10 research outputs found
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Quantitative Dynamics of Proteome, Acetylome, and Succinylome during Stem-Cell Differentiation into Hepatocyte-like Cells
Stem-cell
differentiation is a complex biological process controlled
by a series of functional protein clusters and signaling transductions,
especially metabolism-related pathways. Although previous studies
have quantified the proteome and phosphoproteome for stem-cell differentiation,
the investigation of acylation-mediated regulation is still absent.
In this study, we quantitatively profiled the proteome, acetylome,
and succinylome in pluripotent human embryonic stem cells (hESCs)
and differentiated hepatocyte-like cells (HLCs). In total, 3843 proteins,
185 acetylation sites in 103 proteins, and 602 succinylation sites
in 391 proteins were quantified. The quantitative proteome showed
that in differentiated HLCs the TGF-β, JAK-STAT, and RAS signaling
pathways were activated, whereas ECM-related processes such as sulfates
and leucine degradation were depressed. Interestingly, it was observed
that the acetylation and succinylation were more intensive in hESCs,
whereas protein processing in endoplasmic reticulum and the carbon
metabolic pathways were especially highly succinylated. Because the
metabolism patterns in pluripotent hESCs and the differentiated HLCs
were different, we proposed that the dynamic acylations, especially
succinylation, might regulate the Warburg-like effect and TCA cycle
during differentiation. Taken together, we systematically profiled
the protein and acylation levels of regulation in pluripotent hESCs
and differentiated HLCs, and the results indicated the important roles
of acylation in pluripotency maintenance and differentiation
Quantitative Dynamics of Proteome, Acetylome, and Succinylome during Stem-Cell Differentiation into Hepatocyte-like Cells
Stem-cell
differentiation is a complex biological process controlled
by a series of functional protein clusters and signaling transductions,
especially metabolism-related pathways. Although previous studies
have quantified the proteome and phosphoproteome for stem-cell differentiation,
the investigation of acylation-mediated regulation is still absent.
In this study, we quantitatively profiled the proteome, acetylome,
and succinylome in pluripotent human embryonic stem cells (hESCs)
and differentiated hepatocyte-like cells (HLCs). In total, 3843 proteins,
185 acetylation sites in 103 proteins, and 602 succinylation sites
in 391 proteins were quantified. The quantitative proteome showed
that in differentiated HLCs the TGF-β, JAK-STAT, and RAS signaling
pathways were activated, whereas ECM-related processes such as sulfates
and leucine degradation were depressed. Interestingly, it was observed
that the acetylation and succinylation were more intensive in hESCs,
whereas protein processing in endoplasmic reticulum and the carbon
metabolic pathways were especially highly succinylated. Because the
metabolism patterns in pluripotent hESCs and the differentiated HLCs
were different, we proposed that the dynamic acylations, especially
succinylation, might regulate the Warburg-like effect and TCA cycle
during differentiation. Taken together, we systematically profiled
the protein and acylation levels of regulation in pluripotent hESCs
and differentiated HLCs, and the results indicated the important roles
of acylation in pluripotency maintenance and differentiation
Quantitative Dynamics of Proteome, Acetylome, and Succinylome during Stem-Cell Differentiation into Hepatocyte-like Cells
Stem-cell
differentiation is a complex biological process controlled
by a series of functional protein clusters and signaling transductions,
especially metabolism-related pathways. Although previous studies
have quantified the proteome and phosphoproteome for stem-cell differentiation,
the investigation of acylation-mediated regulation is still absent.
In this study, we quantitatively profiled the proteome, acetylome,
and succinylome in pluripotent human embryonic stem cells (hESCs)
and differentiated hepatocyte-like cells (HLCs). In total, 3843 proteins,
185 acetylation sites in 103 proteins, and 602 succinylation sites
in 391 proteins were quantified. The quantitative proteome showed
that in differentiated HLCs the TGF-β, JAK-STAT, and RAS signaling
pathways were activated, whereas ECM-related processes such as sulfates
and leucine degradation were depressed. Interestingly, it was observed
that the acetylation and succinylation were more intensive in hESCs,
whereas protein processing in endoplasmic reticulum and the carbon
metabolic pathways were especially highly succinylated. Because the
metabolism patterns in pluripotent hESCs and the differentiated HLCs
were different, we proposed that the dynamic acylations, especially
succinylation, might regulate the Warburg-like effect and TCA cycle
during differentiation. Taken together, we systematically profiled
the protein and acylation levels of regulation in pluripotent hESCs
and differentiated HLCs, and the results indicated the important roles
of acylation in pluripotency maintenance and differentiation
Quantitative Dynamics of Proteome, Acetylome, and Succinylome during Stem-Cell Differentiation into Hepatocyte-like Cells
Stem-cell
differentiation is a complex biological process controlled
by a series of functional protein clusters and signaling transductions,
especially metabolism-related pathways. Although previous studies
have quantified the proteome and phosphoproteome for stem-cell differentiation,
the investigation of acylation-mediated regulation is still absent.
In this study, we quantitatively profiled the proteome, acetylome,
and succinylome in pluripotent human embryonic stem cells (hESCs)
and differentiated hepatocyte-like cells (HLCs). In total, 3843 proteins,
185 acetylation sites in 103 proteins, and 602 succinylation sites
in 391 proteins were quantified. The quantitative proteome showed
that in differentiated HLCs the TGF-β, JAK-STAT, and RAS signaling
pathways were activated, whereas ECM-related processes such as sulfates
and leucine degradation were depressed. Interestingly, it was observed
that the acetylation and succinylation were more intensive in hESCs,
whereas protein processing in endoplasmic reticulum and the carbon
metabolic pathways were especially highly succinylated. Because the
metabolism patterns in pluripotent hESCs and the differentiated HLCs
were different, we proposed that the dynamic acylations, especially
succinylation, might regulate the Warburg-like effect and TCA cycle
during differentiation. Taken together, we systematically profiled
the protein and acylation levels of regulation in pluripotent hESCs
and differentiated HLCs, and the results indicated the important roles
of acylation in pluripotency maintenance and differentiation
Quantitative Dynamics of Proteome, Acetylome, and Succinylome during Stem-Cell Differentiation into Hepatocyte-like Cells
Stem-cell
differentiation is a complex biological process controlled
by a series of functional protein clusters and signaling transductions,
especially metabolism-related pathways. Although previous studies
have quantified the proteome and phosphoproteome for stem-cell differentiation,
the investigation of acylation-mediated regulation is still absent.
In this study, we quantitatively profiled the proteome, acetylome,
and succinylome in pluripotent human embryonic stem cells (hESCs)
and differentiated hepatocyte-like cells (HLCs). In total, 3843 proteins,
185 acetylation sites in 103 proteins, and 602 succinylation sites
in 391 proteins were quantified. The quantitative proteome showed
that in differentiated HLCs the TGF-β, JAK-STAT, and RAS signaling
pathways were activated, whereas ECM-related processes such as sulfates
and leucine degradation were depressed. Interestingly, it was observed
that the acetylation and succinylation were more intensive in hESCs,
whereas protein processing in endoplasmic reticulum and the carbon
metabolic pathways were especially highly succinylated. Because the
metabolism patterns in pluripotent hESCs and the differentiated HLCs
were different, we proposed that the dynamic acylations, especially
succinylation, might regulate the Warburg-like effect and TCA cycle
during differentiation. Taken together, we systematically profiled
the protein and acylation levels of regulation in pluripotent hESCs
and differentiated HLCs, and the results indicated the important roles
of acylation in pluripotency maintenance and differentiation
Quantitative Dynamics of Proteome, Acetylome, and Succinylome during Stem-Cell Differentiation into Hepatocyte-like Cells
Stem-cell
differentiation is a complex biological process controlled
by a series of functional protein clusters and signaling transductions,
especially metabolism-related pathways. Although previous studies
have quantified the proteome and phosphoproteome for stem-cell differentiation,
the investigation of acylation-mediated regulation is still absent.
In this study, we quantitatively profiled the proteome, acetylome,
and succinylome in pluripotent human embryonic stem cells (hESCs)
and differentiated hepatocyte-like cells (HLCs). In total, 3843 proteins,
185 acetylation sites in 103 proteins, and 602 succinylation sites
in 391 proteins were quantified. The quantitative proteome showed
that in differentiated HLCs the TGF-β, JAK-STAT, and RAS signaling
pathways were activated, whereas ECM-related processes such as sulfates
and leucine degradation were depressed. Interestingly, it was observed
that the acetylation and succinylation were more intensive in hESCs,
whereas protein processing in endoplasmic reticulum and the carbon
metabolic pathways were especially highly succinylated. Because the
metabolism patterns in pluripotent hESCs and the differentiated HLCs
were different, we proposed that the dynamic acylations, especially
succinylation, might regulate the Warburg-like effect and TCA cycle
during differentiation. Taken together, we systematically profiled
the protein and acylation levels of regulation in pluripotent hESCs
and differentiated HLCs, and the results indicated the important roles
of acylation in pluripotency maintenance and differentiation
Quantitative Dynamics of Proteome, Acetylome, and Succinylome during Stem-Cell Differentiation into Hepatocyte-like Cells
Stem-cell
differentiation is a complex biological process controlled
by a series of functional protein clusters and signaling transductions,
especially metabolism-related pathways. Although previous studies
have quantified the proteome and phosphoproteome for stem-cell differentiation,
the investigation of acylation-mediated regulation is still absent.
In this study, we quantitatively profiled the proteome, acetylome,
and succinylome in pluripotent human embryonic stem cells (hESCs)
and differentiated hepatocyte-like cells (HLCs). In total, 3843 proteins,
185 acetylation sites in 103 proteins, and 602 succinylation sites
in 391 proteins were quantified. The quantitative proteome showed
that in differentiated HLCs the TGF-β, JAK-STAT, and RAS signaling
pathways were activated, whereas ECM-related processes such as sulfates
and leucine degradation were depressed. Interestingly, it was observed
that the acetylation and succinylation were more intensive in hESCs,
whereas protein processing in endoplasmic reticulum and the carbon
metabolic pathways were especially highly succinylated. Because the
metabolism patterns in pluripotent hESCs and the differentiated HLCs
were different, we proposed that the dynamic acylations, especially
succinylation, might regulate the Warburg-like effect and TCA cycle
during differentiation. Taken together, we systematically profiled
the protein and acylation levels of regulation in pluripotent hESCs
and differentiated HLCs, and the results indicated the important roles
of acylation in pluripotency maintenance and differentiation
Quantitative Dynamics of Proteome, Acetylome, and Succinylome during Stem-Cell Differentiation into Hepatocyte-like Cells
Stem-cell
differentiation is a complex biological process controlled
by a series of functional protein clusters and signaling transductions,
especially metabolism-related pathways. Although previous studies
have quantified the proteome and phosphoproteome for stem-cell differentiation,
the investigation of acylation-mediated regulation is still absent.
In this study, we quantitatively profiled the proteome, acetylome,
and succinylome in pluripotent human embryonic stem cells (hESCs)
and differentiated hepatocyte-like cells (HLCs). In total, 3843 proteins,
185 acetylation sites in 103 proteins, and 602 succinylation sites
in 391 proteins were quantified. The quantitative proteome showed
that in differentiated HLCs the TGF-β, JAK-STAT, and RAS signaling
pathways were activated, whereas ECM-related processes such as sulfates
and leucine degradation were depressed. Interestingly, it was observed
that the acetylation and succinylation were more intensive in hESCs,
whereas protein processing in endoplasmic reticulum and the carbon
metabolic pathways were especially highly succinylated. Because the
metabolism patterns in pluripotent hESCs and the differentiated HLCs
were different, we proposed that the dynamic acylations, especially
succinylation, might regulate the Warburg-like effect and TCA cycle
during differentiation. Taken together, we systematically profiled
the protein and acylation levels of regulation in pluripotent hESCs
and differentiated HLCs, and the results indicated the important roles
of acylation in pluripotency maintenance and differentiation
High Fat Diet and High Sucrose Intake Divergently Induce Dysregulation of Glucose Homeostasis through Distinct Gut Microbiota-Derived Bile Acid Metabolism in Mice
A high
calorie diet such as excessive fat and sucrose intake is
always accompanied by impaired glucose homeostasis such as T2DM (type
2 diabetes mellitus). However, it remains unclear how fat and sucrose
individually affect host glucose metabolism. In this study, mice were
fed with high fat diet (HFD) or 30% sucrose in drinking water (HSD)
for 24 weeks, and glucose metabolism, gut microbiota composition,
as well as bile acid (BA) profile were investigated. In addition,
the functional changes of HFD or HSD-induced gut microbiota were further
verified by fecal microbiota transplantation (FMT) and ex
vivo culture of gut bacteria with BAs. Our results showed
that both HFD and HSD caused dysregulated lipid metabolism, while
HFD feeding had a more severe effect on impaired glucose homeostasis,
accompanied by reduced hyocholic acid (HCA) levels in all studied
tissues. Meanwhile, HFD had a more dramatic influence on composition
and function of gut microbiota based on α diversity indices,
β diversity analysis, as well as the abundance of secondary
BA producers than HSD. In addition, the phenotypes of impaired glucose
homeostasis and less formation of HCA caused by HFD can be transferred
to recipient mice by FMT. Ex vivo culture with gut
bacteria and BAs revealed HFD-altered gut bacteria produced less HCA
than HSD, which might closely associate with reduced relative abundance
of C7 epimerase-coding bacteria g_norank/unclassified_f_Eggerthellaceae and bile salt hydrolase-producing bacteria Lactobacillus and Bifidobacterium in HFD group. Our findings
revealed that the divergent effects of different high-calorie diets
on glucose metabolism may be due to the gut microbiota-mediated generation
and metabolism of BAs, highlighting the importance of dietary management
in T2DM