Genome analysis reveals insights into physiology and longevity of the Brandt’s bat Myotis brandtii

Seim, Inge; Fang, Xiaodong; Xiong, Zhiqiang; Lobanov, Alexey V.; Huang, Zhiyong; Ma, Siming; Feng, Yue; Turanov, Anton A.; Zhu, Yabing; Lenz, Tobias L.; Gerashchenko, Maxim V.; Fan, Dingding; Yim, Sun Hee; Yao, Xiaoming; Jordan, Daniel M.; Xiong, Yingqi; Ma, Yan; Lyapunov, Andrey N.; Chen, Guanxing; Kulakova, O. I.; Sun, Yankuo; Lee, Sang Goo; Bronson, Roderick T.; Moskalev, Alexey; Sunyaev, Shamil; Zhang, Guojie; Krogh, Anders; Wang, Jun; Gladyshev, Vadim N.

doi:10.1038/ncomms3212

Cited by 230 publications

(242 citation statements)

References 60 publications

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“…However, changes in the amino acid sequence during evolution are concentrated in the N-terminal region of the TTR subunit, and produce variations in the length and hydropathy of amino acid sequence in the C-terminal region of TTR subunits as are also observed in some animal species including pig 3 and bats 4,5 . In a previous work, we demonstrated that the unstructured N-terminal region of TTR had effects on the affinity of the binding between TTR and TH 6 , and it also affected the binding of RBP to the binding site at the C-terminal region of TTR 7 .…”

Section: Discussionmentioning

confidence: 99%

“…The predominant changes in the TTRs from birds, reptiles, amphibians, and fishes are in the N-terminal region which is longer and more hydrophobic in the sequences compared to that in TTRs from mammals 1,2 . In addition, variations in the length of the C-terminal region of TTRs from pig 3 and microbats 4,5 compared with that from human have also been detected. The changes in length and hydrophobicity were demonstrated to affect the binding affinities of TTR for THs and retinol binding protein (RBP) 6,7 .…”

Section: Introductionmentioning

confidence: 97%

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Proteolytic activity of Crocodylus porosus transthyretin protease and role of the terminal polypeptide sequences

Leelawatwattana¹,

Praphanphoj²,

Prapunpoj³

2016

ScienceAsia

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Human transthyretin (TTR), a recently identified protease, participates in the biology of high density lipoprotein and in the nervous system. In the present study, we determined whether TTR from a non-mammal Crocodylus porosus (crocTTR) has proteolytic activity and whether the N-and C-termini of the TTR polypeptide affect the proteolytic activity. The proteolytic activity of crocTTR and three chimeric crocTTRs: xenoN/crocTTR (crocTTR in which the N-terminal sequence was replaced with that of Xenopus laevis TTR), pigC/crocTTR (crocTTR in which the C-terminal sequence was replaced with that of Sus scrofa TTR), and xenoN/pigC/crocTTR (crocTTR in which the N-and C-terminal sequences were replaced with that of X. laevis TTR and S. scrofa TTR, respectively) were studied and compared. Using either casein or apoAI as a substrate, crocTTR had a lower proteolytic activity than human TTR. Replacing the C-terminal sequence of crocTTR increased the activity (casein: 1008 ± 36 pmol/min; apoAI: 231 ± 43 pmol/min), whereas replacing the N-terminal sequence decreased the activity (casein: 299 ± 26 pmol/min; apoAI: 31.5 ± 2.0 pmol/min). The activity of xenoN/pigC/crocTTR (casein: 502 ± 11 pmol/min; apoAI: 371 ± 23 pmol/min) was higher than those of crocTTR or xenoN/crocTTR, but similar to that of pigC/crocTTR. These results are the first to show the proteolytic activity of reptile TTR, and that the activity is changed when the N-and/or C-terminal amino acid sequences of the TTR subunit are changed.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 97%

Proteolytic activity of Crocodylus porosus transthyretin protease and role of the terminal polypeptide sequences

Leelawatwattana¹,

Praphanphoj²,

Prapunpoj³

2016

ScienceAsia

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“…For hibernating mammals, this is reflected in seasonal changes in the expression of genes that regulate the carbohydrate to lipid switch, including the increased expression of pyruvate dehydrogenase kinase isoenzyme 4 (PDK4) which inhibits the conversion of the glycolytic product pyruvate to acetyl-CoA in the heart, white adipose tissue, and skeletal muscle (64,477). Other changes at the mRNA and/or protein levels that facilitate the switch from carbohydrate to lipid fuels during hibernation include increases in carnitine palmitoyltranserferase 1A (CPT1A), fatty acid binding protein 1 (FABP1), 3-hydroxy-3-methylglutaryl-CoA synthase (HMGCS2), fibroblast growth factor 21 (FGF21), and reductions in acetyl-CoA carboxylase 2 (ACACB), stearoyl-CoA desaturase (SCD), and elongation of very long chain fatty acids protein 6 (ELOVL6) (156,168,262,351,470,503,507,579,580).…”

Section: Lipidsmentioning

confidence: 99%

Integrative Physiology of Fasting

Secor

Carey

2016

Comprehensive Physiology

135

144

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Extended bouts of fasting are ingrained in the ecology of many organisms, characterizing aspects of reproduction, development, hibernation, estivation, migration, and infrequent feeding habits. The challenge of long fasting episodes is the need to maintain physiological homeostasis while relying solely on endogenous resources. To meet that challenge, animals utilize an integrated repertoire of behavioral, physiological, and biochemical responses that reduce metabolic rates, maintain tissue structure and function, and thus enhance survival. We have synthesized in this review the integrative physiological, morphological, and biochemical responses, and their stages, that characterize natural fasting bouts. Underlying the capacity to survive extended fasts are behaviors and mechanisms that reduce metabolic expenditure and shift the dependency to lipid utilization. Hormonal regulation and immune capacity are altered by fasting; hormones that trigger digestion, elevate metabolism, and support immune performance become depressed, whereas hormones that enhance the utilization of endogenous substrates are elevated. The negative energy budget that accompanies fasting leads to the loss of body mass as fat stores are depleted and tissues undergo atrophy (i.e., loss of mass). Absolute rates of body mass loss scale allometrically among vertebrates. Tissues and organs vary in the degree of atrophy and downregulation of function, depending on the degree to which they are used during the fast. Fasting affects the population dynamics and activities of the gut microbiota, an interplay that impacts the host's fasting biology. Fasting-induced gene expression programs underlie the broad spectrum of integrated physiological mechanisms responsible for an animal's ability to survive long episodes of natural fasting.

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“…The author will mention, although briefly, Gladyshev's contributions to the area of aging, including mechanisms of aging and control of lifespan, in addition to the application of redox biology to understanding aging discussed earlier. The Gladyshev lab also sequenced and characterized the genomes, transcriptomes, and/or metabolomes of several exceptionally long-lived mammals, most notably the naked mole rat, Brandt's bat, and bowhead whale (11,32,53,54), providing numerous insights into the biology of these animals, their adaptations, and the associated molecular mechanisms involved (many of which were related to selenium and redox biology) (Fig. 5).…”

Section: Mechanisms Of Thiol-based Redox Controlmentioning

confidence: 99%

Redox Pioneer: Professor Vadim N. Gladyshev

Hatfield

2016

Antioxidants & Redox Signaling

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Professor Vadim N. Gladyshev is recognized here as a Redox Pioneer, because he has published an article on antioxidant/redox biology that has been cited more than 1000 times and 29 articles that have been cited more than 100 times. Gladyshev is world renowned for his characterization of the human selenoproteome encoded by 25 genes, identification of the majority of known selenoprotein genes in the three domains of life, and discoveries related to thiol oxidoreductases and mechanisms of redox control. Gladyshev's first faculty position was in the Department of Biochemistry, the University of Nebraska. There, he was a Charles Bessey Professor and Director of the Redox Biology Center. He then moved to the Department of Medicine at Brigham and Women's Hospital, Harvard Medical School, where he is Professor of Medicine and Director of the Center for Redox Medicine. His discoveries in redox biology relate to selenoenzymes, such as methionine sulfoxide reductases and thioredoxin reductases, and various thiol oxidoreductases. He is responsible for the genome-wide identification of catalytic redox-active cysteines and for advancing our understanding of the general use of cysteines by proteins. In addition, Gladyshev has characterized hydrogen peroxide metabolism and signaling and regulation of protein function by methionine-R-sulfoxidation. He has also made important contributions in the areas of aging and lifespan control and pioneered applications of comparative genomics in redox biology, selenium biology, and aging. Gladyshev's discoveries have had a profound impact on redox biology and the role of redox control in health and disease. He is a true Redox Pioneer. Antioxid. Redox Signal. 25, 1-9.

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Genome analysis reveals insights into physiology and longevity of the Brandt’s bat Myotis brandtii

Cited by 230 publications

References 60 publications

Proteolytic activity of Crocodylus porosus transthyretin protease and role of the terminal polypeptide sequences

Proteolytic activity of Crocodylus porosus transthyretin protease and role of the terminal polypeptide sequences

Integrative Physiology of Fasting

Redox Pioneer: Professor Vadim N. Gladyshev

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