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Information on EC 1.1.1.21 - aldose reductase and Organism(s) Mus musculus and UniProt Accession P45376
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EC Tree
1.1.1.21 aldose reductaseIUBMB Comments
Has wide specificity.
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Word Map
- 1.1.1.21
- lens
- nerve
- neuropathy
- sorbinil
- cataract
- mellitus
- retinopathy
- hyperglycemia
-
glycation
- streptozotocin
- galactose
-
sciatic
- fructose
- retinal
- endothelial
-
streptozotocin-induced
- myo-inositol
- erythrocyte
- reductases
-
nadph-dependent
-
streptozotocin-diabetic
-
microvascular
-
galactosemic
- galactitol
-
hypertonic
-
diabetes-induced
-
stz-induced
- opacity
-
antidiabetic
-
glucose-induced
-
osmolytes
- pericytes
-
nondiabetic
-
cataractogenesis
-
galactose-induced
- microangiopathy
-
endoneurial
- xylitol
-
sural
- hne
-
hyperglycemia-induced
- polyneuropathy
-
lenticular
-
glycaemic
-
mesangial
- synthesis
-
opacification
-
stz-diabetic
- alr
- akr1c3
- microaneurysms
- nutrition
- medicine
- drug development
- diagnostics
- biotechnology
The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
aldose reductase, akr1b10, akr1b3, akr1b, aldose reductase-like, aldose reductase-like protein, aldo-keto reductase family 1 member b1, akr1b14, aldose reductase 2, aldrxv4, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AKR1B1
20-alpha-HSD
-
-
-
-
20-alpha-hydroxysteroid dehydrogenase
-
-
-
-
aldehyde reductase
-
-
-
-
alditol:NADP 1-oxidoreductase
-
-
-
-
alditol:NADP oxidoreductase
-
-
-
-
aldo-keto reductase family 1 member B7
-
-
-
-
aldose xylose reductase
-
-
-
-
ALR2
-
-
-
-
Fibroblast growth factor regulated protein
-
-
-
-
FR-1 protein
-
-
-
-
MVDP
-
-
-
-
NADPH-aldopentose reductase
-
-
-
-
NADPH-aldose reductase
-
-
-
-
polyol dehydrogenase (NADP2)
-
-
-
-
TPN-polyol dehydrogenase
-
-
-
-
VAS deferens androgen-dependent protein
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
alditol:NAD(P)+ 1-oxidoreductase
Has wide specificity.
CAS REGISTRY NUMBER
COMMENTARY
9028-31-3
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
aldose + NADPH + H+
alditol + NADP+
-
the enzyme mediates the lipopolysaccharide-induced release of inflammatory mediators in macrophages, overview, inhibition of the aldehyde-metabolizing enzyme modulates NF-kappaB-dependent activation of inflammatory cytokines and chemokines in mouse serum, liver, heart, and spleen, overview
-
-
?
D-glucose + NADPH + H+
sorbitol + NADP+
-
the aldose reductase polyol pathway pathway and advanced glycation end products, AGEs, are involved in myocardial ischemic injury in diabetis, mechanisms implicated in polyol pathwaylinked functional abnormalities include myoinositol depletion and associated impaired phosphatidylinositol metabolism, osmotic imbalance due to accumulation of sorbitol, and decreased availability of NADPH
-
-
?
additional information
?
-
reduction of carnosine-propanal conjugates in murine tissues, overview
-
-
?
additional information
?
-
-
reduction of carnosine-propanal conjugates in murine tissues, overview
-
-
?
additional information
?
-
-
aldose reductase plays an important role in the regulation of hepatic peroxisome proliferator-activated receptor alpha phosphorylation and activity and lipid homeostasis
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
aldose + NADPH + H+
alditol + NADP+
-
the enzyme mediates the lipopolysaccharide-induced release of inflammatory mediators in macrophages, overview, inhibition of the aldehyde-metabolizing enzyme modulates NF-kappaB-dependent activation of inflammatory cytokines and chemokines in mouse serum, liver, heart, and spleen, overview
-
-
?
D-glucose + NADPH + H+
sorbitol + NADP+
-
the aldose reductase polyol pathway pathway and advanced glycation end products, AGEs, are involved in myocardial ischemic injury in diabetis, mechanisms implicated in polyol pathwaylinked functional abnormalities include myoinositol depletion and associated impaired phosphatidylinositol metabolism, osmotic imbalance due to accumulation of sorbitol, and decreased availability of NADPH
-
-
?
additional information
?
-
reduction of carnosine-propanal conjugates in murine tissues, overview
-
-
?
additional information
?
-
-
reduction of carnosine-propanal conjugates in murine tissues, overview
-
-
?
additional information
?
-
-
aldose reductase plays an important role in the regulation of hepatic peroxisome proliferator-activated receptor alpha phosphorylation and activity and lipid homeostasis
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1-O-Galloyl-beta-D-glucose
i.e. beta-glucogallin or BGG, a major component of the Emblica officinalis medicinal plant, and a stable, potent, and specific inhibitor of aldose reductase, noncompetitive inhibition through binding the active site of AKR1B1, occupying both the anionic and the specificity pockets
fidarestat
-
inhibition of enzyme in neural stem cells exposed to high glucose concentration results in decrease of oxidative stress, restoration of cell viability and proliferation, and reduction of apoptotic cell death. Inhibition attenuates the down-regulation of glucose transporter 1 expression
fidarestat
-
fidarestat decreases doxorubicin-induced upregulation of CD11b in THP-1 monocytes. Fidarestat attenuates doxorubicin-induced upregulation of IL-6, IL-1bta, and Nos2 in murine BMDM. Fidarestat also attenuates doxorubicin-induced activation and infiltration of multiple subsets of inflammatory immune cells identified by expression of markers CD11b+, CD11b+F4/80+, Ly6C+CCR2high, and Ly6C+CD11b+ in the mouse spleen and liver. Upregulation of markers of mitochondrial biogenesis PGC-1alpha, COX IV, TFAM, and phosphorylation of AMPKalpha1 (Ser485) is observed in THP-1 cells and livers of mice treated with doxorubicin in combination with fidarestat
sorbinil
-
inhibition of aldose reductase suppresses lipopolysaccharide-stimulated production of nitric oxide and over-expression of inducible nitric oxide synthase. Inhibition also prevents the lipopolysaccaride-induced apoptosis, cell cycle arrest, activation of caspase-3, downregulation of Bcl-xl and up-regulation of Bax and Bak in macrophages
Tolrestat
-
inhibition of aldose reductase suppresses lipopolysaccharide-stimulated production of nitric oxide and over-expression of inducible nitric oxide synthase. Inhibition also prevents the lipopolysaccaride-induced apoptosis, cell cycle arrest, activation of caspase-3, downregulation of Bcl-xl and up-regulation of Bax and Bak in macrophages
zopolrestat
-
inhibition of aldose reductase suppresses lipopolysaccharide-stimulated production of nitric oxide and over-expression of inducible nitric oxide synthase. Inhibition also prevents the lipopolysaccaride-induced apoptosis, cell cycle arrest, activation of caspase-3, downregulation of Bcl-xl and up-regulation of Bax and Bak in macrophages
additional information
no inhibition by the triazole 1-(beta-D-glucopyranosyl)-4-(3,4,5-trihydroxyphenyl)-1,2,3-triazole, the amide N-phenylacetyl beta-D-glucopyranosylamine, and the glycosides of beta-glucogallin, 2-(3,4,5-trihydroxyphenyl)ethyl beta-D-glucopyranoside, [1-(3,4,5-trihydroxybenzyl)-1,2,3-triazole-4-yl]methyl beta-D-glucopyranoside, and 3-(3,4,5-trihydroxyphenyl)propyl beta-D-glucopyranoside, synthesis and evaluation, overview
-
additional information
-
inhibition of the aldehyde-metabolizing enzyme modulates NF-kappaB-dependent activation of inflammatory cytokines and chemokines in mouse serum, liver, heart, and spleen, overview
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
inhibition or RNA interference ablation of aldose reductase suppresses lipopolysaccharide-stimulated production of nitric oxide and over-expression of inducible nitric oxide synthase. Inhibition also prevents the lipopolysaccaride-induced apoptosis, cell cycle arrest, activation of caspase-3, downregulation of Bcl-xl and up-regulation of Bax and Bak in macrophages
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
malfunction
-
enzyme knockdown reduces the development of diet-induced liver fibrosis
physiological function
evolution
aldose reductase (AKR1B1) is a member of the aldo-keto reductase superfamily
evolution
aldose reductase belongs to the aldoketo reductase superfamily, which includes several enzymes that catalyze oxidation and reduction reactions involved in various cellular processes
malfunction
carnosine-propanals are converted to carnosine-propanols in the lysates of heart, skeletal muscle, and brain tissue from wild-type but not AR-null mice. In comparison with wild-type mice, the urinary excretion of carnosine-propanols is decreased in AR-null mice, overview
malfunction
enzyme deficiency-induced microglia/macrophages induce the M2 rather than the M1 response (classically activated pro-inflammatory (M1) or alternatively activated anti-inflammatory (M2) cells) and promote locomotion recovery after spinal cord injury in mice. In the in vitro experiments, microglia cell lines (N9 or BV2) are treated with the enzyme inhibitor fidarestat. Enzyme inhibition causes 4-hydroxynonenal accumulation, which induces the phosphorylation of the cAMP response element-binding. Enzyme deficiency causes NF-kappaB downregulation and CREB upregulation after spinal cord injury in mice
malfunction
lipopolysacchride-induced RMG activation and migration into the inner nuclear layer or outer nuclear layer is largely prevented by enzyme inhibitors or in aldose reductase null mice, or is exacerbated in transgenic mice that over-express the enzyme
metabolism
AKR1B1 functions in the polyol pathway as an NADPH-dependent enzyme, catalyzing the reduction of glucose to sorbitol, which is then converted to fructose by sorbitol dehydrogenase
metabolism
aldose reductase is the only enzyme responsible for reducing glucose to sorbitol in the polyol pathway of glucose metabolism
physiological function
aldose reductase regulates cytokine and chemokine production in the eye and mediates retinal microglia activation, role of the enzyme in RMG activation and migration in vivo, overview. Retinal microglia (RMG) are one of the major immune cells in charge of surveillance of inflammatory responses in the eye. In the absence of an inflammatory stimulus, RMG reside predominately in the ganglion layer and inner or outer plexiform layers. Under stress RMG become activated and migrate into the inner nuclear layer or outer nuclear layer. Activated RMG in cell culture secrete pro-inflammatory cytokines in a manner sensitive to downregulation by aldose reductase inhibitors. Aldose reductase expression in retinal microglia may contribute to the proinflammatory phenotypes common to various eye diseases such as uveitis and diabetic retinopathy
physiological function
aldose reductase regulates microglia/macrophages polarization through the cAMP response element-binding protein after spinal cord injury in mice, mechanism, overview
physiological function
lipid peroxidation generates unsaturated aldehydes, such as acrolein, that form conjugates with histidyl dipeptides.Carnosine-aldehyde conjugates form covalent adducts with proteins and are reduced by aldose reductase. Detoxification of carnosine-aldehyde by aldose reductase prevents protein carnosinylation. Aldose reductase prevents tissue injury due to aldehyde-carnosine conjugates. Carnosine-propanals are converted to carnosine-propanols in the lysates of heart, skeletal muscle, and brain tissue from wild-type but not AR-null mice. Role of aldose reductase as a critical regulator of protein carnosinylation and carnosine-mediated tissue protection, overview
physiological function
-
aldose reductase metabolizes both free and phospholipid aldehydes and exacerbates atherosclerotic lesion formation, increase in lesion area attributable to inhibition of the enzyme or deletion of the gene encoding the enzyme occurs in both male and female mice, phenotype of enzyme-deficient male and female mice with increases in arterial lesions, macrophage accumulation and interstitial fibrosis, and decreases smooth muscle cell content of arterial lesions, detailed overview
physiological function
-
aldose reductase catalyzes the rate-limiting reduction of glucose to sorbitol with the aid of cofactor NADPH. The enzyme induces elevations on the level of CYP2E1 expression, reactive oxygen species, mRNA expression of TNF-alpha, and IL-6, confirmed in AML12 hepatocytes. The enzyme is involved in the development of methionine-choline-deficient diet-induced steatohepatitis in diabetic db/db mice, and plays a role in the development of diabetic complications. The enzyme alleviates the diet-induced (via methionine-choline-deficient (MCD) diet) liver inflammation and fibrosis in db/db mice, probably through dampening CYP2E1 mediated-oxidative stress and ameliorating the expression of pro-inflammatory cytokines
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). ALDR_MOUSE
316
0
35732
Swiss-Prot
other Location (Reliability: 1)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with NADPH, to 2.4 A resolution. Space group P412121 or P43212
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
recombinant enzyme overexpression elevates RMG activation in retina
additional information
-
recombinant enzyme overexpression elevates RMG activation in retina
additional information
-
aldose reductase overexpression causes strong suppression of peroxisome proliferator-activated receptor alpha/delta activity together with significant down-regulation of mRNA expression for acetyl-CoA oxidase and carnitine palmitoyltransferase-1. Suppressive effects are attenuated by the selective aldose reductase inhibitor zopolrestat. Aldose reductase overexpression greatly increases the levels of phosphorylated peroxisome proliferator-activated receptor alpha and ERK1/2. Aldose reductase-induced suppression of peroxisome proliferator-activated receptor alpha activity is attenuated by treatment with an inhibitor for ERK1/2 but not that for phosphoinositide 3-kinase, p38, or JNK
additional information
-
inhibition or RNA interference ablation of aldose reductase suppresses lipopolysaccharide-stimulated production of nitric oxide and over-expression of inducible nitric oxide synthase. Inhibition also prevents the lipopolysaccaride-induced apoptosis, cell cycle arrest, activation of caspase-3, downregulation of Bcl-xl and up-regulation of Bax and Bak in macrophages
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene AKR1B1, quantitative real-time PCR enzyme expression analysis in wild-type and mutant mice
gene AKR1B1, quantitative real-time PCR enzyme expression analysis, recombinant expression of FLAG-tagged enzyme in AML12 cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of enzyme aldose reductase is upregulated in microglia/macrophages after spinal cord injury in wild-type mice. In enzyme knockout mice, spinal cord injury leads to smaller injury lesion areas compared to wild-type
lippolysaccharide, from Salmonella enterica serotype typhimurium, induces the enzyme in mouse retina
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
inhibition of AR may be a significant therapeutic approach in preventing bacterial endotoxin-induced sepsis and tissue damage
medicine
-
in streptozotocin-diabetic mice, aldose reductase inhibitor treatment or genetic deficiency of aldose reductase result in significant dephosphorylation of both peroxisome proliferator-activated receptor alpha and ERK1/2
medicine
-
inhibition of enzyme in neural stem cells exposed to high glucose concentration results in decrease of oxidative stress, restoration of cell viability and proliferation, and reduction of apoptotic cell death. Inhibition attenuates the down-regulation of glucose transporter 1 expression
medicine
-
fidarestat decreases doxorubicin-induced upregulation of CD11b in THP-1 monocytes. Fidarestat attenuates doxorubicin-induced upregulation of IL-6, IL-1bta, and Nos2 in murine bone-marrow derived macrophages. Fidarestat also attenuates doxorubicin-induced activation and infiltration of multiple subsets of inflammatory immune cells identified by expression of markers CD11b+, CD11b+F4/80+, Ly6C+CCR2high, and Ly6C+CD11b+ in the mouse spleen and liver. Upregulation of markers of mitochondrial biogenesis PGC-1alpha, COX IV, TFAM, and phosphorylation of AMPKalpha1 (Ser485) is observed in THP-1 cells and livers of mice treated with doxorubicin in combination with fidarestat
medicine
-
mice devoid of AKR1B3 and exposed to acute occlusion of the left anterior descending coronary artery display reduced infarct size and improved functional recovery at 48 hours compared to wild-type mice. The cardioprotection observed in AKR1B3 null mice is linked to acute activation of the beta-catenin pathway and consequent activation of mesenchymal markers and genes linked to fibrotic remodeling. The increased activity of the beta-catenin pathway at 48 hours of recovery is not observed at 28 days post-infarction. In ex vivo studies, inhibition of beta-catenin blocks the cardioprotection observed in AKR1B3 null mice hearts
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kaneko, M.; Bucciarelli, L.; Hwang, Y.C.; Lee, L.; Yan, S.F.; Schmidt, A.M.; Ramasamy, R.
Aldose reductase and AGE-RAGE pathways: key players in myocardial ischemic injury
Ann. N. Y. Acad. Sci.
1043
702-709
2005
Homo sapiens, Mus musculus
Ramana, K.V.; Fadl, A.A.; Tammali, R.; Reddy, A.B.; Chopra, A.K.; Srivastava, S.K.
Aldose reductase mediates the lipopolysaccharide-induced release of inflammatory mediators in RAW264.7 murine macrophages
J. Biol. Chem.
281
33019-33029
2006
Mus musculus
Ramana, K.V.; Reddy, A.B.; Tammali, R.; Srivastava, S.K.
Aldose reductase mediates endotoxin-induced production of nitric oxide and cytotoxicity in murine macrophages
Free Radic. Biol. Med.
42
1290-1302
2007
Mus musculus
Qiu, L.; Wu, X.; Chau, J.F.; Szeto, I.Y.; Tam, W.Y.; Guo, Z.; Chung, S.K.; Oates, P.J.; Chung, S.S.; Yang, J.Y.
Aldose reductase regulates hepatic peroxisome proliferator-activated receptor alpha phosphorylation and activity to impact lipid homeostasis
J. Biol. Chem.
283
17175-17183
2008
Mus musculus
Fu, J.; Tay, S.S.; Ling, E.A.; Dheen, S.T.
Aldose reductase is implicated in high glucose-induced oxidative stress in mouse embryonic neural stem cells
J. Neurochem.
103
1654-1665
2007
Mus musculus
Srivastava, S.; Vladykovskaya, E.; Barski, O.A.; Spite, M.; Kaiserova, K.; Petrash, J.M.; Chung, S.S.; Hunt, G.; Dawn, B.; Bhatnagar, A.
Aldose reductase protects against early atherosclerotic lesion formation in apolipoprotein E-null mice
Circ. Res.
105
793-802
2009
Mus musculus
Takashima, Y.; Hatanaka, S.; Mizohata, E.; Nagata, N.; Fukunishi, Y.; Matsumura, H.; Urade, Y.; Inoue, T.
Crystallization and preliminary X-ray diffraction analysis of mouse prostaglandin F2alpha synthase, AKR1B3
Acta Crystallogr. Sect. F
67
1630-1632
2011
Mus musculus (P45376), Mus musculus
Chang, K.C.; Shieh, B.; Petrash, J.M.
Aldose reductase mediates retinal microglia activation
Biochem. Biophys. Res. Commun.
473
565-571
2016
Mus musculus (P45376), Mus musculus, Mus musculus C57BL/6 (P45376)
Baba, S.P.; Hoetker, J.D.; Merchant, M.; Klein, J.B.; Cai, J.; Barski, O.A.; Conklin, D.J.; Bhatnagar, A.
Role of aldose reductase in the metabolism and detoxification of carnosine-acrolein conjugates
J. Biol. Chem.
288
28163-28179
2013
Homo sapiens (P15121), Homo sapiens, Mus musculus (P45376), Mus musculus
Li, L.; Chang, K.C.; Zhou, Y.; Shieh, B.; Ponder, J.; Abraham, A.D.; Ali, H.; Snow, A.; Petrash, J.M.; LaBarbera, D.V.
Design of an amide N-glycoside derivative of beta-glucogallin: a stable, potent, and specific inhibitor of aldose reductase
J. Med. Chem.
57
71-77
2014
Homo sapiens (P15121), Mus musculus (P45376)
Zhang, Q.; Bian, G.; Chen, P.; Liu, L.; Yu, C.; Liu, F.; Xue, Q.; Chung, S.K.; Song, B.; Ju, G.; Wang, J.
Aldose reductase regulates microglia/macrophages polarization through the cAMP response element-binding protein after spinal cord injury in mice
Mol. Neurobiol.
53
662-676
2016
Mus musculus (P45376), Mus musculus C57BL/6 (P45376)
Qiu, L.; Lin, J.; Ying, M.; Chen, W.; Yang, J.; Deng, T.; Chen, J.; Shi, D.; Yang, J.Y.
Aldose reductase is involved in the development of murine diet-induced nonalcoholic steatohepatitis
PLoS ONE
8
e73591
2013
Mus musculus
Sonowal, H.; Saxena, A.; Qiu, S.; Srivastava, S.; Ramana, K.
Aldose reductase regulates doxorubicin-induced immune and inflammatory responses by activating mitochondrial biogenesis
Eur. J. Pharmacol.
895
173884
2021
Mus musculus
Thiagarajan, D.; O Shea, K.; Sreejit, G.; Ananthakrishnan, R.; Quadri, N.; Li, Q.; Schmidt, A.M.; Gabbay, K.; Ramasamy, R.
Aldose reductase modulates acute activation of mesenchymal markers via the beta-catenin pathway during cardiac ischemia-reperfusion
PLoS ONE
12
e0188981
2017
Mus musculus
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