Fanconi–Bickel Syndrome: A Review of the Mechanisms That Lead to Dysglycaemia
<p>Role of glucose transporter 2 (GLUT2) in pancreatic β cell glucose-stimulated insulin secretion. Glucose enters the β-cells facilitated by GLUT2, which is then phosphorylated by glucokinase (GK) and metabolized by glycolysis and tricarboxylic acid cycle (TCA), leading to increased generation of ATP. Glucagon like peptide-1 (GLP1), glucagon, and GIP (gastric inhibitory polypeptide) activation of G protein-coupled receptors (GPCRs) responsive adenylyl cyclases (AC), leading to increased formation of cyclic adenosine monophosphate (cAMP). cAMP activates protein kinase A (PKA) and epac2 (cAMP-regulated guanine nucleotide exchange factor) to potentiate glucose-stimulated secretion of insulin. Increased ratio of ATP/ADP due to increased glucose metabolism closes the ATP-gated K+ channel (K<sub>ATP</sub>), causing membrane depolarization, and voltage-dependent calcium channels (VDCC) opening, leading to Ca<sup>2+</sup> influx via VDCC, which activates insulin secretion. This action of Ca<sup>2+</sup> is potentiated by PKA. For exocytosis of insulin from β-cells, Rab3a and Rab27a GTPases are important signaling mediators that become activated by this mechanism and contribute to the exocytosis of insulin from glucose-stimulated cells.</p> "> Figure 2
<p>Regulation of glycogen metabolism in liver by GLUT2. The insulin-independent GLUT2 facilitates glucose transport across the cell membranes. Sodium-glucose cotransporter (SGLT) transport activity can be regulated by protein kinases including PKA (protein kinase A) and PKC (protein kinase C). PKA activation positively regulates SGLT1 expression and activity. Increased glucose concentration causes conformational change and activation of glucokinase (GK), which phosphorylates glucose to glucose-6-phosphate (G6P) and serves as a substrate for glycogen synthesis or glycolysis. In hepatic glycogen metabolism, G6P serves as the central intermediate. During glycolysis, utilization of G6P provides energy in the form of pyruvate, NADH and ATP. Acetyl-CoA produced from pyruvate, enters the mitochondrial tricarboxylic acid cycle (TCA). During fasting, G6P serves as a substrate for synthesis of glucose during gluconeogenesis or glycogenolysis. Glycogen phosphorylase (GP) catalyze glycogenolysis, activated by AMP or PKA, and inhibited by insulin. GSK-3β (a serine/threonine kinase) is a downstream element of PI3K/AKT pathway, whose activity can be inhibited by protein kinase B (PKB)-mediated phosphorylation at Ser9 of GSK-3β. Glycogen synthase (GS) is phosphorylated and inactivated by GSK3. SGLT: sodium-glucose cotransporter; G: glucose. Green arrows (stimulation); Red arrows (inhibition); Green Sp (phosphorylated serine): activating phosphorylation; Red Sp: inhibiting phosphorylation. Dashed lines indicate many steps not listed in the gluconeogenesis and glycogenolysis pathways to glucose.</p> "> Figure 3
<p>Human glucose transporter 2 (GLUT2) structural topology including location of variants and conserved amino acids. GLUT2 is a glucose transporter containing 12 transmembrane domains (524 amino acids) connected with extracellular and intracellular loops, facilitating the movement of glucose across the cell membranes. It has high capacity but low affinity (high km) for glucose, and functions as a glucose sensor. GLUT2 mediates bidirectional glucose transport, and is mostly expressed in pancreatic β-cells, liver, small intestine, brain and renal tubular cells.</p> "> Figure 4
<p>GLUT2-mediated glucose transport across cell membranes and communication to different organs. GLUT2 is a low affinity and high capacity glucose transporter and facilitates the transport of glucose in intestinal cells. SGLTs are high-affinity and low capacity transporters, capable of transporting glucose against a concentration gradient. Ghrelin increases the GLUT2 expression by modulating the GLUT2 transcription via GHS-R1 (growth hormone secretagogue receptor 1a) and PLC/PKC pathway. Ghrelin also stimulates translocation of GLUT2 to the surfaces of intestinal cell from intracellular vesicles, leading to increased glucose absorption. GLUT2 is highly expressed in the liver, pancreas, brain and kidney cells. Activation of nervous signals, induces the first phase of insulin release from pancreatic β-cells induced by increased glucose transport to pancreatic β-cells. These signals also induce other physiological processes. In the liver, GLUT2 maintains the glucose homeostasis during fasting and fed state by regulating the expression of glucose-sensitive genes. GLUT2 is more highly expressed in rodent β-cells than in human β-cells. In the brain, glucose-sensing cells expressing GLUT2, regulate glucose by parasympathetic and sympathetic systems. GLUT2-dependent glucose-sensing cells also regulate leptin sensitivity and regulate the expressions of uncoupling protein 1 (UCP1) and thermogenesis. Homozygous GLUT2 mutation leads to a dysfunctional and reduced expression of GLUT2, which causes FBS. Dysfunctional GLUT2 causes fasting hypoglycemia, postprandial hyperglycemia, glucose and galactose intolerance, hepatomegaly, glucosuria, reduced GSIS (glucose-stimulated insulin secretion), rickets, GH (growth hormone) deficiency and poor, growth. (G; glucose).</p> ">
Abstract
:1. Introduction
2. Physiological Roles of GLUT2
2.1. Overview
2.2. Role of GLUT2 in β-Cells
2.3. Role of GLUT2 in Liver
2.4. Role of GLUT2 in Kidney
2.5. Role of GLUT2 in Intestine
2.6. Role of GLUT2 in Brain
3. SLC2A2 (GLUT2) Mutations and Patterns of Dysglycaemia
3.1. Potential Biochemical Mechanisms Leading to Dysglycaemia in Patients with FBS
3.2. Birth Weight in FBS
3.3. Neonatal Diabetes in FBS
3.4. Frank Diabetes in FBS
3.5. Glycogen Storage in FBS
3.6. Structure Function Relationship of GLUT2 in FBS
4. Conclusions and Future Perspective
Author Contributions
Funding
Conflicts of Interest
Abbreviations
GLUT2 | Glucose transporter 2 |
cAMP | Cyclic adenosine monophosphate |
FBS | Fanconi–Bickel Syndrome |
HbA1c | Haemoglobin-A1c |
GP | Glycogen phosphorylase |
PKA | Protein kinase A |
G6P | Glucose-6-phosphate |
GK | Glucokinase |
G | Glucose |
NR | Not Reported |
aa | amino acid |
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Patient Number | Reference | Sex | Origin | Mutation | Amino Acid Change |
---|---|---|---|---|---|
1 | [9] | F | Pakistani | c.497-2A > T | p.(Gly166_Ser169del)] |
2 | [9] | M | Pakistani | c.497-2A > T | p.(Gly166_Ser169del)] |
3 | [54] | F | Turkish | IVS8g.24401-24406del6 | NR |
4 | [55] | F | India | c.952G>A | p.Gly318Arg |
5 | [55] | M | India | c.952G>A | p.Gly318Arg |
6 | [55] | F | India | c.952G>A | p.Gly318Arg |
7 | [56] | M | Kuwait | c.474A>C | p. Arg158Ser |
8 | [57] | M | Turkish | c.108+5G>A | NR |
9 | [58] | M | Turkish | c.1069delGinsAATAA | p. Val357AsnfsTer37 |
10 | [58] | F | Turkish | c.482_483insC | p. Gly162ArgfsTer17 |
11 | [58] | NR | Turkish | c.482_483insC | p. Gly162ArgfsTer17 |
12 | [58] | M | Turkish | c.482_483insC | p. Gly162ArgfsTer17 |
13 | [58] | NR | Turkish | c.482_483insC | p. Gly162ArgfsTer17 |
14 | [58] | M | Turkish | c.482_483insC | p. Gly162ArgfsTer17 |
15 | [58] | M | Turkish | c.482_483insC | p. Gly162ArgfsTer17 |
16 | [58] | M | Turkish | c.575A>G | p. His192Arg |
17 | [59] | M | Iran | C.685_701del GCCATCCTTCAGTCTCT ins CAGAAAA | p.A229 QfsX19 |
18 | [60] | M | NR | NR | E85fsX177 and G189D |
19 | [61] | F | Indian | c.1246G>A | p. Gly416Ser |
20 | [60] | M | NR | NR | NR |
21 | [62] | M | Kashmir | NR | NR |
22 | [63] | F | Indian | NR | NR |
23 | [64] | M | Indian? | c.16-1G>A or IVS 1-1G>A | NR |
24 | [65] | F | African American | c.670 | Cys224Del |
25 | [66] | F | Palestinian | c.901C>T | p. Arg301Ter |
26 | [66] | M | Palestinian | c.901C>T | p. Arg301Ter |
27 | [67] | F | Pakistani | c.339delC | p. Phe114LeufsTer16 |
28 | [67] | M | Pakistani | c.339delC | p. Phe114LeufsTer16 |
29 | [68] | NR | Chinese | c.380C>A and c.970dupT | p.Ala127Asp and p.324TyrfsX392 |
30 | [68] | NR | Chinese | c.1068+5G>C | IVS8+5G>C |
31 | [68] | NR | Chinese | c.1194T>A | p.Tyr398X |
32 | [69] | F | Iranian | c.1061_1066del6 | p.V355_S356del2 |
33 | [69] | M | Iranian | c.1061_1066del6 | p.V355_S356del2 |
34 | [70] | M | Algerian | IVS 3+2T>C/IVS 3+2T>C | NR |
35 | [10] | M | Indian | c.1330T>C | p. W444R |
36 | [71] | F | Iranian | c. 685_701del GCCATCCTTCAGTCTCTins CAGAAAA | P.A229QFsX19 |
37 | [72] | F | Indian | c.56T>C | p. Leu19Pro |
38 | [73] | F | Indian | NR | NR |
39 | [74] | F | Chinese | c.609T>A | p.Ser203Arg |
40 | [74] | M | Oman | c.1127T>G | p.Met376Arg |
41 | [74,75] | F | Iran | c.963+1G>A | NR |
42 | [74] | M | Sudanese | c.157C>T | p.Arg53X |
43 | [74] | M | Saudi Arabia | c.339del | p.Phe114LeufsX16 |
44 | [76] | F | Egyptian | c.1250C>T | p. P417L |
45 | [76] | M | Egyptian | c.253_254del GA | p. Glu85fs |
46 | [77] | M | Egyptian | c.776-1G>C | NR |
47 | [78] | F | Caucasian | c.1439C>G and c.1469delA | T480R and L490SfsX24 |
48 | [79] | M | Turkish | c.835_836delGA | p.E279KfsX6 |
49 | [80] | F | NR | c.1213C>T | NR |
50 | [81] | M | Turkish | 783del17 | NR |
51 | [81] | F | Turkish | c.818C>G | NR |
52 | [81] | F | Turkish | IVS5+1 G>T | NR |
53 | [82] | M | Italian | 425_7/delTAA | NR |
54 | [83] | F | Korean | c.322A>T | K5X |
55 | [84] | F | Japanese | c.96T>G | N32K |
56 | [85] | M | Japanese | c.1093 C>T and c.1642 T>C | p. Arg365Ter and p. Trp444Arg |
57 | [86] | F | Japanese | nt 1580T>A | V423E |
58 | [86] | M | Japanese | IVS2–2A>G | NR |
59 | [86] | M | Japanese | c.1171C>T and c.1478T>C | Q287X and L389P |
60 | [87] | M | Japanese | c.1159G>A | W420X |
61 | [87] | F | Japanese | NR | NR |
62 | [88] | M | Saudi-Arabian | c.1250 C>T | Pro417Leu |
63 | NR | Arabian | c.1250C>T | NR | |
64 | NR | Arabian | c.1250 C>T | NR | |
65 | NR | Arabian | c.1250 C>T | NR | |
66 | NR | Arabian | c.1250 C>T | NR | |
67 | NR | Arabian | c.1250 C>T | NR | |
68 | [6,89] | M | Swiss | c.1251C>T or 1213 C>T | R301X |
69 | [6] | F | NR | ΔT446-449 | |
70 | [6] | M | NR | ΔT446-449 | |
71 | [6] | M | NR | c.1405C>T | R365X |
72 | [90] | M | Japanese | c.1171C>T and c.1478 T>C | NR |
73 | [91] | M | Caucasian | NR | NR |
74 | [91] | M | Caucasian | NR | NR |
75 | [4] | NR | Japanese | c.1571G>A | NR |
76 | [2] | F | Arabian | c.1562C>T | NR |
77 | M | Arabian | c.1562C>T | NR | |
78 | M | Arabian | c.1562C>T | NR | |
79 | NR | Arabian | c.1562C>T | NR | |
80 | NR | Arabian | c.1562C>T | NR | |
81 | NR | Arabian | c.1562C>T | NR | |
82 | NR | Arabian | c.1562C>T | NR | |
83 | NR | Arabian | c.1562C>T | NR | |
84 | NR | Arabian | c.1562C>T | NR | |
85 | [92] | M | Iran | IVS8+1 G>T | NR |
86 | [93] | M | Caucasian | c.457_462delCTTATA and c.1250C>G | p.153_4delLI and p.P417R |
87 | [93] | F | Caucasian | c.457_462delCTTATA and c.1250C>G | p.153_4delLI and p.P417R |
88 | [45] | M | Dominican Republic | IVS 4-2A>G | p. Gln166AspfsTer4 |
89 | [45] | M | Dominican Republic | IVS 4-2A>G | p. Gln166AspfsTer4 |
90 | [45] | F | Israeli | c.372A>C | p. Arg124Ser |
91 | [45] | M | Israeli | c.372A>C | p. Arg124Ser |
92 | [45] | F | Israeli | c.372A>C | p. Arg124Ser |
93 | [94] | F | Chinese Han | c.682C>T and c.1185 G>A | p. Arg228X and p. Trp395X |
94 | [94] | M | Chinese Han/Yao | c.196G>T and c.1117delA | p. Glu66X and p. Met373X |
95 | [95] | M | NR | NR | NR |
96 | [80] | F | NR | c.1213C>T | NR |
97 | [96] | F | Indian | NR | NR |
98 | [97] | M | Arab | c.1213C>T | p.Phe405>Leu |
99 | [98] | F | Turkish | NR | NR |
100 | [99] | F | German | NR | NR |
101 | M | German | 627 delAGTTGGTGins GT | NR | |
102 | M | Turkish-Assyrian | 793–4 ins C | NR | |
103 | F | Turkish-Assyrian | 793–4 ins C | NR | |
104 | M | German | NR | NR | |
105 | M | German | NR | NR | |
106 | M | Italian (?) | c.1213C>T | NR | |
107 | F | Italian (?) | c.889C>T | NR | |
108 | M | English | 1363 del G and 1405C>T | NR | |
109 | M | English | 1364 del G and 1405C>T | NR | |
110 | M | Caucasian | 1264 G>A and 469C>T | NR | |
111 | M | Turkish | 449 del T | NR | |
112 | F | Turkish | 450 del T | NR | |
113 | M | Turkish | c.1405C>T | NR | |
114 | M | Caucasian | c.1405C>T and 1008 ins A | NR | |
115 | M | Arabian | c.1213C>T | NR | |
116 | M | Polish (?) | NR | NR | |
117 | F | Polish (?) | c.469C>T | NR | |
118 | F | Polish (?) | NR | NR | |
119 | M | Algerian | IVS 6 +1 G>C | NR | |
120 | M | Moroccan | 1288–9TC>AA | NR | |
121 | F | NR | c.1562C>T and IVS 8 + | NR | |
122 | 1 G>A | NR | |||
123 | M | Algerian | IVS 5 +5 G>C | NR | |
124 | M | Algerian | IVS 5 +5 G>C | NR | |
125 | F | French (?) | 1573 ins GT and 1751C>G | NR | |
126 | M | French (?) | 1574 ins GT and 1751C>G | NR | |
127 | F | Italian | 1264G>A | NR | |
128 | F | Italian | 371G>A and 1751C>G | NR | |
129 | M | Turkish | 1562C>T | NR | |
130 | F | NR | IVS 6 +1 g>a | NR | |
131 | M | NR | NR | NR | |
132 | M | NR | NR | NR | |
133 | F | French-Canadian | 494 ins 26 and 1751C>G | NR | |
134 | F | Eskimo | 1415–6 del TC | NR | |
135 | M | Arabian | 1213C>T | NR | |
136 | F | NR | IVS 8 +1 G>A | NR | |
137 | F | NR | NR | NR | |
138 | F | Turkish-Assyrian | 793–4 ins C | NR | |
139 | F | Greek | 712–3 del CT | NR | |
140 | M | Algerian | IVS 3 +2 T>C | NR | |
141 | M | NR | 1092C>A | NR | |
142 | M | Turkish | 738 del 17 | NR | |
143 | F | Turkish | IVS 5 +1 G>T | NR | |
144 | [100] | M | Japanese | c.1405C>T and c.1642T>C | NR |
Missense Mutations | Nonsense Mutations | fs/indel Mutations | Intronic Mutations | Compound Heterozygous Mutations |
---|---|---|---|---|
G20E | K5X | I39 | c.497-2A>T | p.Ala127Asp and p.324TyrfsX392 |
N32K | R53X | L153_I154 | c.108+5G>A | p. Arg365Ter and p. Trp444Arg |
R158S | E66X | C239 | IVS 3+2T>C | Q287X and L389P |
S203R | S169X | V355_S356 | c.963+1G>A | Gly20Glu and T480R |
S242R | Q193X | V45 | c.776-1G>C | T480R and L490SfsX24 |
G318R | R228X | V60 | IVS5+1 G>T | p.153_4delLI and p.P417R |
S326K | Q287X | A105 | IVS 2 - 2 A>G | E85fsX177 and G189D |
M376R | R301X | I133 | IVS4+1G>A | p. Arg228X and p. Trp395X |
L389P | R365X | S145 | IVS 8+1 G>T | p. Glu66X and p. Met373X |
G416S | W420X | S161 | IVS 5-1 G>A | |
P417L | M350 | c.16-1G>A or IVS 1-1G>A | ||
P417R | L368 | IVS8g.24401-24406del6 | ||
V423E | W420 | c.1068+5 G>C | ||
W444R | Glu85fs | |||
T480R | E279KfsX6 | |||
His192Arg | Val357AsnfsTer37 | |||
Arg124Ser | Gly162ArgfsTer17 | |||
Leu19Pro ** | A229QFsX19 | |||
p.Phe405>Leu | Phe114LeufsX16 | |||
Gln166AspfsTer4 | ||||
Cys224Del |
Type of Dysglycaemia | Mutation | Amino Acid Change | Reference |
---|---|---|---|
Transient neonatal diabetes | c.952G>A | p.Gly318Arg | [55] |
c.609 T>A | p.Ser203Arg | [74] | |
c.1127 T>G | p.Met376Arg | [74] | |
c.963+1G>A | NR | [74] | |
c.157C>T | p.Arg53X | [74] | |
c.339del | p.Phe114LeufsX16 | [74] | |
322 A>T | K5X | [83] | |
Glucose intolerance/diabetes mellitus | c.482_483insC | p. Gly162ArgfsTer17 | [58] |
c.575A>G | p. His192Arg | [58] | |
c.56 T>C | p. Leu19Pro ** | [72] | |
Gestational diabetes | c.1439C>G and c.1469delA | T480R and L490SfsX24 | [78] |
NR | valine 197 to isoleucine | [4] | |
Other: 2 patients [101], and 1 patient [102] | |||
Fasting hypoglycemia | c.108+5G>A | NR | [57] |
783del17 | NR | [81] | |
818C>G | NR | [81] | |
IVS5+1 G>T | NR | [81] | |
c.1580T>A | V423E | [86] | |
IVS 2 - 2 A>G | NR | [86] | |
c.952G>A | p.Gly318Arg | [55] | |
NR | E85fsX177 and G189D | [60] | |
NR | NR | [62] | |
NR | NR | [91] | |
NR | NR | [103] | |
c.1246 G>A | p. Gly416Ser | [61] | |
c.339delC | p. Phe114LeufsTer16 | [67] | |
c.339delC | p. Phe114LeufsTer16 | [67] | |
Post-prandial hyperglycemia | c.1061_1066del6 | p.V355_S356del2 | [69] |
IVS8g.24401-24406del6 | NR | [54] | |
NR | NR | [73] | |
NR | NR | [96] | |
Fasting hypoglycemia and postprandial hyperglycemia | c.1069delGinsAATAA | p. Val357AsnfsTer37 | [58] |
c.482_483insC | p. Gly162ArgfsTer17 | [58] | |
c.482_483insC | p. Gly162ArgfsTer17 | [58] | |
c.482_483insC | p. Gly162ArgfsTer17 | [58] | |
c.482_483insC | p. Gly162ArgfsTer17 | [58] | |
c.482_483insC | p. Gly162ArgfsTer17 | [58] | |
c.901C > T | p. Arg301Ter | [66] | |
c.16-1G>A or IVS 1-1G>A | [64] | ||
c.380C>A and c.970dupT | p.Ala127Asp and p.324TyrfsX392 | [68] | |
c.1068+5 G>C | IVS8+5G>C | [68] | |
c.1194T>A | p.Tyr398X | [68] | |
c.1250C>T | p. P417L | [76] | |
IVS 3+2t>c/IVS 3+2t>c) | NR | [70] | |
c. 685_70l del GCCATCCTTCAGTCTCTins CAGAAAA | P.A229QFsX19 | [71] | |
c.253_254delGA | p. Glu85fs | [77] | |
c.776-1G>C | NR | [77] | |
c.835_836delGA | p.E279KfsX6 | [79] | |
C1213T | NR | [80] | |
96T>G | N32K | [84] | |
c.1171C>T and c.1478T>C | Q287X and L389P | [86] | |
c.1213C>T | R301X | [89] | |
ΔT446-449 | [6] | ||
ΔT446-449 | [6] | ||
C1405T | R365X | [6] | |
c.1213 C>T | p.Phe405>Leu | [97] | |
C.685_701del GCCATCCTTCAGTCTCT ins CAGAAAA | p.A229 QfsX19 | [59] | |
c.670 | Cys224Del | [65] | |
c.682C>T and c.1185 G>A | p. Arg228X and p. Trp395X | [94] | |
c.196G>T and c.1117delA | p. Glu66X and p. Met373X | [94] | |
c.1330 T>C | p. W444R | [10] |
Mutation | Birth Weight (kg) | References | |
---|---|---|---|
DNA | Protein | ||
Missense | |||
c.609T>A | p.Ser203Arg | 1.85 | [74] |
c.1127T>G | p.Met376Arg | 2.5 | [74] |
c.952G>A | p.Gly318>Arg | 2.4 | [55] |
c.952G>A | p.Gly318>Arg | 2.8 | [55] |
c.952G>A | p.Gly318>Arg | 2.3 | [55] |
c.1213C>T | p.Phe405>Leu | 3.23 | [97] |
Non-sense | |||
c.901C>T | p.Arg301X | 2.8 | [66] |
c.901C>T | p.Arg301X | 2.2 | [66] |
fs/indel | |||
c.322A>T | p.Lys5>X | 2 | [83] |
c.339delC | p.Phe114LeufsX16 | 2.5 | [74] |
c. 685_701 del GCCATCCTTCAGTCTCT ins CAGAAAA | P.A229QFsX19 | 2.6 | [71] |
c.1069delGinsAATAA | p. Val357AsnfsTer37 | 3 | [58] |
C.685_701del GCCATCCTTCAGTCTCT ins CAGAAAA | p.A229 QfsX19 | 2.6 | [59] |
c.783del17 | 2.6 | [81] | |
c.670 | Cys224Del | 2.09 | [65] |
Intronic | |||
c.963+1G>A | NR | 2 | [74] |
c.16-1G>A or IVS 1- 1G>A | NR | 2.5 | [64] |
IVS8 g.24401-24406del6 | NR | 2.6 | [54] |
c.963+1 G>A | NR | 2.05 | [75] |
(IVS2+5G>A[c.108+5G>A]) | NR | 3.25 | [57] |
Compound Heterozygous | |||
c.457_462delCTTATA in Exon 4 and c.1250C>G in Exon 10 | (p.153_4delLI) and (p.Pro417Arg) | 3.773.97 | [93] |
E85fsX177 and G189D | 3.0 | [60] | |
Undefined | |||
2.8 | [62] | ||
2.5 | [63] | ||
2.9 | [73] | ||
2.1 | [96] | ||
2.5 | [95] | ||
2.8 | [104] |
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Share and Cite
Sharari, S.; Abou-Alloul, M.; Hussain, K.; Ahmad Khan, F. Fanconi–Bickel Syndrome: A Review of the Mechanisms That Lead to Dysglycaemia. Int. J. Mol. Sci. 2020, 21, 6286. https://doi.org/10.3390/ijms21176286
Sharari S, Abou-Alloul M, Hussain K, Ahmad Khan F. Fanconi–Bickel Syndrome: A Review of the Mechanisms That Lead to Dysglycaemia. International Journal of Molecular Sciences. 2020; 21(17):6286. https://doi.org/10.3390/ijms21176286
Chicago/Turabian StyleSharari, Sanaa, Mohamad Abou-Alloul, Khalid Hussain, and Faiyaz Ahmad Khan. 2020. "Fanconi–Bickel Syndrome: A Review of the Mechanisms That Lead to Dysglycaemia" International Journal of Molecular Sciences 21, no. 17: 6286. https://doi.org/10.3390/ijms21176286