与饮食相比,腹部手术后IGF结合蛋白-2的度更高
Chino Aneke-Nash1, Sarah Borden2, Emily G Werth3
1Digestive and Liver Disease, Department of Medicine, Columbia University Vagelos College of Physicians and Surgeons, New York, NY 10032, USA.
Journal of the Endocrine Society
|February 2, 2026
概括
腹腔外科手术和生活方式的改变改善了代谢标记物,如阿迪波涅克丁/叶丁和IGFBP-2. 手术导致IGFBP-2的增加更大,这表明除了仅仅减肥之外的好处.
科学领域:
- 代谢性疾病研究研究.
- 腹腔外科手术的结果
- 内分泌学 在内分泌学.
背景情况:
- 减肥手术提供了优越的持续减肥和代谢改善,而不是改变生活方式.
- 从独立的代谢变化中区分依赖减肥的体重变化仍然是一个挑战.
研究的目的:
- 量化阿迪波内克/叶丁比率和IGF结合蛋白2 (IGFBP-2) 的变化.
- 评估这些标志物作为代谢性疾病干预后改善的指标.
主要方法:
- 体重指数≥35kg/m2的成年人接受了为期12周的低卡路里饮食 (LCD) 或减肥手术 (袖子胃切除术或Roux-en-Y胃绕道).
- 测量是在基线,早期减肥 (T2) 和1年 (T3) 进行的.
- 由于结果相似,手术组被组合在一起.
主要成果:
- 液晶显示器和手术组都显示出类似的早期体重减轻 (15%) 和阿迪波涅克/莱普比率的增加.
- 在手术后,IGFBP-2显著增加 (203 ng/mL),相比于LCD (153 ng/mL) 在T2.
- 手术后持续减肥进一步增加了阿迪波涅克丁/莱普丁比率,而IGFBP-2水平稳定.
结论:
- 随着体重减轻,IGFBP-2和阿迪波内克/叶丁比率都会有所改善.
- 减肥手术后IGFBP-2的明显增加表明潜在的长期代谢益处独立于减肥的程度.
相关概念视频
The Equilibrium Binding Constant and Binding Strength
15.1K
The equilibrium binding constant (Kb) quantifies the strength of a protein-ligand interaction. Kb can be calculated as follows when the reaction is at equilibrium:
15.1K
Factors Affecting Protein-Drug Binding: Protein-Related Factors
559
Drug binding to proteins is a key aspect of pharmacokinetics and can influence a drug's distribution, absorption, and elimination in the body. Several factors, including the drug's physiochemical properties, protein concentration, disease states, and the number of binding sites on the protein, influence this process.
The physicochemical properties of a drug play a significant role in its ability to bind to proteins. Lipophilic drugs, which dissolve in fats, oils, and lipids, can be...
The physicochemical properties of a drug play a significant role in its ability to bind to proteins. Lipophilic drugs, which dissolve in fats, oils, and lipids, can be...
559
Conserved Binding Sites
5.2K
Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...
5.2K
Drug Distribution: Plasma Protein Binding
8.8K
Drugs predominantly attach to plasma proteins, with only a small percentage remaining unbound. The unbound portion can be calculated as one minus the bound fraction. Acidic drugs form large, inactive complexes by reversibly binding to plasma albumin, which prevents them from diffusing across biological barriers. These drug-protein complexes act as reservoirs for the drugs. As the concentration of unbound drugs decreases, these complexes quickly dissociate to release the free drug, maintaining...
8.8K
Protein-Drug Binding: Determination Methods
651
Determining protein-drug binding can be achieved through indirect and direct methods, each providing valuable insights into the interaction between proteins and drugs.
Indirect methods involve isolating the bound drug from its free form in biological samples such as blood, serum, or plasma. These techniques aim to measure the percentage of drugs bound to proteins. Equilibrium dialysis is a commonly used method where the free drug concentration at equilibrium is measured by separating the bound...
Indirect methods involve isolating the bound drug from its free form in biological samples such as blood, serum, or plasma. These techniques aim to measure the percentage of drugs bound to proteins. Equilibrium dialysis is a commonly used method where the free drug concentration at equilibrium is measured by separating the bound...
651
Single-Strand DNA Binding Proteins
16.7K
For successful DNA replication, the unwinding of double-stranded DNA must be accompanied by stabilization and protection of the separated single strands of the DNA. This crucial task is performed by single-strand DNA-binding (SSB) proteins. They bind to the DNA in a sequence-independent manner, which means that the nitrogenous bases of the DNA need not be present in a specific order for binding of SSB proteins to it. The binding of SSB proteins straightens single-stranded DNA (ssDNA) and makes...
16.7K


