Human FABP1 (liver)
- Known as:
- Human FABP1 (liver)
- Catalog number:
- E-80FPL
- Product Quantity:
- 1 x 96 well plate
- Category:
- -
- Supplier:
- ICL
- Gene target:
- Human FABP1 (liver)
Related genes to: Human FABP1 (liver)
- Gene:
- FABP1 NIH gene
- Name:
- fatty acid binding protein 1
- Previous symbol:
- -
- Synonyms:
- L-FABP
- Chromosome:
- 2p11.2
- Locus Type:
- gene with protein product
- Date approved:
- 2001-06-22
- Date modifiied:
- 2016-10-05
- Gene:
- FABP3 NIH gene
- Name:
- fatty acid binding protein 3
- Previous symbol:
- MDGI, FABP11
- Synonyms:
- H-FABP, O-FABP
- Chromosome:
- 1p35.2
- Locus Type:
- gene with protein product
- Date approved:
- 1991-08-06
- Date modifiied:
- 2016-10-05
Related products to: Human FABP1 (liver)
Related articles to: Human FABP1 (liver)
- Premature infants are at high risk for brain injuries such as intraventricular hemorrhage and periventricular white matter injury. This study applies omics technology to analyze urinary protein expression, aiming to clarify preterm brain injury mechanisms and identify therapeutic targets. Urine samples were collected from 29 very preterm infants (VPI) without brain injury and 11 with moderate/severe injury at eight time points: Days 1, 2, 3, 4, 6, 8, 28, and term-equivalent age (TEA). Brain damage was assessed using the Kidokoro scale and MRI at TEA. SWATH-MS and bioinformatics were used to identify differentially expressed urinary proteins and affected pathways. Fifty-six proteins showed significant expression differences. Notably, extracellular proteoglycans (NCAN, ACAN, BCAN), associated with neuroprotection, were markedly reduced in infants with brain injury. Conversely, fatty acid-binding proteins (FABP1, FABP3, FABP4, FABP7) decreased over time in uninjured infants but increased in those with brain injury, suggesting a role in exacerbating damage. In summary, the urinary proteome of VPI with moderate/severe brain injury differs significantly from those without injury. Reduced neuroprotective proteoglycans and elevated FABPs highlight potential molecular markers and targets for intervention in preterm brain injury. - Source: PubMed
Publication date: 2025/09/09
Zasada MagdalenaSuski MaciejOlszewska MartaKowalik AleksandraŁapińska NataliaPogoda WeronikaKwinta Przemko - Fatty acid-binding proteins (FABPs) are intracellular lipid chaperones with molecular weights of approximately 14-15 kDa. By binding and transporting fatty acids and lipid-related molecules, FABPs precisely regulate metabolic pathways, signal transduction, and gene expression, playing a central role in cancer initiation and progression. The 11 identified subtypes (FABP1-FABP12; FABP11 is identical to FABP3) exhibit tissue-specific expression and influence tumor progression through metabolic reprogramming, immune microenvironment modulation, and therapy resistance. Metabolically, FABPs enhance fatty acid uptake, β-oxidation, and synthesis, meeting the high proliferative demands of tumors. In immune regulation, FABP4 + macrophages secrete IL-6 to suppress T cell activity, while FABP6 downregulates MHC-I molecule expression to reduce CD8 + T cell infiltration, fostering an immunosuppressive microenvironment. Regarding therapy resistance, FABP4 enhances mitochondrial β-oxidation to reduce apoptosis in ovarian cancer, and FABP5 promotes chemoresistance in HCC via the HIF-1α pathway. Functional heterogeneity exists among subtypes: FABP7 drives glioblastoma stem cell migration via RXRα signaling, while FABP5 exhibits context-dependent roles, promoting HCC progression but suppressing colorectal cancer (CRC) through mTOR-mediated autophagy. Clinically, FABPs serve as diagnostic biomarkers and therapeutic targets. However, challenges such as insufficient target specificity, cross-cancer heterogeneity, and normal tissue toxicity remain. Future studies should integrate multi-omics and single-cell technologies to elucidate cell-specific mechanisms and develop precise combination therapies for clinical translation. - Source: PubMed
Publication date: 2025/07/15
Wu LongOu Guang-LingZhang WeiMa Hua-XingLi Xiao-YunZhen Yun-HuanWu HuanCao KunLi Hai-Yang - Adipose is a complex tissue comprised of adipocytes, immune cells, endothelial and progenitor stem cells. In humans, there are at least nine defined adipose depots, each containing variable numbers of genetically identified adipocyte clusters suggesting remarkable heterogeneity and potential functionality in each depot with respect to lipid metabolism. Although subcutaneous and visceral depots are commonly analyzed for biochemical and molecular functions, the mesenteric depot has been overlooked yet strongly implicated in lipid mediated immune surveillance. Since fatty acid binding proteins (FABPs) are primary cellular conduits to lipid trafficking, we evaluated the expression patterns for four major fatty acid binding proteins (FABP1, FABP3, FABP4 and FABP5) using a combination of gene expression, immunoblotting, and immunofluorescence in mesenteric fat from both young and old, male and female C57Bl/6J mice. All four FABPs were expressed at the mRNA and protein level in murine mesenteric adipose tissue. While there was no statistical change in expression of mesenteric FABP isoforms with sex or age, the expression of mesenteric FABP1 was increased, and FABP4 decreased, in both males and females as compared to perigonadal and inguinal depots. Surprisingly, immunofluorescence staining revealed that compared to subcutaneous or perigonadal depots, mesenteric fat expresses FABP3, but little FABP5, in adipocytes. These results highlight the diversity in adipose tissue and the importance of evaluating the mesenteric depot in the context of lipid transport and metabolism. - Source: PubMed
Publication date: 2025/01/20
Fish Shayla RHalley Catherine LDileepan MythiliHertzel Ann VDickey Deborah MBernlohr David A - Although a giant Egyptian domestic non-migratory duck breed is phenotypically identical to the migratory Mallard, yet it is three times larger. The current study sought to determine the genetic and metabolic differences between this duck and Mallard, which arrives in Egypt in September for wintering and departs in March. Mitochondrial DNA control region (D-loop) was extracted, amplified, sequenced, and analyzed in both ducks. Both ducks were given a high-fat diet (HFD) for 6 weeks to assess their metabolic response to this diet. Polymorphism results indicated that the D-loop is highly variable and both populations expansion is balanced. The hierarchical analysis of molecular variants (AMOVA) and interpopulation difference parameters revealed significant genetic differentiation and minimal gene flow between migrant and resident populations. Phylogeny and Network analyses revealed that domestic ducks are a distinct group that separated from mallards. Physiologically, domestic duck blood and adipose tissue had a higher level of triglycerides and adipocyte volume than that of the depleting arriving migratory Mallard ducks, while leaving Mallard parameters were the highest, suggesting a high level of preparatory fat deposition and utilization before starting the trip. In response to HFD, the expression of FA uptake genes cd36, fabp1 was upregulated similarly in livers of domestic and migratory Mallard ducks, while the expression of lipid accumulation genes dgat2 and plin2 was higher in domestic than in migratory Mallards. However, the highest body mass and adipocytes volume gain was observed in the arriving migratory Mallards. In pectoral muscle, the expression of cd36 and fabp3 was higher in domestic than in leaving ducks, while in arriving Mallards, both genes were not upregulated in response to HFD. Dgat2 was upregulated only in domestic muscle, while lipid oxidation genes cpt1, lpl, and the controlling ppara were more upregulated in leaving Mallard. In conclusion, both ducks can be genetically and metabolically differentiated. Migratory mallards are more flexible and efficient in lipid metabolism than domestic ducks. - Source: PubMed
Publication date: 2025/01/19
Sheta BasmaHassan AsmaaSallam Alaa El-DinHabbak LotfyHyder Ayman - Menin is a scaffold protein encoded by the Men1 gene, which interacts with various transcriptional proteins to activate or repress cellular processes and is a key mediator in multiple organs. Both liver-specific and hepatocyte-specific Menin deficiency promotes high-fat diet-induced liver steatosis in mice, as well as insulin resistance and type 2 diabetic phenotype. The potential link between Menin and hepatic metabolism homeostasis may provide new insights into the mechanism of fatty liver disease. - Source: PubMed
Publication date: 2023/09/22
Liu TingjunLi RanranSun LiliXu ZhongjinWang ShengxuanZhou JingxuanWu XuanningShi Kerong