast cancer. In this review we will describe the role of SUMOylation in breast tumorigenesis and its implication for breast cancer therapy.","PeriodicalId":10794,"journal":{"name":"Critical Reviews in Biochemistry and Molecular Biology","volume":"55 1","pages":"54-70"},"PeriodicalIF":6.5,"publicationDate":"2020-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/10409238.2020.1738332","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"37747420","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 10

Transcription factors and transporters in zinc homeostasis: lessons learned from fungi. 锌稳态中的转录因子和转运体:从真菌中获得的经验教训。

IF 6.5 2区生物学

Critical Reviews in Biochemistry and Molecular Biology Pub Date : 2020-02-01 Epub Date: 2020-03-19 DOI: 10.1080/10409238.2020.1742092

David J Eide

{"title":"Transcription factors and transporters in zinc homeostasis: lessons learned from fungi.","authors":"David J Eide","doi":"10.1080/10409238.2020.1742092","DOIUrl":"https://doi.org/10.1080/10409238.2020.1742092","url":null,"abstract":"Zinc is an essential nutrient for all organisms because this metal serves as a critical structural or catalytic cofactor for many proteins. These zinc-dependent proteins are abundant in the cytosol as well as within organelles of eukaryotic cells such as the nucleus, mitochondria, endoplasmic reticulum, Golgi, and storage compartments such as the fungal vacuole. Therefore, cells need zinc transporters so that they can efficiently take up the metal and move it around within cells. In addition, because zinc levels in the environment can vary drastically, the activity of many of these transporters and other components of zinc homeostasis is regulated at the level of transcription by zinc-responsive transcription factors. Mechanisms of post-transcriptional control are also important for zinc homeostasis. In this review, the focus will be on our current knowledge of zinc transporters and their regulation by zinc-responsive transcription factors and other mechanisms in fungi because these organisms have served as useful paradigms of zinc homeostasis in all organisms. With this foundation, extension to other organisms will be made where warranted.","PeriodicalId":10794,"journal":{"name":"Critical Reviews in Biochemistry and Molecular Biology","volume":"55 1","pages":"88-110"},"PeriodicalIF":6.5,"publicationDate":"2020-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/10409238.2020.1742092","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"37755044","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 22

Spatial control of AMPK signaling at subcellular compartments. 亚细胞区室中AMPK信号的空间控制。

IF 6.5 2区生物学

Critical Reviews in Biochemistry and Molecular Biology Pub Date : 2020-02-01 Epub Date: 2020-02-18 DOI: 10.1080/10409238.2020.1727840

Anoop Singh Chauhan, Li Zhuang, Boyi Gan

引用次数: 22