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Que no podrá ser cancelada sin la conformidad previa y por escrito de “LA UNAM”, y

NOMBRE Y FIRMA DEL REPRESENTANTE LEGAL

CONTRATO DE PRESTACIÓN DE SERVICIOS QUE CELEBRAN POR UNA PARTE LA UNIVERSIDAD NACIONAL AUTONOMA DE MEXICO, A LA QUE EN LO SUCESIVO SE LE DENOMINARÁ “LA UNAM”,

III. DECLARAN AMBAS PARTES:

III. 1 Que leídas las anteriores declaraciones, reconocen mutuamente la personalidad que ostentan y acreditan estar de acuerdo con obligarse, conviniendo en celebrar el presente Contrato al tenor de

2. Que no podrá ser cancelada sin la conformidad previa y por escrito de “LA UNAM”, y

TXNIP  was  first  shown  to  play  a  critical  role  in  metabolic  control  when  a  mutant   mouse   strain,   HcB-­‐‑19/Dem   (HcB-­‐‑19)   with   a   nonsense   mutation   in   the   TXNIP   gene   causing   a   lack   of   TXNIP   expression,   resulted   in   features   of   familial   combined  

hyperlipidemia  (FCHL)  including  hypertriglyceridemia,  hypercholesterolemia,  elevated   plasma   apolipoprotein   B   and   increased   secretion   of   triglyceride-­‐‑rich   lipoproteins   (Bodnar  et  al.,  2002).    It  was  later  shown  that  no  association  was  found  between  FCHL   families   and   the   TXNIP   gene   (Coon   et   al.,   2004),   but   the   impact   of   the   deficiency   of   TXNIP  on  lipid  metabolism  was  clear.    In  addition  to  hypertriglyceridemia,  HcB-­‐‑19  mice   in  the  prolonged  fasted  state  (≥18h)  have  elevated  plasma  free  fatty  acids,  ketones  and   lactate   with   lower   pyruvate   levels   in   comparison   to   wild   type   controls   (Bodnar   et   al.,   2002;  Donnelly  et  al.,  2004;  Hui  et  al.,  2004;  Sheth  et  al.,  2005).    Moreover,  decreased  TCA   cycle   flux   as   measured   by   CO2   production   from   isolated   liver   slices   was   significantly  

decreased  suggesting  mitochondrial  dysfunction  with  TXNIP  deficiency  (Bodnar  et  al.,   2002).  

Subsequently,   mice   generated   with   a   targeted   inactivation   of   TXNIP   (TBP-­‐‑2-­‐‑/-­‐‑)  

displayed  a  similar  phenotype  with  even  more  pronounced  abnormalities,  such  as  liver   steatosis,   severe   gastrointestinal   bleeding   and   hepatic-­‐‑renal   dysfunction   after   24h   fasting,  and  a  predisposition  to  death  under  extreme  fasting  conditions  ≥48h  (Oka  et  al.,   2006a).    The  phenotypic  presentation  in  both  of  these  mouse  models  of  TXNIP  deficiency   points   toward   impairment   in   liver   fatty   acid   flux   through   the   TCA   cycle,   possibly   sparing  those  fatty  acids  for  incorporation  into  triglycerides  and  ketones  (Bodnar  et  al.,   2002;  Donnelly  et  al.,  2004;  Oka  et  al.,  2006a;  Sheth  et  al.,  2005).  

In   addition   to   its   function   in   lipid   metabolism,   TXNIP   is   a   key   regulator   in   glucose  homeostasis.    TXNIP  is  transcriptionally  upregulated  by  glucose  (Stoltzman  et   al.,  2008)  and  its  mRNA  expression  is  elevated  in  muscle  of  insulin  resistant  and  diabetic   humans   (Parikh   et   al.,   2007).     Moreover,   silencing   TXNIP   expression   in   human   adipocytes   and   skeletal   muscle   myocytes   enhances   glucose   uptake,   whereas   TXNIP   overexpression   inhibits   glucose   uptake.     Under   prolonged   fasted   conditions,   both   the   HcB-­‐‑19   and   TBP-­‐‑2-­‐‑/-­‐‑   mouse   models   of   TXNIP   deficiency   display   higher   insulin   with  

lower   blood   glucose   levels   in   comparison   to   wild   type   controls   (Bodnar   et   al.,   2002;   Donnelly  et  al.,  2004;  Hui  et  al.,  2004;  Sheth  et  al.,  2005),  which  was  shown  to  be  due  to  a   defect   in   hepatocyte   glucose   production   (Chutkow   et   al.,   2008)   and   increased   insulin   secretion  and  sensitivity  (Hui  et  al.,  2004).      

A   third   and   fourth   model   of   TXNIP   ablation   generated   through   a   Cre-­‐‑loxP-­‐‑ mediated   gene   recombination   (TKO)   and   targeted   gene   deletion   (TXNIP-­‐‑null),   respectively,  share  similar  phenotypes  to  the  previous  two  models  (HcB-­‐‑19  and  TBP-­‐‑2-­‐‑/-­‐‑)  

with  the  exception  of  normal  insulin  levels  (Chutkow  et  al.,  2010;  Chutkow  et  al.,  2008;   Hui  et  al.,  2008).    The  reason  for  the  varied  fasting  insulin  levels  between  the  models  is   unknown,   but   Chutkow   et   al.   (2008)   suggest   that   it   could   be   caused   by   experimental   conditions   for   fasting   and   susceptibility   or   modifier   gene   effects   resulting   from   strain   differences.    Nonetheless,  in  all  models  in  which  TXNIP  is  disrupted,  there  is  consistent   enhancement  of  glucose  tolerance,  insulin  sensitivity  and  augmented  glucose  transport  

in  some  peripheral  tissues  (Chutkow  et  al.,  2010;  Chutkow  et  al.,  2008;  Hui  et  al.,  2008;   Oka  et  al.,  2006a).    For  instance,  TXNIP  null  mice  challenged  on  a  4-­‐‑week  high  fat  diet   were  insulin  sensitive  and  demonstrated  augmented  glucose  uptake  into  skeletal  muscle   and  white  adipose  tissue  by  30  and  40%,  respectively,  relative  to  WT  controls  (Chutkow   et  al.,  2010).    These  conditions  occured  in  spite  of  a  2-­‐‑fold  increase  in  adiposity  due  to   hyperphagia.     TXNIP   deficiency   similarly   improved   glucose   intolerance   and   insulin   resistance   in   the   skeletal   muscle   of   diabetic   ob/ob   mice   crossed   with   TBP-­‐‑2-­‐‑/-­‐‑   mice  

(ob/ob•TBP-­‐‑2-­‐‑/-­‐‑),   without   amelioration   of   obesity   or   obesity-­‐‑induced   adipocytokines  

(Yoshihara  et  al.,  2010).      

Interestingly,   the   peripheral   tissue   phenotypes   as   a   result   of   TXNIP   ablation   vary.    TKO  (total  body  knock-­‐‑out)  mice  created  by  Hui  et  al.  (2008)  exhibited  increased   insulin   signaling,   insulin   sensitivity   and   glycolysis   in   oxidative   tissues   (skeletal   muDeBalsi.Thesis.9.5.13scle  and  hearts),  but  not  in  lipogenic  tissues  (adipose  and  liver).     This  is  in  contrast  to  the  enhanced  glucose  uptake  reported  by  Chutkow  et  al.  (2010)  in   both   skeletal   muscle   and   liver   of   TXNIP   null   mice,   which   may   be   due   to   strain   differences  or  specific  aspects  of  the  gene-­‐‑targeting  approaches.    Also  in  the  TKO  mice,   oxidative  tissues  displayed  impaired  mitochondrial  glucose  and  fatty  acid  oxidation  and   were   predicted   to   have   disrupted   mitochondrial   respiration,   while   no   comparable   studies  were  conducted  with  the  TXNIP  null  mice  of  Chutkow  et  al  (2010).    Conversely,   in   other   studies   mitochondrial   fatty   acid   oxidation   was   not   impaired   in   the   hearts   of  

HcB-­‐‑19   mice,   although   the   TXNIP-­‐‑deficient   hearts   preferentially   used   fatty   acids   as   a   substrate  over  glucose  as  measured  by  percentage  of  acetyl-­‐‑CoA  originated  from  fats  or   glucose   for   the   TCA   cycle   (Sheth   et   al.,   2005).     More   interestingly,   in   this   same   study   fatty  acid  oxidation  in  skeletal  muscle  was  dramatically  increased  by  35%  in  the  TXNIP   deficient  mice  as  compared  to  controls,  but  only  in  a  prolonged  fasted  state.  

In  summary,  although  TXNIP  is  ubiquitously  expressed  in  all  tissues  (Junn  et  al.,   2000),  existing  data  suggests  that  the  precise  metabolic  function  of  TXNIP  varies  among   tissues   and   possibly   under   different   physiological   conditions   (i.e.   extreme   fasting/starvation).     Further,   genetic   ablation   of   TXNIP   appears   to   compromise   mitochondrial   oxidative   function   across   multiple   catabolic   pathways   and   impair   respiratory/ETC   function   in   some   peripheral   tissues   but   systematic   comparisons   of   mitochondrial  function  in  disparate  tissues  under  various  physiological  states  have  not   been  addressed.    These  studies  will  be  described  in  chapter  3.  

1.5.2 TXNIP in Metabolic Syndrome and the Pathogenesis of Type 2