Journal Home > Volume 3 , Issue 3-4

The energy substances (mainly carbohydrates and fats) are the basis and guarantee of life activity, especially the oxidative phosphorylation for energy supply. However, excessive absorption and accumulation of these substances can lead to metabolic diseases such as obesity, hyperlipidemia, diabetes, and cancers. A large amount of studies demonstrate that G protein-coupled receptors (GPCRs) play a key role in identification and absorption of energy substances, and the signaling network of nerves, immune, and endocrine regulates their storage and utilization. The gastrointestinal mucus layer not only identifies these substances through identification in diet components but also transfers immune, metabolic, and endocrine signals of hormones, cytokines, and chemokines by promoting interactions between receptors and ligands. These signaling molecules are transferred to corresponding organs, tissues, and cells by the circulatory system, and cell activity is regulated by amplifying of cell signals that constitute the wireless communication network among cells in the body. Absorption, accumulation, and utilization of energy substances in the body obey the law of energy conservation. Energy is stored in the form of fat, and meets the demand of body via two coupled mechanisms: catabolism and oxidative phosphorylation. Under normal physiological conditions, fat consumption involves ketone body metabolism through the circulatory system and glucose consumption requires blood lactic acid cycle. Accumulation of excessive energy leads to the abnormal activation of mammalian target of rapamycin (mTOR), thus promoting the excretion of glucose or glycogen in the form of blood glucose and urine glucose. Alternatively, the body cancels the intercellular contact inhibition and promotes cell proliferation to induce carcinogenesis, which can induce the consumption of large amounts of glucose. Intercellular communication is performed by signaling molecules via sensing, absorption, accumulation, and utilization of energy substances, and anabolism and catabolism are controlled by the central metabolic pathway. Therefore, slower catabolism will result in longer life expectancy, whereas faster catabolism results in shorter life expectancy. Energy substances in diet influence the balance between energy and metabolism in the body through the sensing function of the gastrointestinal system at two levels: cellular communication network and metabolic network. The present review of studies aims to strengthen our knowledge on cellular communication and metabolic networks to offer a dietary guidance on the metabolism and communication role of various foods.


menu
Abstract
Full text
Outline
About this article

Energy intake, metabolic homeostasis, and human health

Show Author's information Guangchang Pang( )Junbo XieQingsen ChenZhihe Hu
Tianjin Key Laboratory of Food Biotechnology, College of Biotechnology and Food Science, Tianjin University of Commerce, Tianjin 300134, China

Peer review under responsibility of Beijing Academy of Food Sciences.

Abstract

The energy substances (mainly carbohydrates and fats) are the basis and guarantee of life activity, especially the oxidative phosphorylation for energy supply. However, excessive absorption and accumulation of these substances can lead to metabolic diseases such as obesity, hyperlipidemia, diabetes, and cancers. A large amount of studies demonstrate that G protein-coupled receptors (GPCRs) play a key role in identification and absorption of energy substances, and the signaling network of nerves, immune, and endocrine regulates their storage and utilization. The gastrointestinal mucus layer not only identifies these substances through identification in diet components but also transfers immune, metabolic, and endocrine signals of hormones, cytokines, and chemokines by promoting interactions between receptors and ligands. These signaling molecules are transferred to corresponding organs, tissues, and cells by the circulatory system, and cell activity is regulated by amplifying of cell signals that constitute the wireless communication network among cells in the body. Absorption, accumulation, and utilization of energy substances in the body obey the law of energy conservation. Energy is stored in the form of fat, and meets the demand of body via two coupled mechanisms: catabolism and oxidative phosphorylation. Under normal physiological conditions, fat consumption involves ketone body metabolism through the circulatory system and glucose consumption requires blood lactic acid cycle. Accumulation of excessive energy leads to the abnormal activation of mammalian target of rapamycin (mTOR), thus promoting the excretion of glucose or glycogen in the form of blood glucose and urine glucose. Alternatively, the body cancels the intercellular contact inhibition and promotes cell proliferation to induce carcinogenesis, which can induce the consumption of large amounts of glucose. Intercellular communication is performed by signaling molecules via sensing, absorption, accumulation, and utilization of energy substances, and anabolism and catabolism are controlled by the central metabolic pathway. Therefore, slower catabolism will result in longer life expectancy, whereas faster catabolism results in shorter life expectancy. Energy substances in diet influence the balance between energy and metabolism in the body through the sensing function of the gastrointestinal system at two levels: cellular communication network and metabolic network. The present review of studies aims to strengthen our knowledge on cellular communication and metabolic networks to offer a dietary guidance on the metabolism and communication role of various foods.

Keywords: Metabolic syndrome, Human health, Energy substance, Metabolism balance, Wireless intercellular communication network, Metabolic network

References(141)

[1]

F. Reimann, G. Tolhurst, F.M. Gribble, G-protein-coupled receptors in intestinal chemosensation, Cell Metab. 15 (2012) 421-431.

[2]

M. Laplante, D.M. Sabatini, mTOR signaling in growth control and disease, Cell 149 (2012) 274-293.

[3]

G. Pang, Q. Chen, Z. Hu, et al., The “five flavor conciliation”, and nutrient balance and their signal transductions, Food Sci. 33 (13) (2012) 1-20.

[4]

F. Laugerette, P. Passilly-degrace, B. Patris, et al., CD36 involvement in orosensory detection of dietary lipids, spontaneous fat preference, and digestive secretions, J. Clin. Invest. 115 (2005) 3177-3184.

[5]

N. Chaudhari, S.D. Roper, The cell biology of taste, J. Cell Biol. 190 (2010) 285-296.

[6]

W. Meyerhof, C. Batram, C. Kuhn, et al., The molecular receptive ranges of human TAS2R bitter taste receptors, Chem. Senses 35 (2010) 157-170.

[7]

C. Cartoni, K. Yasumatsu, T. Ohkuri, et al., Taste preference for fatty acids is mediated by GPR40 and GPR120, J. Neurosci. 30 (2010) 8376-8382.

[8]

G.T. Wong, K.S. Gannon, F. Robert, Transduction of bitter and sweet taste by gustducin, Nature 381 (1996) 796-800.

[9]

S. Janssen, I. Depoortere, Nutrient sensing in the gut: new roads to therapeutics? Trends Endocrinol. Metab. 24 (2) (2013) 92-100.

[10]

M.S. Engelstoft, K.L. Egerod, B. Holst, et al., A gut feeling for obesity: 7TM sensors on enteroendocrine cells, Cell Metab. 8 (2008) 447-449.

[11]

H.R. Berthoud, M. Kressel, H.E. Raybould, et al., Vagal sensors in the rat duodenal mucosa: distribution and structure as revealed by in vivo DiI-tracing, Anat. Embryol. 191 (1995) 203-212.

[12]

T.E. Finger, B. Böttger, A. Hansen, et al., Solitary chemoreceptor cells in the nasal cavity serve as sentinels of respiration, Proc. Natl. Acad. Sci. U.S.A. 100 (2003) 8981-8986.

[13]

S. Janssen, J. Laermans, P.J. Verhulst, et al., Bitter taste receptors and alpha-gustducin regulate the secretion of ghrelin with functional effects on food intake and gastric emptying, Proc. Natl. Acad. Sci. U.S.A. 108 (2011) 2094-2099.

[14]

O.J. Mace, J. Affleck, N. Patel, et al., Sweet taste receptors in rat small intestine stimulate glucose absorption through apical GLUT2, J. Physiol. 582 (2007) 379-392.

[15]

G.A. Bewick, Bowels control brain: gut hormones and obesity, Biochem. Med. 22 (3) (2012) 283-297.

[16]

I.M. Brennan, N.D. Luscombe-Marsh, R.V. Seimon, et al., Effects of fat, protein, and carbohydrate and protein load on appetite, plasma cholecystokinin, peptide YY, and ghrelin, and energy intake in lean and obese men, Am. J. Physiol. Gastrointest. Liver Physiol. 303 (2012) G129-G140.

[17]

N. Hass, K. Schwarzenbacher, H. Breer, T1R3 is expressed in brush cells and ghrelin producing cells of murine stomach, Cell Tissue Res. 339 (2010) 493-504.

[18]

K. Iwatsuki, M. Nomura, A. Shibata, et al., Generation and characterization of T1R2-LacZ knock-in mouse, Biochem. Biophys. Res. Commun. 402 (2010) 495-499.

[19]

G. Nelson, J. Chandrashekar, M.A. Hoon, et al., An amino-acid taste receptor, Nature 416 (2002) 199-202.

[20]

Y. Akiba, C. Watanabe, M. Mizumori, et al., Luminal l-glutamate enhances duodenal mucosal defense mechanisms via multiple glutamate receptors in rats, Am. J. Physiol. Gastrointest. Liver Physiol. 297 (2009) G781-G791.

[21]

D.C. Haid, C. Jordan-Biegger, P. Widmayer, et al., Receptors responsive to protein breakdown products in G-cells and D-cells of mouse, swine and human, Front. Physiol. 3 (2012) 65-80.

[22]

A.P. Liou, Y. Sei, X. Zhao, et al., The extracellular calcium-sensing receptor is required for cholecystokinin secretion in response to L-phenylalanine in acutely isolated intestinal I cells, Am. J. Physiol. Gastrointest. Liver Physiol. 300 (2011) G538-G546.

[23]

A.B. Ballinger, M.L. Clark, l-Phenylalanine releases cholecystokinin (CCK) and is associated with reduced food intake in humans: evidence for a physiological role of CCK in control of eating, Metabolism 43 (1994) 735-738.

[24]

P. Wellendorph, H. Bräuner-Osborne, Molecular basis for amino acid sensing by family C G-protein-coupled receptors, Br. J. Pharmacol. 156 (2009) 869-884.

[25]

D. Haid, P. Widmayer, H. Breer, Nutrient sensing receptors in gastric endocrine cells, J. Mol. Histol. 42 (2011) 355-364.

[26]

S. Choi, M. Lee, A.L. Shiu, et al., Identification of a protein hydrolysate responsive G protein-coupled receptor in enterocytes, Am. J. Physiol. Gastrointest. Liver Physiol. 292 (2007) G98-G112.

[27]

M. Cordier-bussat, C. Bernard, F. Levenez, et al., Peptones stimulate both the secretion of the incretin hormone glucagon-like peptide 1 and the transcription of the proglucagon gene, Diabetes 47 (1998) 1038-1045.

[28]

N.P. Darcel, A.P. Liou, D. Tomé, et al., Activation of vagal afferents in the rat duodenum by protein digests requires PepT1, J. Nutr. 135 (2005) 1491-1495.

[29]

O.J. Mace, N. Lister, E. Morgan, et al., An energy supply network of nutrient absorption coordinated by calcium and T1R taste receptors in rat small intestine, J. Physiol. 587 (2009) 195-210.

[30]

S. Edfalk, P. Steneberg, H. Edlund, Gpr40 is expressed in enteroendocrine cells and mediates free fatty acid stimulation of incretin secretion, Diabetes 57 (2008) 2280-2287.

[31]

T. Tanaka, T. Yano, T. Adachi, et al., Cloning and characterization of the rat free fatty acid receptor GPR120: in vivo effect of the natural ligand on GLP-1 secretion and proliferation of pancreatic beta cells, Naunyn Schmiedebergs Arch. Pharmacol. 377 (2008) 515-522.

[32]

A.J. Brown, S.M. Goldsworthy, A.A. Barnes, et al., The orphan G protein-coupled receptors GPR41 and GPR43 are activated by propionate and other short chain carboxylic acids, J. Biol. Chem. 278 (2003) 11312-11319.

[33]

G. Tolhurst, H. Heffron, Y.S. Lam, et al., Short-chain fatty acids stimulate glucagonlike peptide-1 secretion via the G-protein-coupled receptor FFAR2, Diabetes 61 (2012) 364-371.

[34]

H.M. Cox, I.R. Tough, A.M. Woolston, et al., Peptide YY is critical for acylethanolamine receptor Gpr119-induced activation of gastrointestinal mucosal responses, Cell Metab. 11 (2010) 532-542.

[35]

H.A. Overton, A.J. Babbs, S.M. Doel, et al., Deorphanization of a G protein-coupled receptor for oleoylethanolamide and its use in the discovery of small molecule hypophagic agents, Cell Metab. 3 (2006) 167-175.

[36]

C.D. Dotson, M.C. Geraedts, S.D. Munger, Peptide regulators of peripheral taste function, Semin. Cell Dev. Biol. 24 (3) (2013) 232-239.

[37]

A. Acosta, M.D. Hurtado, O. Gorbatyuk, et al., Salivary PYY: a putative bypass to satiety, PLoS ONE 6 (2011) e26137.

[38]

B. Martin, Y.K. Shin, C.M. White, et al., Vasoactive intestinal peptide-null mice demonstrate enhanced sweet taste preference, dysglycemia, and reduced taste bud leptin receptor expression, Diabetes 59 (2010) 1143-1152.

[39]

S. Herness, F.L. Zhao, The neuropeptides CCK and NPY and the changing view of cell-to-cell communication in the taste bud, Physiol. Behav. 97 (2009) 581-591.

[40]

A.C. Shin, R.L. Townsend, L.M. Patterson, et al., “Liking” and “wanting” of sweet and oily food stimuli as affected by high-fat diet-induced obesity, weight loss, leptin, and genetic predisposition, Am. J. Physiol.: Regul. Integr. Comp. Physiol. 301 (2011) R1267-R1280.

[41]

L.L. Baggio, D.J. Drucker, Biology of incretins: GLP-1 and GIP, Gastroenterology 132 (2007) 2131-2157.

[42]

P.L. Brubaker, The glucagon-like peptides: pleiotropic regulators of nutrient homeostasis, Ann. N. Y. Acad. Sci. 1070 (2006) 10-26.

[43]

C. Martin, P. Passilly-Degrace, M. Chevrot, et al., Lipid-mediated release of GLP-1 by mouse taste buds from circumvallate papillae: putative involvement of GPR120 and impact on taste sensitivity, J. Lipid Res. 53 (2012) 2256-2265.

[44]

R.H. Unger, A.D. Cherrington, Glucagonocentric restructuring of diabetes: a pathophysiologic and therapeutic makeover, J. Clin. Invest. 122 (2012) 4-12.

[45]

R.W. Gelling, P.M. Vuguin, X.Q. DU., Pancreatic beta-cell overexpression of the glucagon receptor gene results in enhanced beta-cell function and mass, Am. J. Physiol.: Endocrinol. Metab. 297 (2009) E695-E707.

[46]

A.E. Elson, C.D. Dotson, J.M. Egan, et al., Glucagon signaling modulates sweet taste responsiveness, FASEB J. 24 (2010) 3960-3969.

[47]

T.W. Moody, T. Ito, N.J. Osefo, et al., PACAP: recent insights into their functions/roles in physiology and disease from molecular and genetic studies, Curr. Opin. Endocrinol. Diabetes Obes. 18 (2011) 61-67.

[48]

L. Dickson, K. Finlayson, VPAC and PAC receptors: from ligands to function, Pharmacol. Therapeut. 121 (2009) 294-316.

[49]

A. Inui, A. Asakawa, C.Y. Bowers, et al., Ghrelin, appetite, and gastric motility: the emerging role of the stomach as an endocrine organ, FASEB J. 18 (2004) 439-456.

[50]

T. Sato, Y. Nakamura, Y. Shiimura, et al., Structure, regulation and function of ghrelin, J. Biochem. 151 (2012) 119-128.

[51]

K.E. Smith, M.W. Walker, R. Artymyshyn, et al., Cloned human and rat galanin GALR3 receptors Pharmacology and activation of G-protein inwardly rectifying K+ channels, J. Biol. Chem. 273 (1998) 23321-23326.

[52]

N.V. Dipatrizio, D. Piomelli, The thrifty lipids: endocannabinoids and the neural control of energy conservation, Trends Neurosci. 20 (2012) 1-9.

[53]

P. Degrace-Passilly, P. Besnard, CD36 and taste of fat, Curr. Opin. Clin. Nutr. Metab. Care 15 (2012) 107-111.

[54]

D. Greenberg, G.P. Smith, The controls of fat intake, Psychosom. Med. 58 (1996) 559-569.

[55]

C.J. Newman, E. Verdin, Ketone bodies as signaling metabolites, Trends Endocrinol. Metab. 25 (1) (2014) 42-52.

[56]

A. Oetting, P.M. Yen, New insights into thyroid hormone action, Best Pract. Res. Clin. Endocrinol. Metab. 21 (2007) 193-208.

[57]

N. Mitro, P.A. Mak, L. Vargas, et al., The nuclear receptor LXR is a glucose sensor, Nature 445 (2006) 219-223.

[58]

M.A. Lazar, T.M. Wilson, Sweet dreams for LXR, Cell Metab. 5 (2007) 159-161.

[59]

S. Jitrapakdee, Transcription factors and coactivators controlling nutrient and hormonal regulation of hepatic gluconeogenesis, Int. J. Biochem. Cell Biol. 44 (2012) 33-45.

[60]

F. Authier, B. Desbuquois, glucagon receptors, Cell Mol. Life Sci. 65 (2008) 1880-1899.

[61]

S.H. Koo, L. Flechner, L. Qi, et al., The CREB coactivator TORC2 is a key regulator of fasting glucose metabolism, Nature 437 (2005) 1109-1111.

[62]

Y. Liu, R. Dentin, D. Chen, et al., A fasting inducible switch modulates gluconeogenesis via activator/coactivator exchange, Nature 456 (2008) 269-273.

[63]

B.L. Skidmore, M.T. Jones, M. Blegen, et al., Matthews, acute effects of three different circuit weight training protocols on blood lactate, heart rate, and rating of perceived exertion in recreationally active women, J. Sports Sci. Med. 11 (2012) 660-668.

[64]

M.L. Goodwin, J.E. Harris, A. Hernández, et al., Blood lactate measurements and analysis during exercise: a guide for clinicians, J. Diabetes Sci. Technol. 1 (4) (2007) 558-569.

[65]

C.O. Mattern, M.J. Gutilla, D.L. Bright, et al., Maximal lactate steady state declines during the aging process, J. Appl. Physiol. 95 (2003) 2576-2582.

[66]

N. Draoui, O. Feron, Lactate shuttles at a glance: from physiological paradigms to anti-cancer treatments, Dis. Models Mech. 4 (2011) 727-732.

[67]

J. Kim, C.V. Dang, Cancer's molecular sweet tooth and the Warburg effect, Cancer Res. 66 (18) (2006) 8927-8930.

[68]

M. Drent, N.A. Cobben, R.F. Henderson, et al., Usefulness of lactate dehydrogenase and its isoenzymes as indicators of lung damage or inflammation, Eur. Respir. J. 9 (1996) 1736-1742.

[69]

A. Halestrap, D. Meredith, The SLC16 gene family-from monocarboxylate transporters (MCTs) to aromatic amino acid transporters and beyond, Pflugers Arch. Eur. J. Physiol. 447 (2004) 619-628.

[70]

F. Boussouar, M. Benahmed, Lactate and energy metabolism in male germ cells, Trends Endocrinol. Metab. 15 (2004) 345-350.

[71]

K. Caesar, P. Hashemi, A. Douhou, et al., Glutamate receptor-dependent increments in lactate, glucose and oxygen metabolism evoked in rat cerebellum in vivo, J. Physiol. 586 (5) (2008) 1337-1349.

[72]

L.T. Costa, D. Da Silva, C.R. Guimarães, et al., Lactate favours the dissociation of skeletal muscle 6-phosphofructo-1-kinase tetramers down-regulating the enzyme and muscle glycolysis, Biochem. J. 408 (2007) 123-130.

[73]

M. Chari, C.K.L. Lam, P.Y.T. Wang, et al., Activation of central lactate metabolism lowers glucose production in uncontrolled diabetes and diet-induced insulin resistance, Diabetes 57 (4) (2008) 836-840.

[74]

D. Allen, H. Westerblad, Lactic acid-the latest performance-enhancing drug, Science 305 (2004) 1112-1113.

[75]

A. Philp, L.A. Macdonald, P.W. Watt, Lactate – a signal coordinating cell and systemic function, J. Exp. Biol. 208 (2005) 4561-4575.

[76]

M.J. MacDonald, M.J. Longacre, S.W. Stoker, et al., Acetoacetate and β-hydroxybutyrate in combination with other metabolites release insulin from INS-1 cells and provide clues about pathways in insulin secretion, Am. J. Physiol. Cell Physiol. 294 (2008) C442-C450.

[77]

K. Mori, Y. Nakaya, S. Sakamoto, et al., Lactate-induced vascular relaxation in porcine coronary arteries is mediated by Ca21-activated K1 channels, J. Mol. Cell Cardiol. 30 (1998) 349-356.

[78]

O. Trabold, S. Wagner, C. Wicke, et al., Lactate and oxygen constitute a fundamental regulatory mechanism in wound healing, Wound. Repair Regen. 11 (2003) 504-509.

[79]

D.J. Samuvel, K.P. Sundararaj, A. Nareika, et al., Lactate boosts TLR4 signaling and NF-κB pathway-mediated gene transcription in macrophages via monocarboxylate transporters and MD-2 up-regulation, J. Immunol. 182 (2009) 2476-2484.

[80]

P.S. Mathupala, H.Y. Ko, P.L. Pedersen, Hexokinase Ⅱ: cancer's double-edged sword acting as both facilitator and gatekeeper of malignancy when bound to mitochondria, Oncogene 25 (2006) 4777-4786.

[81]

P.S. Mathupala, B.C. Colen, P. Parajuli, et al., Lactate and malignant tumors: a therapeutic target at the end stage of glycolysis, J. Bioenerg. Biomembr. 39 (2007) 73-77.

[82]

J.C. Newman, E. Verdin, Ketone bodies as signaling metabolites, Trends Endocrinol. Metab. 25 (1) (2014) 42-52.

[83]

S. Tunaru, J. Kero, A. Schaub, et al., PUMA-G and HM74 are receptors for nicotinic acid and mediate its anti-lipolytic effect, Nat. Med. 9 (2003) 352-355.

[84]

A.K.P. Taggart, J. Kero, X. Gan, et al., (D)-β-Hydroxybutyrate inhibits adipocyte lipolysis via the nicotinic acid receptor PUMA-G, J. Biol. Chem. 280 (2005) 26649-26652.

[85]

B.B. Fredholm, A.P. IJzerman, K.A. Jacobson, et al., International Union of Basic and Clinical Pharmacology. LXXXII: nomenclature and classification of adenosine receptors—an update, Pharmacol. Rev. 63 (2011) 269-290.

[86]

I. Kimura, D. Inoue, T. Maeda, et al., Short-chain fatty acids and ketones directly regulate sympathetic nervous system via G protein-coupled receptor 41 (GPR41), Proc. Natl. Acad. Sci. U.S.A. 108 (2011) 8030-8035.

[87]

C.C. Blad, C. Tang, S. Offermanns, G protein-coupled receptors for energy metabolites as new therapeutic targets, Nat. Rev. Drug Discov. 11 (2012) 603-619.

[88]

D.G. Cotter, R.C. Schugar, P.A. Crawford, Ketone body metabolism and cardiovascular disease, Am. J. Physiol. Heart Circ. Physiol. 304 (2013) H1060-H1076.

[89]

S.E. Hugo, L. Cruz-Garcia, S. Karanth, et al., A monocarboxylate transporter required for hepatocyte secretion of ketone bodies during fasting, Genes Dev. 26 (2012) 282-293.

[90]

T. Scully, Diabetes in numbers, Nature 485 (2012) s2-s3.

[91]

S.P. Edwards, Nipped in the bud, Nature 485 (2012) s18-s19.

[92]

J. Nunnari, A. Suomalainen, Mitochondria: in sickness and in health, Cell 148 (2012) 1145-1159.

[93]

R.J. DeBerardinis, C.B. Thompson, Cellular metabolism and disease: what do metabolic outliers teach us? Cell 148 (2012) 1132-1144.

[94]

G. Taubes, Unraveling the obesity–cancer connection, Science 335 (2012) 28-32.

[95]

A. Ichimura1, A. Hirasawa1, O. Poulain-Godefroy, et al., Dysfunction of lipid sensor GPR120 leads to obesity in both mouse and human, Nature 483 (2012) 350-354.

[96]

S.H. Caldwell, D.H. Oelsner, J.C. Iezzoni, et al., Cryptogenic cirrhosis: clinical characterization and risk factors for underlying disease, Hepatology 29 (1999) 664-669.

[97]

M. Shimada, E. Hashimoto, M. Taniai, et al., Hepatocellular carcinoma in patients with non-alcoholic steatohepatitis, J. Hepatol. 37 (2002) 154-160.

[98]

A. Propst, T. Propst, G. Judmaier, et al., Prognosis in nonalcoholic steatohepatitis, Gastroenterology 108 (1995) 1607-1608.

[99]

J. Henao-Mejia, E. Elinav, C. Jin, et al., Inflammasome-mediated dysbiosis regulates progression of NAFLD and obesity, Nature 482 (2012) 179-185.

[100]

J. Couzin-Frankel, Aging genes: the sirtuin story unravels, Science 334 (2011) 1194-1198.

[101]

D. Shore, M. Squire, K.A. Nasmyth, Characterization of two genes required for the position-effect control of yeast mating-type genes, EMBO J. 3 (1984) 2817-2823.

[102]

S.I. Imai, C.M. Armstrong, M. Kaeberlein, et al., Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase, Nature 403 (2000) 795-800.

[103]

K.G. Tanner, J. Landry, R. Sternglanz, et al., Silent information regulator 2 family of NAD-dependent histone/protein deacetylases generates a unique product, 1-O-acetyl-ADP-ribose, Proc. Natl. Acad. Sci. U.S.A. 97 (2000) 14178-14182.

[104]

L. Guarente, Sir2 links chromatin silencing, metabolism, and aging, Genes Dev. 14 (2000) 1021-1026.

[105]

R.A. Frye, Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins, Biochem. Biophys. Res. Commun. 273 (2000) 793-798.

[106]

C. Canto, J. Auwerx, Caloric restriction, SIRT1 and longevity, Trends Endocrinol. Metab. 20 (7) (2009) 325-331.

[107]

S.R. Bhaumik, E. Smith, A. Shilatifard, Covalent modifications of histones during development and disease pathogenesis, Nat. Struct. Mol. Biol. 14 (2007) 1008-1016.

[108]

V.A. Spencer, J.R. Davie, Role of covalent modifications of histones in regulating gene expression, Gene 240 (1999) 1-12.

[109]

K.K. Lee, J.L. Workman, Histone acetyltransferase complexes: one size doesn’t fit all, Nat. Rev. Mol. Cell Biol. 8 (2007) 284-295.

[110]

B.T. Weinert, V. Iesmantavicius, T. Moustafa, et al., Acetylation dynamics and stoichiometry in Saccharomyces cerevisiae, Mol. Syst. Biol. 10 (2014) 716-728.

[111]

D.L. Topping, P.M. Clifton, Short-chain fatty acids and human colonic function: roles of resistant starch and nonstarch polysaccharides, Physiol. Rev. 81 (2001) 1031-1064.

[112]

M. Bauer-Marinovic, S. Florian, K. Müller-Schmehl, et al., Dietary resistant starch type 3 prevents tumor induction by 1 2-dimethylhydrazine and alters proliferation, apoptosis and dedifferentiation in rat colon, Carcinogenesis 27 (2006) 1849-1859.

[113]

J.M. Clarke, D.L. Topping, A.R. Bird, et al., Effects of high-amylose maize starch and butyrylated high-amylose maize starch on azoxymethane-induced intestinal cancer in rats[J], Carcinogenesis 29 (2008) 2190-2194.

[114]

J.C. Mathers, M. Movahedi, F. Macrae, et al., Long-term effect of resistant starch on cancer risk in carriers of hereditary colorectal cancer: an analysis from the CAPP2 randomised controlled trial, Lancet Oncol. 13 (2012) 1242-1249.

[115]

B. Holst, G. Williamson, Nutrients and phytochemicals: from bioavailability to bioefficacy beyond antioxidants, Curr. Opin. Biotechnol. 19 (2008) 73-82.

[116]

G. Pang, J. Xie, Q. Chen, et al., How functional foods play critical roles in human health, Food Sci. Hum. Wellness 1 (2012) 26-60.

[117]

K.K. Ryan, R.J. Seeley, Food as a hormone, Science 339 (2013) 918-919.

[118]

D.Y. Oh, S. Talukdar, E.J. Bae, et al., GPR120 is an omega-3 fatty acid receptor mediating potent anti-inflammatory and insulin-sensitizing effects, Cell 142 (2010) 687-698.

[119]

S.G. Dann, G. Thomas, The amino acid sensitive TOR pathway from yeast to mammals, FEBS Lett. 580 (2006) 2821-2829.

[120]

B.T. Layden, A.R. Angueira, M. Brodsky, et al., Short chain fatty acids and their receptors: new metabolic targets, Transl. Res. 61 (3) (2013) 131-140.

[121]

E. Pouteau, P. Nguyen, O. Ballevre, et al., Production rates and metabolism of short-chain fatty acids in the colon and whole body using stable isotopes, Proc. Nutr. Soc. 62 (2003) 87-93.

[122]

X. Tang, Y. Wang, D. Li, et al., Orphan G protein coupled receptors (GPCRs): biological functions and potential drug targets, Acta Pharmacol. Sin. 33 (2012) 363-371.

[123]

R. O’lone, M.C. Frith, E.K. Karlsson, et al., Genomic targets of nuclear estrogen receptors, Mol. Endocrinol. 18 (8) (2004) 1859-1875.

[124]

B.A. Bruce, TLRs and innate immunity, Blood 113 (7) (2009) 1399-1407.

[125]

H. Li, X. Liu, Y. Li, et al., Effects of the polysaccharide from Pholiota nameko on human cytokine network in serum, Int. J. Biol. Macromol. 50 (2012) 164-170.

[126]

J. Xie, L. Guo, G. Pang, et al., Modulation effect of Semen Ziziphi Spinosae extracts on IL-1β, IL-4, IL-6, IL-10, TNF-α and IFN-γ in mouse serum, Nat. Prod. Res. 25 (4) (2011) 464-467.

[127]
Y. Hua, G. Pang, Cellular communication network modeling method based on cytokines, in: 2011 International Conference on Network Computing and Information Security, 2011, pp. 441–445.
DOI
[128]

X. Wang, G. Ma, J. Xie, et al., Influence of JuA in evoking communication changes between the small intestines and brain tissues of rats and the GABAA and GABAB receptor transcription levels of hippocampal neurons, J. Ethnopharmacol. 159 (2015) 215-223.

[129]

Y. Sun, Y. Ma, Z. Xu, et al., Immunoregulatory role of Pleurotus eryngii superfine powder through intercellular communication of cytokines, Food Agric. Immunol. 25 (4) (2014) 586-599.

[130]

Y. Sun, Y. Shao, Z. Zhang, et al., Regulation of human cytokines by Cordyceps Militaris, J. Food Drug Anal. 22 (2014) 463-467.

[131]

Z. Frankenstein, U. Alon, I.R. Cohen, The immune-body cytokine network defines a social architecture of cell interactions, Biol. Direct 1 (32) (2006) 1-15.

[132]

D.J. Watts, S.H. Strogatz, Collective dynamics of ‘small-world’ networks, Nature 393 (1998) 440-442.

[133]

H. Jeong, B. Tombor, R. Albert, et al., The large-scale organization of metabolic networks, Nature 407 (2000) 651-654.

[134]

H. Jeong, S.P. Mason, A.L. Barabási, et al., Lethality and centrality in protein networks, Nature 411 (2001) 41-42.

[135]

L. Hakes, J.W. Pinney, D.L. Robertson, et al., Protein–protein interaction networks and biology – what's the connection? Nat. Biotechnol. 26 (2008) 69-72.

[136]

R. Milo, S. Itzkovitz, N. Kashtan, et al., Superfamilies of evolved and designed networks, Science 303 (2004) 1538-1542.

[137]

N.V. Torres, F. Mateo, E. Melendez-Hevia, et al., Kinetics of metabolic pathways. A system in vitro to study the control of flux, Biochem. J. 234 (1986) 169-174.

[138]

S. Thomas, P. Mooney, M. Burrell, et al., Metabolic control analysis of glycolysis in tuber tissue of potato (Solanum tuberosum): explanation for the low control coefficient of phosphofructokinase over respiratory flux, Biochem. J. 322 (1997) 119-127.

[139]

V.A. Pierce, D.L. Crawford, Phylogenetic analysis of glycolytic enzyme expression, Science 276 (1997) 256-259.

[140]

X. Cai, H. Wang, G. Pang, Flux control analysis of a lactate and sucrose metabolic network at different storage temperatures for Hami melon (Cucumis melo var. saccharinus), Sci. Horticult. 181 (2015) 4-12.

[141]

E. Almaas, B. Kovacs, T. Vicsek, et al., Global organization of metabolic fluxes in the bacterium Escherichia coli, Nature 427 (2004) 839-843.

Publication history
Copyright
Rights and permissions

Publication history

Received: 16 December 2014
Accepted: 28 December 2014
Published: 14 January 2015
Issue date: December 2014

Copyright

© 2015 Beijing Academy of Food Sciences.

Rights and permissions

Return