(12) INTERNATIONAL APPLICATION PUBLISHED UNDER THE PATENT COOPERATION TREATY (PCT) (19) World Intellectual Property Organization International Bureau (10) International Publication Number (43) International Publication Date 10 June 2010 (10.06.2010) WO 2010/065567 A2 (51) International Patent Classification: (81) Designated States (unless otherwise indicated, for every A61K 36/889 (2006.01) A61K 31/16 (2006.01) kind of national protection available): AE, AG, AL, AM, A61K 36/736 (2006.01) A61K 31/05 (2006.01) AO, AT, AU, AZ, BA, BB, BG, BH, BR, BW, BY, BZ, A61K 31/166 (2006.01) A61P 5/00 (2006.01) CA, CH, CL, CN, CO, CR, CU, CZ, DE, DK, DM, DO, DZ, EC, EE, EG, ES, FI, GB, GD, GE, GH, GM, GT, (21) International Application Number: HN, HR, HU, ID, IL, IN, IS, JP, KE, KG, KM, KN, KP, PCT/US2009/066294 KR, KZ, LA, LC, LK, LR, LS, LT, LU, LY, MA, MD, (22) International Filing Date: ME, MG, MK, MN, MW, MX, MY, MZ, NA, NG, NI, 1 December 2009 (01 .12.2009) NO, NZ, OM, PE, PG, PH, PL, PT, RO, RS, RU, SC, SD, SE, SG, SK, SL, SM, ST, SV, SY, TJ, TM, TN, TR, TT, (25) Filing Language: English TZ, UA, UG, US, UZ, VC, VN, ZA, ZM, ZW. (26) Publication Language: English (84) Designated States (unless otherwise indicated, for every (30) Priority Data: kind of regional protection available): ARIPO (BW, GH, 61/1 18,945 1 December 2008 (01 .12.2008) US GM, KE, LS, MW, MZ, NA, SD, SL, SZ, TZ, UG, ZM, ZW), Eurasian (AM, AZ, BY, KG, KZ, MD, RU, TJ, (71) Applicant (for all designated States except US): LIFES¬ TM), European (AT, BE, BG, CH, CY, CZ, DE, DK, EE, PAN EXTENSION LLC [US/US]; 933 First Colonial ES, FI, FR, GB, GR, HR, HU, IE, IS, IT, LT, LU, LV, Road, Suite 114, Virginia Beach, VA 23454 (US). MC, MK, MT, NL, NO, PL, PT, RO, SE, SI, SK, SM, TR), OAPI (BF, BJ, CF, CG, CI, CM, GA, GN, GQ, GW, (72) Inventor; and ML, MR, NE, SN, TD, TG). (75) Inventor/Applicant (for US only): MCDANIEL, David, H. [US/US]; 933 First Colonial Road, Suite 114, Virginia Declarations under Rule 4.17: Beach, VA 23454 (US). — of inventorship (Rule 4Λ 7(iv)) (74) Agent: HARDING, Tanya, M.; Klarquist Sparkman, Published: LLP, One World Trade Center, Suite 1600, 121 SW Salmon Street, Portland, OR 97204 (US). — without international search report and to be republished upon receipt of that report (Rule 48.2(g)) (54) Title: METHODS AND COMPOSITIONS FOR ALTERING HEALTH, WELLBEING, AND LIFESPAN (57) Abstract: Described herein are the results of comprehensive genetic expression and other molecular analysis of the effect of antioxidants on biological systems, including specifically different human cells. Based on these analyses, methods and composi- tions are described for modifying or influencing the lifespan of cells, tissues, organs, and organisms. In various embodiments, there are provided methods for modulating the activity of the gene maintenance process in order to influence the length and/or structural integrity of the telomere in living cells, as well as methods for modulating the rate/efficiency of the cellular respiration provided by the mitochondria, mitochondrial biogenesis, and maintenance of the mitochondrial membrane potential. Exemplary lifespan altering compounds include natural and synthetic antioxidants, such as plant antioxidant and polyphenol compounds de- rived from coffee cherry, tea, berry, and so forth, including but not limited to caffeic acid, chlorogenic acid, ferulic acid, quinic acid, proanthocyanidins, ubiquinone, idebenone, or a synthetic form or derivatives thereof. METHODS AND COMPOSITIONS FOR ALTERING HEALTH, WELLBEING, AND LIFESPAN CROSS REFERENCE TO RELATED APPLICATION This application claims the benefit of the earlier filing date of U.S. Provisional Application No. 61/118,945, filed December 1, 2008, the entire content of which is incorporated herein by reference. FIELD Described herein are methods and compositions for altering mitochondrial biogenesis and/or mitochondrial maintenance, respiratory efficiency, DNA maintenance, DNA repair, gene expression, and/or gene function, for instance in order to (in various embodiments) increase, extend, or shorten the lifespan and/or retard or increase rate of senescence of a cell, tissue, organ, and/or organism. In example embodiments, this involves altering the maintenance or function of telomeres and telomere structure, maintenance and control, cellular responses to oxidative stress and/or oxidative DNA damage, and cellular response to environmental damage or disease or immune response or genetic alteration of cells. BACKGROUND All living cells and organisms have a finite lifespan. They live for a period of time and die. Cells and organisms have both a chronological age and a biological age. The former is measured in days, months or years while the latter may be measured by a host of complex testing of biological functions including but not limited to: gene expression, protein production or metabolic pathways. The rate of aging may also be measured, and an accelerated rate of aging may be considered 'premature aging', while a slower rate of aging may extend lifespan. It is desirable to maximize the healthy lifespan of cells and organisms and it is also desirable to extend the healthy lifespan by delaying the rate of aging and the onset of dysfunctional or disease states. Shortening the lifespan and/or accelerating apoptosis of unhealthy, diseased, damaged, or cancerous cells may also be desirable. Oxidative stress is one of the primary causes of cell and organism dysfunction or disease and also accelerated or premature aging and death. The ability to enhance in a favorable manner the ability of cells and organisms to resist or repair damage due to oxidative stress produced by environmental injury, lifestyle choices as well as diseases and medical therapies may extend the healthy function and/or lifespan and/or retard aging and senescence. Antioxidants have the potential not only to neutralize reactive oxygen species, but also may provide vital anti-aging benefits by affecting various other key cellular mechanisms. One such example is the telomere (and/or telomere unit and associated proteins and structural configurations) which are special chromatin structures at the end of chromosomes. Telomeres are coated by DNA binding proteins, including TRFl and TRF2 and associated proteins, TIN2, TPPl, POTl, Tankyrase 1, and Rapl. Premature or accelerated telomere shortening may produce premature aging and death. Telomerase is a DNA polymerase which plays an essential role in protecting these regions, but which may also be associated with cancer. Thus the ability to modulate telomerase activity provides the opportunity to alter health both positively and negatively. One way to extend the lifespan of a living cell - and by extension possibly the organ, tissue or entire organism - is to repair damage in addition to preventing damage. The genes which control the cellular repair mechanisms, if activated or enhanced in the proper way, may effectively extend the lifespan of a cell. This may take several forms: extending the lifespan of a cell which is damaged or injured by properly repairing that damage and/or by causing the cell to live longer or replicate itself longer than it would have occurred naturally. Mammalian mitochondria are organelles that produce more than 90% of cellular ATP under aerobic conditions through a process called oxidative phosphorylation. Mitochondria are also involved in fatty acid metabolism, hormone production, ketone body production, apoptosis, and Ca2+ homeostasis. Mitochondria contain, inter alia, the TCA cycle (also known as the Kreb cycle), enzymes involved in heme biosynthesis and the electron transport chain (OXPHOS system). Due to the large flux of redox reactions necessary to maintain oxidative phosphorylation, the organelle is the site of production of reactive oxygen species (ROS), which in controlled production have a signaling function, but in overproduction are toxic and are believed to be the cause of many human diseases including, for example, Parkinson' s disease and other neurodegenerative conditions, diabetes, and the aging process itself. The OXPHOS system is composed of five large multi-protein enzyme complexes, which collectively transform the reducing energy of NADH and FADH2 to ATP. NADH ubiquinone oxidoreductase (Complex I) contains 45 different subunits, and succinate ubiquinone reductase (Complex II), ubiquinone-cytochrome c oxidoreductase (Complex III), cytochrome c oxidase (Complex IV) and the ATP synthase (Complex V) have 4, 11, 13 and 16 subunits respectively. Although composed of five individual enzyme complexes (each, an "OXPHOS complex" or "OXPHOS enzyme") and containing a total of approximately 89 subunit proteins (each, an "OXPHOS protein"), the OXPHOS system has traditionally been considered to function as a single unit. This single-unit concept has been supported with evidence of structural associations between complexes, which associations are believed to enhance overall functional efficiency (Chen et al., J. Biol. Chem., 279:31761-31768, 2004; Ko et al., J. Biol. Chem., 278:12305-12309, 2003). Four of the OXPHOS enzyme complexes (Complexes I, III, IV and V) have a dual genetic origin. That is, they are composed of both nuclear DNA-encoded proteins and mtDNA-encoded proteins. Thus, 7 subunits of Complex I, 1 subunit of Complex III, 3 subunits of Complex IV and 2 subunits of Complex V are encoded by intDNA. Mitochondria contain their own DNA (intDNA) which is prokaryote-like. In mammals, this DNA is a 16 kb double-stranded circular DNA encoding 13 different polypeptides, all involved in oxidative phosphorylation, along with 2 rRNAs and 22 tRNAs. mtDNA lacks protective histones and has minimal repair mechanisms, which leads to a relatively high mutation rate that is further enhanced by the proximity of the DNA to the OXPHOS system, the site of production of ROS. Accumulation of mutations and deletions in mtDNA occurs throughout life in humans and becomes physiologically relevant where they affect sufficient number of copies of the mtDNA to alter oxidative phosphorylation.