Molecular Mechanisms of Crosstalk Between Glucose and Lipid Metabolism in the Initiation and Progression of Metabolic Diseases
Molecular Mechanisms of Crosstalk Between Glucose and Lipid Metabolism in the Initiation and Progression of Metabolic Diseases
Glucose metabolism and lipid metabolism together constitute the core network that sustains systemic energy homeostasis, biosynthesis, and signaling responses. Excess glucose can drive lipid production, whereas lipid intermediates can in turn interfere with insulin sensitivity, inflammatory status, and energy utilization efficiency. Accordingly, the initiation and progression of metabolic diseases are, in essence, systemic consequences of disrupted crosstalk between glucose and lipid metabolism.
Keywords: glucose-lipid metabolism; metabolic reprogramming; insulin resistance; de novo lipogenesis; diacylglycerol; ceramide; O-GlcNAc; hepatic steatosis; inter-organ crosstalk; metabolic disease
I. Why Crosstalk Between Glucose and Lipid Metabolism Constitutes a Core Framework in Metabolic Disease Research
1.1 Glucose metabolism and lipid metabolism share substrates, signaling pathways, and regulatory layers
(1) Glucose metabolism provides the substrate basis for lipid synthesis
After entering the cell, glucose is not only used for glycolysis and oxidative energy production, but may also enter fatty acid synthesis pathways through intermediate metabolites such as pyruvate, citrate, and acetyl-CoA. Thus, increased glucose intake does not merely mean an increased glycemic burden, but also signifies a concurrent increase in substrates available for lipid generation.
(2) Lipid metabolic intermediates reversely shape glucose signaling pathways
Lipid accumulation is not simply a storage phenomenon. Diacylglycerol, ceramide, and specific acyl-CoA species can directly interfere with insulin signal transduction, membrane receptor organization, and mitochondrial function, thereby suppressing glucose uptake, glycogen synthesis, and the inhibitory effect on gluconeogenesis.
1.2 Metabolic diseases are essentially consequences of glucose-lipid network remodeling
(1) A single “high-glucose” or “high-lipid” framework is insufficient to explain disease progression
Obesity, type 2 diabetes, and metabolic dysfunction-associated fatty liver disease are commonly accompanied by abnormalities in glucose metabolism, lipotoxicity, chronic inflammation, and endocrine imbalance. Their essence is not a defect in a single pathway, but rather a network-level pathological state caused by disordered allocation of glucose and lipid flux.
(2) Different tissues play distinct roles in glucose-lipid imbalance
The liver is responsible for substrate integration and output, adipose tissue for energy storage and buffering, skeletal muscle for glucose clearance, and pancreatic β-cells for compensatory secretion. Dysfunction in these tissues amplifies one another and ultimately gives rise to systemic metabolic abnormalities.
II. Glucose-Driven Lipid Generation Is an Important Upstream Origin of Disrupted Glucose-Lipid Crosstalk
2.1 Excess glucose can actively drive de novo lipogenesis
(1) Glucose metabolic intermediates possess dual roles as substrates and signals
Intermediate metabolites such as glucose-6-phosphate and fructose-6-phosphate not only reflect the state of glycolysis, but also serve as nutrient-excess signals that enhance the expression of lipid synthesis-related genes.
(2) Conversion of glucose to lipid evolves from an adaptive process into a pathological process
Under short-term nutrient abundance, conversion of glucose to lipid helps package and store energy. However, under chronic high-glucose conditions, persistent enhancement of this process can drive hepatic lipid deposition, ectopic lipid storage, and lipotoxic accumulation.
2.2 Nutrient-sensing transcriptional axes determine the strength of glucose-to-lipid conversion
(1) ChREBP is a central regulator of glucose-driven lipogenesis
ChREBP can translate changes in glucose metabolic intermediates into changes in the expression of lipid synthesis genes, making it a key transcriptional node linking glucose load to de novo lipogenesis.
(2) SREBP-1c participates in insulin-dependent lipogenic programs
Under hyperinsulinemic conditions, activation of SREBP-1c enhances fatty acid synthesis and triglyceride assembly, thereby aggravating glucose-lipid metabolic reprogramming in the liver.
2.3 Glucose nutrient sensing can also amplify metabolic reprogramming through the modification layer
(1) O-GlcNAcylation links nutrient state to signaling regulation
The hexosamine pathway can integrate glucose and other nutrient fluxes into the donor substrate UDP-GlcNAc, thereby driving protein O-GlcNAcylation and altering the functional state of transcription factors, metabolic enzymes, and signaling proteins.
(2) This modification layer is deeply involved in lipolysis and pancreatic islet compensation
O-GlcNAcylation can regulate lipolysis in adipose tissue, thermogenic capacity, and the compensatory secretory response of pancreatic β-cells to glucose-lipid stimulation. It is therefore an important upper-level regulatory mechanism in glucose-lipid crosstalk.
III. Key Enzymatic Nodes Determine the Direction and Strength of Glucose-Lipid Crosstalk
3.1 Crosstalk between glucose and lipid metabolism is not determined solely by metabolite concentrations
(1) Key enzymes determine the direction of carbon flux
Whether glucose enters oxidative energy production, glycogen storage, or is redirected toward fatty acid synthesis depends first on the activity state of key enzymes, rather than solely on total substrate abundance.
(2) Key enzymes determine lipid fate
Whether fatty acids enter β-oxidation, triglyceride storage, or are converted into signaling lipids such as diacylglycerol and ceramide is likewise determined by key enzymatic systems.
3.2 Key enzymes involved in glucose-lipid crosstalk
Enzyme Name | Major Metabolic Step | Main Function | Significance in Glucose-Lipid Crosstalk | Related Pathological Consequences |
Glucokinase | Initial phosphorylation of glucose | Promotes glucose entry into intracellular metabolism | Determines the initiation intensity of glycolysis and glucose-to-lipid conversion | Abnormal hepatic glucose metabolism; enhanced lipid generation |
Phosphofructokinase | Rate-limiting step of glycolysis | Regulates glycolytic flux | Influences whether glucose-derived carbon is directed toward energy production or biosynthesis | Reduced metabolic flexibility |
Pyruvate Dehydrogenase Complex | Pyruvate oxidation | Generates acetyl-CoA | Connects glucose oxidation with fatty acid synthesis | Enhanced glucose-to-lipid conversion |
ATP-Citrate Lyase (ACLY) | Citrate cleavage | Generates cytosolic acetyl-CoA | A key hub by which glucose-derived carbon enters fatty acid synthesis | Hepatic steatosis |
Acetyl-CoA Carboxylase (ACC) | Initiation of fatty acid synthesis | Generates malonyl-CoA | Enhances de novo fatty acid synthesis and inhibits fatty acid oxidation | Lipid accumulation |
Fatty Acid Synthase (FASN) | De novo lipogenesis | Synthesizes long-chain fatty acids | Directly executes conversion of glucose-derived carbon into stored lipids | Steatosis; obesity-related lipid overload |
Stearoyl-CoA Desaturase 1 (SCD1) | Fatty acid remodeling | Generates monounsaturated fatty acids | Alters the tendency toward lipid droplet formation and lipotoxicity | Lipid droplet accumulation; membrane lipid remodeling |
Glycerol Kinase (GK) | Glycerol metabolism and triglyceride re-synthesis | Catalyzes the conversion of glycerol to glycerol-3-phosphate | Links lipolysis-derived glycerol with triglyceride re-synthesis and gluconeogenic substrate utilization, serving as an important bridge enzyme for glucose-lipid substrate redistribution | Enhanced hepatic lipid re-esterification; altered allocation of gluconeogenic substrates; aggravated hepatic glucose-lipid imbalance |
Diacylglycerol Acyltransferase (DGAT) | Final step of triglyceride synthesis | Catalyzes conversion of DAG to TAG | Determines whether DAG is buffered or continues to accumulate | Triglyceride accumulation or amplification of DAG toxicity |
Adipose Triglyceride Lipase (ATGL) | Initiation of lipolysis | Catalyzes triglyceride breakdown | Controls lipolytic output from adipose tissue | Overflow of free fatty acids |
Hormone-Sensitive Lipase (HSL) | Intermediate step of lipolysis | Hydrolyzes diacylglycerol and related lipids | Determines the strength of lipid droplet mobilization | Aggravated ectopic lipid deposition |
Carnitine Palmitoyltransferase 1 (CPT1) | Entry into β-oxidation | Promotes mitochondrial import of long-chain fatty acids | Determines lipid clearance capacity | Insufficient fatty acid oxidation |
Acyl-CoA Oxidase 1 (ACOX1) | Peroxisomal β-oxidation | Catalyzes the initial oxidation of very-long-chain fatty acids | Affects processing of specialized lipids and peripheral lipid signaling | Systemic metabolic imbalance |
Protein Kinase Cε (PKCε) | DAG signaling pathway | Responds to membrane DAG accumulation | Mediates hepatic insulin resistance | Impaired insulin signaling |
Ceramide Synthase (CerS) | Sphingolipid synthesis | Generates ceramides with specific acyl-chain lengths | Determines the toxicity spectrum of ceramides | Insulin resistance in muscle and liver |
O-GlcNAc Transferase (OGT) | O-GlcNAc modification | Catalyzes protein O-GlcNAcylation | Links glucose nutrient sensing with lipolysis and islet compensation | Reduced metabolic flexibility |
O-GlcNAcase (OGA) | Removal of O-GlcNAc modification | Removes protein O-GlcNAc | Maintains the dynamic balance of this modification | Persistent abnormal signaling |
IV. Lipid Intermediates Are the Key Effector Layer Through Which Glucose-Lipid Imbalance Converts into Insulin Resistance
4.1 Diacylglycerol is an important signaling molecule in hepatic insulin resistance
(1) Membrane-localized DAG possesses stronger pathological activity
What is most closely associated with insulin resistance is not total DAG abundance per se, but rather specific DAG species that accumulate abnormally within membrane compartments. These molecules are more likely to activate PKCε and thereby suppress downstream insulin receptor signaling.
(2) Enhanced glucose-to-lipid conversion continuously amplifies DAG burden
Under high-glucose and hyperinsulinemic conditions, increased de novo lipogenesis and triglyceride synthesis make DAG, as an intermediate, more prone to accumulation, thereby forming a critical bridge between glucose excess and signaling lipotoxicity.
4.2 Ceramide represents another major lipotoxic axis
(1) Ceramide can actively suppress insulin signaling
Ceramide can inhibit Akt activation, disturb membrane structure, and impair mitochondrial function. It therefore represents an actively regulatory lipid species rather than a simple storage product.
(2) Ceramide toxicity is species- and tissue-specific
Ceramides of different chain lengths do not exert identical effects in skeletal muscle, liver, and adipose tissue. This is one of the reasons current research has shifted from focusing on “total sphingolipid levels” toward “molecular-species-resolved analysis.”
V. Inter-Organ Crosstalk Amplifies the Systemic Effects of Glucose-Lipid Metabolic Imbalance
5.1 The liver is the central hub for glucose-lipid integration and output
(1) The liver simultaneously controls glucose and lipid flux
The liver regulates gluconeogenesis and glycogen metabolism while also participating in fatty acid synthesis, lipid oxidation, and lipoprotein export. It is therefore one of the most concentrated organs for glucose-lipid crosstalk.
(2) Hepatic abnormalities spill over systemically
Metabolic reprogramming in the liver alters circulating lipid profiles, the intensity of glucose output, and the secretion of hepatokines, thereby further influencing adipose tissue, skeletal muscle, and pancreatic islets.
5.2 Adipose tissue is both a buffer and a pathological amplifier
(1) Failure of adipose tissue buffering is a turning point in disease progression
When adipose tissue can no longer safely continue storing lipids, overflow of free fatty acids increases and ectopic lipid deposition rapidly worsens. At this stage, systemic metabolic imbalance enters an accelerated phase.
(2) Changes in the adipose secretory profile can remodel whole-body metabolism
Under overload conditions, adipose tissue alters the output of adipokines, inflammatory mediators, and stress signals, thereby exerting sustained effects on the liver, muscle, and pancreatic islets.
5.3 Skeletal muscle and pancreatic islets represent the clearance side and compensatory side, respectively
(1) Lipotoxicity in skeletal muscle directly affects glucose clearance
Skeletal muscle is the major tissue responsible for insulin-dependent glucose uptake. Accordingly, lipotoxic accumulation within skeletal muscle can rapidly amplify the risk of systemic hyperglycemia.
(2) Islet compensation may ultimately progress to failure
In early stages, β-cells can respond to peripheral insulin resistance by increasing insulin secretion. However, chronic lipotoxicity, oxidative stress, and inflammation progressively weaken this compensatory capacity.
VI. How Disrupted Glucose-Lipid Crosstalk Drives the Development of Major Metabolic Diseases
6.1 Obesity is the initiating disease state of disordered glucose-lipid allocation
(1) Expansion of adipose tissue shifts from adaptation to pathology
Obesity is not merely characterized by increased fat mass, but reflects the transition of adipose tissue from adaptive energy storage toward inflammation, dysfunction, and failure of buffering capacity.
(2) Chronic low-grade inflammation and glucose-lipid imbalance mutually reinforce each other
Inflammation in adipose tissue can impair insulin sensitivity, whereas glucose-lipid imbalance feeds back to intensify inflammation. This positive feedback loop drives the progression of obesity toward systemic metabolic dysfunction.
6.2 Metabolic dysfunction-associated fatty liver disease is a representative organ phenotype of disrupted glucose-lipid crosstalk
(1) Hepatic steatosis reflects abnormally enhanced glucose-to-lipid conversion
Under conditions of high glucose, high lipid supply, and high insulin, the liver persistently enhances de novo lipogenesis. This is one of the most intuitive organ-level manifestations of disrupted glucose-lipid crosstalk.
(2) Liver pathology further spills over into systemic abnormalities
Hepatic steatosis is not the pathological endpoint, but rather a source that further drives lipid abnormalities, insulin resistance, and inflammatory amplification.
6.3 Type 2 diabetes reflects a global mismatch of the glucose-lipid network
(1) It is not simply a disease of hyperglycemia
Type 2 diabetes is the systemic outcome jointly driven by tissue insulin resistance, lipotoxic accumulation, and β-cell functional failure.
(2) The dominant pathological axis differs across individuals
In different patients, dysfunction may be primarily driven by abnormalities in the liver, adipose tissue, skeletal muscle, or pancreatic islets. Therefore, both research stratification and clinical stratification must take heterogeneity into account.
6.4 Correspondence between major metabolic diseases and disrupted glucose-lipid crosstalk
Disease/State | Main Features of Glucose-Lipid Imbalance | Key Molecules or Pathways | Typical Consequences |
Obesity | Enhanced glucose-to-lipid conversion; reduced buffering capacity of adipose tissue | ChREBP, OGT, adipose tissue lipolysis axis | Ectopic lipid deposition; chronic inflammation |
Hepatic insulin resistance / metabolic dysfunction-associated fatty liver disease | Enhanced hepatic DNL, membrane DAG accumulation, increased lipotoxicity | ACLY, ACC, FASN, PKCε | Hepatic steatosis; failure to suppress gluconeogenesis |
Muscle insulin resistance | Ceramide accumulation; restricted glucose oxidation | CerS, CPT1-related oxidative imbalance | Reduced glucose clearance; aggravated systemic insulin resistance |
Early compensatory phase of type 2 diabetes | Enhanced islet secretion under dual glucose-lipid stimulation | O-GlcNAc modification, nutrient-sensing pathways | Compensatory hyperinsulinemia |
Decompensated type 2 diabetes | Coexistence of tissue insulin resistance and β-cell failure | Disrupted multi-organ glucose-lipid crosstalk | Persistent hyperglycemia together with lipid metabolic abnormalities |
VII. Relevant Pathways, Key Targets, and Analytical Indicators in Glucose-Lipid Crosstalk Research
7.1 Organization of research pathways
(1) Glucose-driven lipogenesis pathway
This direction focuses on the full process by which glucose proceeds through glycolysis, citrate export, acetyl-CoA generation, and de novo fatty acid synthesis. The core pathway is the ChREBP-SREBP-1c-DNL axis, which is well suited to studies of hepatic steatosis, obesity, and enhanced lipid generation under hyperglycemic conditions.
(2) Lipotoxicity-mediated insulin resistance pathway
This direction is centered primarily on the DAG-PKCε axis, the ceramide-Akt inhibitory axis, mitochondrial fatty acid oxidation imbalance, and stress-signaling pathways, and is suitable for explaining hepatic and muscular insulin resistance.
(3) Nutrient-sensing modification pathways
This direction focuses on O-GlcNAcylation, AMPK/mTOR signaling, and nutrient-sensing transcription factors in the maintenance of glucose-lipid balance, and is suitable for investigating reduced metabolic flexibility and early compensatory abnormalities.
(4) Inter-organ crosstalk pathways
This direction emphasizes communication among liver-derived lipid signals, adipose tissue-derived secreted factors, skeletal muscle substrate utilization states, and pancreatic islet compensatory responses, and represents an important expansion of current systems metabolism research.
7.2 Organization of key targets
(1) Upstream metabolic reprogramming targets
These include ChREBP, SREBP-1c, ACLY, ACC, FASN, and SCD1, and are mainly used to explain and intervene in enhanced glucose-to-lipid conversion and hepatic lipid deposition.
(2) Lipotoxic signaling targets
These include the DAG-PKCε axis, the CerS family, ceramide synthesis pathways, and lipid droplet mobilization-related enzymes, and are mainly used to explain insulin resistance and amplification of lipotoxic signaling.
(3) Energy sensing and metabolic flexibility targets
These include AMPK, CPT1, ACOX1, OGT, and OGA, and are mainly associated with fatty acid oxidation capacity, nutrient sensing, and metabolic adaptability.
(4) Inter-organ communication targets
These include adipose tissue-derived secreted factors, liver-derived signaling molecules, and receptor-level pathways, and are mainly used to explain how single-organ abnormalities are converted into systemic metabolic disease.
7.3 Organization of analytical indicators
(1) Basic metabolic phenotype indicators
① Fasting blood glucose, fasting insulin, HOMA-IR
② Parameters related to glucose tolerance and insulin tolerance
③ Serum triglycerides, total cholesterol, and free fatty acids
(2) Tissue metabolic burden indicators
① Hepatic triglyceride content
② DAG and ceramide levels in skeletal muscle and liver
③ Adipose tissue mass, lipid droplet size, and degree of inflammatory infiltration
(3) Molecular mechanistic indicators
① Expression levels of ChREBP, SREBP-1c, FASN, ACC, and SCD1
② PKCε activation state and Akt phosphorylation level
③ Expression and activity of the CerS family, OGT/OGA, CPT1, and ACOX1
(4) Advanced research indicators
① Glucose flux and de novo fatty acid synthesis rate under stable isotope tracing
② Lipidomic profiling of DAG, ceramide, and fatty acid molecular species
③ Spatial transcriptomics or spatial metabolomics analysis of intratissue heterogeneity
7.4 Correspondence among pathways, targets, and analytical indicators
Research Direction | Representative Pathway | Key Targets | Common Analytical Indicators |
Glucose-driven lipogenesis | ChREBP-SREBP-1c-DNL axis | ChREBP, ACLY, ACC, FASN, SCD1 | Hepatic TG, DNL rate, fatty acid composition, expression of related proteins |
Lipotoxicity and insulin resistance | DAG-PKCε axis, ceramide-Akt axis | PKCε, CerS, Akt-related nodes | DAG, ceramide subclassification, Akt phosphorylation, HOMA-IR |
Fatty acid oxidation and metabolic flexibility | CPT1-β-oxidation, ACOX1 pathway | CPT1, ACOX1, AMPK | β-oxidation capacity, mitochondrial function, respiratory quotient |
Nutrient-sensing modification regulation | O-GlcNAc modification axis | OGT, OGA | Protein O-GlcNAc levels, islet compensatory indices, lipolysis/thermogenesis indices |
Inter-organ crosstalk | Liver-adipose-muscle-islet communication | Liver-derived signals, adipose tissue-secreted factors | Circulating lipid profiles, adipokines, tissue-specific metabolic phenotypes |
VIII. Aladdin-Related Products
8.1 Products Related to Glucose-Driven Lipid Generation
Catalog No. | Name | Grade and Purity | Suitable Research Direction/Application |
AM 2394 | ≥98%(HPLC) | Enhancement of initial glucose phosphorylation; studies on glycolytic initiation and glucose-to-lipid conversion driving mechanisms | |
GKA 50 | ≥98%(HPLC) | GK activation; studies related to abnormal hepatic glucose metabolism and enhanced lipid generation | |
Rat Glucokinase (GK) ELISA Kit | BioReagent | Detection of rat GK expression; evaluation of glucose metabolic entry intensity | |
Mouse Glucokinase (GK) ELISA Kit | BioReagent | Detection of mouse GK expression; studies on hepatic glucose-to-lipid conversion | |
Glucokinase (GK) Activity Assay Kit (UV Colorimetric Method) | BioReagent | Detection of GK activity; analysis of glycolytic initiation capacity | |
Glucokinase (GK) Activity Assay Kit (Micro Method) | BioReagent | Detection of GK activity; analysis of glucose metabolic phenotypes in micro-volume samples | |
Recombinant Glucose Kinase (GLCK) | Bioactive, ActiBioPure™, High Performance, EnzymoPure™, ≥90%(SDS-PAGE), ≥200 U/mg protein | GK enzymology studies; validation of coupling mechanisms between glucose metabolic entry and glucose-to-lipid conversion | |
Human Phosphofructokinase, Muscle (PFKM) ELISA Kit | BioReagent | Detection of PFKM expression; studies on glycolytic rate limitation and muscle metabolic flexibility | |
Human 6-phosphofructokinase, Liver Type (PFKL) ELISA Kit | BioReagent | Detection of PFKL expression; studies on hepatic glycolytic flux and glucose-to-lipid shift | |
Phosphofructokinase (PFK) Activity Assay Kit (UV Micro Method) | BioReagent | Detection of PFK activity; studies on the rate-limiting step of glycolysis | |
Phosphofructokinase,Bacillus stearothermophilus |
| PFK enzymology studies; analysis of mechanisms governing allocation of glucose-derived carbon to energy production or biosynthesis | |
Phosphofructokinase 1 |
| Functional validation of PFK1; mechanistic studies related to reduced metabolic flexibility | |
Pyruvate Dehydrogenase (PDH) Activity Assay Kit (DCPIP, Micro Method) | BioReagent | Detection of PDH activity; studies on glucose oxidation and acetyl-CoA output | |
ATP Citrate Lyase (ACL) Activity Assay Kit (UV Micro Method) | BioReagent | Detection of ACLY activity; analysis of cytosolic acetyl-CoA generation capacity | |
ATP Citrate Lyase (ACL) Activity Assay Kit (UV Colorimetric Method) | BioReagent | Detection of ACLY activity; studies on the hub by which glucose-derived carbon enters fatty acid synthesis | |
BMS 303141 | ≥98% | ACLY inhibition; studies on hepatic steatosis and glucose-driven lipid generation | |
SB 204990 | ≥98%(HPLC) | ACLY inhibition; intervention studies on upstream pathways of de novo lipogenesis | |
PF 05175157 | ≥98%(HPLC) | ACC1/2 inhibition; studies on the balance between de novo fatty acid synthesis and fatty acid oxidation | |
Acetyl CoA Carboxylase (ACC) Activity Assay Kit (AHM, Micro Method) | BioReagent | Detection of ACC activity; studies on malonyl-CoA generation and lipid accumulation | |
Acetyl-CoA Carboxylase (ACC) Activity Assay Kit (AHM, Colorimetric Method) | BioReagent | Detection of ACC activity; evaluation of mechanisms related to enhanced glucose-to-lipid conversion | |
Human Acetyl Coenzyme A Carboxylase Alpha (ACACa) ELISA Kit | BioReagent | Detection of human ACACA expression; studies on initiation of de novo fatty acid synthesis | |
Rat Acetyl Coenzyme A Carboxylase Alpha (ACACA) ELISA Kit | BioReagent | Detection of rat ACCα expression; studies on hepatic lipid deposition | |
Mouse Acetyl-CoA Carboxylase(AACase) ELISA Kit | BioReagent | Detection of mouse ACC expression; evaluation of metabolic reprogramming models | |
Fatty Acid Synthase (FAS) Activity Assay Kit (UV Micro Method) | BioReagent | Detection of FASN activity; analysis of de novo lipogenic capacity | |
Fatty Acid Synthase (FAS) Activity Assay Kit (UV Colorimetric Method) | BioReagent | Detection of FASN activity; studies on obesity-related lipid overload | |
Human Stearoyl Coenzyme A Desaturase (SCD) ELISA Kit | BioReagent | Detection of SCD/SCD1 expression; studies on monounsaturated fatty acid generation and membrane lipid remodeling | |
Glycerol kinase | EnzymoPure™, ≥25u/mg,derived from Arthrobacter | Studies on glycerol reutilization; analysis of triglyceride re-synthesis and gluconeogenic substrate allocation | |
Glycerol Kinase (GK) | Bioactive, ActiBioPure™, EnzymoPure™, High Performance, ≥90%(SDS-PAGE), ≥180 U/mg protein | Functional validation of glycerol kinase; studies on hepatic glucose-lipid imbalance | |
Recombinant Glycerol Kinase (GK) | Bioactive,Recombinant,ActiBioPure™,High Performance,EnzymoPure™,≥30 U/mg enzyme powder | Recombinant GK enzymology studies; studies on glycerol-3-phosphate generation and lipid re-esterification |
8.2 Products Related to DAG/TAG Partitioning and Lipid Droplet Mobilization
Catalog No. | Name | Grade and Purity | Suitable Research Direction/Application |
A922500 | ≥98% | DGAT1 inhibition; studies on DAG-to-TAG buffering capacity | |
ABT-046 |
| DGAT1 inhibition; studies on terminal control of triglyceride synthesis | |
AZD 3988 | ≥98%(HPLC) | DGAT1 inhibition; studies on DAG accumulation and amplification of lipotoxicity | |
AZD7687 | Moligand™, ≥98% | DGAT1 inhibition; studies on hepatic lipid re-esterification | |
Amidepsine D | ≥95% | DGAT inhibition; studies on TAG generation and lipid droplet formation | |
DGAT-1 inhibitor 2 | 10mM in DMSO | DGAT1 inhibition; studies of cellular DAG/TAG partitioning | |
DGAT-1 inhibitor 2 | ≥95% | DGAT1 inhibition; studies on lipid droplet biogenesis | |
DGAT1 Human Pre-designed siRNA Set A |
| DGAT1 gene silencing; studies on failure of DAG buffering mechanisms | |
DGAT1-IN-1 | ≥95% | DGAT1 inhibition; intervention studies on the terminal step of TAG synthesis | |
DGAT1-IN-1 | 10mM in DMSO | DGAT1 inhibition; studies on lipid droplet formation in cell models | |
DGAT1-IN-3 | 10mM in DMSO | DGAT1 inhibition; studies on lipid storage and DAG accumulation | |
DGAT1-IN-3 | ≥99% | DGAT1 inhibition; studies on amplification mechanisms of glucose-lipid toxicity | |
DGAT2 Human Pre-designed siRNA Set A |
| DGAT2 gene silencing; studies on hepatic TAG synthesis and steatosis | |
DGAT2-IN-3 |
| DGAT2 inhibition; studies on lipid droplet maturation and triglyceride storage | |
IONIS-DGAT 2Rx |
| DGAT2-targeted silencing; studies on hepatic lipid deposition | |
IONIS-DGAT 2Rx sodium |
| DGAT2-targeted silencing; studies on fatty liver and glucose-lipid imbalance | |
JNJ DGAT2-A | ≥98% | DGAT2 inhibition; studies on hepatic TAG generation and steatosis | |
JNJ-DGAT1-A |
| DGAT1 inhibition; studies on TAG synthesis regulation | |
JNJ-DGAT2-A | Moligand™, 10 mM in DMSO | DGAT2 inhibition; studies on DAG/TAG balance | |
LCQ-908 | Moligand™ | DGAT1 inhibition; studies on hepatic re-esterification and lipid droplet formation | |
PF 06424439 | ≥98%(HPLC) | DGAT2 inhibition; studies on triglyceride storage and steatosis | |
PF-04620110 | Moligand™, ≥99% | DGAT1 inhibition; studies on metabolic lipid deposition | |
Atglistatin | 10mM in DMSO | ATGL inhibition; studies on initiation of lipolysis and free fatty acid overflow | |
COP1-ATGL modulator 1 | ≥99% | ATGL-related modulation; studies on lipid droplet mobilization intensity | |
COP1-ATGL modulator 1 | Moligand™, 10 mM in DMSO | ATGL-related modulation; studies on lipolysis and lipid droplet homeostasis | |
Human Adipose Triglyceride Lipase (ATGL) ELISA Kit | BioReagent | Detection of ATGL expression; studies on lipolytic output from adipose tissue | |
Human Hormone Sensitive Lipase (HSL) ELISA Kit | BioReagent | Detection of HSL expression; studies on lipid droplet mobilization and ectopic lipid deposition |
8.3 Products Related to Fatty Acid Oxidation and Metabolic Flexibility
Catalog No. | Name | Grade and Purity | Suitable Research Direction/Application |
Acyl-CoA oxidase (ACO) | Recombinant, ActiBioPure™, EnzymoPure™, High Performance, ≥80%(SDS-PAGE), ≥30 U/mg protein | Studies on ACOX1-related peroxisomal β-oxidation; evaluation of specialized lipid clearance capacity | |
Acyl-CoA oxidase (ACO) | Bioactive,Recombinant,ActiBioPure™,High Performance,EnzymoPure™,8-12 U/mg enzyme powder | Functional validation of ACOX1; studies on fatty acid oxidation and metabolic flexibility |
8.4 Products Related to O-GlcNAc Modification and Glucose-Lipid Crosstalk Regulation
Catalog No. | Name | Grade and Purity | Suitable Research Direction/Application |
OGT Human Pre-designed siRNA Set A |
| OGT gene silencing; studies on glucose nutrient sensing and lipolysis/islet compensation | |
OGT-IN-2 | Moligand™, 10 mM in DMSO | OGT inhibition; intervention studies on O-GlcNAc modification levels | |
OGT-IN-4 |
| OGT inhibition; studies on upper-layer modification mechanisms in glucose-lipid crosstalk regulation | |
OSMI-1 | ≥98% | OGT inhibition; studies on reduced metabolic flexibility and abnormal islet compensation | |
Recombinant OGT Antibody | ExactAb™, Validated, Recombinant, 0.6 mg/mL | Detection of OGT protein; expression analysis of the O-GlcNAc modification axis | |
Recombinant OGT Antibody | KD Validation | Detection of OGT protein; validation of gene silencing and mechanistic studies | |
ST 045849 | ≥98%(HPLC) | OGT inhibition; studies on glucose-lipid metabolic crosstalk and persistent signaling abnormalities | |
Human O-Linked-N-Acetylglucosamine Transferase(OGT) ELISA Kit | BioReagent | Detection of OGT expression; evaluation of the nutrient-sensing modification axis | |
O-GlcNAcase-IN-2 |
| OGA inhibition; studies on dynamic balance of O-GlcNAc removal |
Crosstalk between glucose and lipid metabolism is not a simple competition between two categories of substrates, glucose and fat, but rather a multilayered regulatory network jointly constituted by nutrient sensing, key enzymatic nodes, lipid intermediates, and inter-organ communication. At the research level, both mechanistic studies and intervention strategies need to move beyond single-pathway thinking toward the perspective of network reprogramming.
For more related articles, please see below:
[1] Twelve Key Enzymes in Glucose Metabolism
[2] A Detailed Guide to the Construction of Animal Models for Metabolic Diseases