富含histidine的结合蛋白:是心脏激发 - 收缩合的分子整合剂
1Department of Physiology, School of Medicine, College of Medicine and Health, University College Cork, Cork, T12 XF62, Ireland.
The Journal of experimental biology
|October 23, 2024
概括
富含西丁的结合蛋白 (HRC) 和阿斯波林调节心肌细胞的水平. 人类碳化合物显示了快速的进化,这表明它适应了陆地生命,并可能在pH感应和氧化还原反应中发挥作用.
科学领域:
- 心脏病学 心脏病学
- 分子生物学分子生物学
- 进化生物学 进化生物学
背景情况:
- 哺乳动物心肌细胞收缩依赖于 (Ca2+) 流入和从质网膜 (SR) 释放.
- 富含histidine的结合蛋白 (HRC) 和aspolin是SR Ca2+水平和功能的关键Ca2+结合调节剂.
- HRC调节SR Ca2+-ATPase 2和氨酸受体通道,影响激发 - 收缩合.
研究的目的:
- 分析HRC和aspolin的演变,以了解它们在心脏功能中的调节作用.
- 研究这些Ca2+结合蛋白的进化起源和多样化.
主要方法:
- 在不同物种中对HRC和aspolin序列进行比较基因组和进化分析.
- 生物信息学分析以确定保护和快速发展的地区.
- 检查蛋白质域和功能推理的动机.
主要成果:
- 在各种物种中发现了HRC同类物种,包括带状动物,类动物,软体动物,珊瑚和海.
- 特里亚丁似乎是一种特定于带状动物的蛋白质.
- 在哺乳动物中,HRC表现出加速的进化,特别是在可能参与pH感应和氧化还原反应的区域,而其C端区域则被保留.
结论:
- HRC和aspolin在调节心脏Ca2+处理方面发挥着至关重要的作用,而HRC正在经历显著的进化适应.
- 人类热带生物的快速进化可能反映了对陆地,内热生物的适应,可能涉及pH传感.
- 保存的富含氨酸的图案表明HRC和阿斯波林在氧化还原反应和金属结合中的作用,而阿斯波林中的聚酸区域与脱甲基酶活性有关.
更多相关视频
相关概念视频
Excitation-Contraction Coupling in Skeletal Muscles
7.9K
Excitation-contraction coupling is a series of events that occur between generating an action potential and initiating a muscle contraction. It occurs at the triad, a structure found in skeletal muscle fibers that comprise a T-tubule and terminal cisternae of the sarcoplasmic reticulum on each side. These triads are visible in longitudinally sectioned muscle fibers. They are typically located at the A-I junction — the junction between the A and I bands of the sarcomere.
When an action...
When an action...
7.9K
Calmodulin-dependent Signaling
5.1K
Calmodulin (CaM) is a calcium-binding protein in eukaryotes that controls various calcium-regulated cellular processes. It has four calcium-binding sites that bind calcium to form the calcium-calmodulin ( Ca2+-CaM) complex. GPCR stimulation increases the calcium levels in the cells that bind to CaM and induces a conformational change.
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
5.1K
G-Protein Gated Ion Channels
4.5K
GPCRs are primarily responsible for our sense of smell, taste, and vision. The binding of a sensory stimulus activates GPCR to stimulate effector proteins, many of which are ion channels in the sensory organs. GPCRs modulate the opening and closing of the target ion channels either directly by binding them, or by releasing second messengers that activate these channels. As ions move across the membrane, the membrane potential is altered, which induces an appropriate response.
Sensory...
Sensory...
4.5K
Feedback Regulation of Calcium Concentration
3.4K
Calcium is an essential signaling molecule required for various cellular functions. Calcium pumps and ion channels on cell and organellar membranes, such as those on the endoplasmic reticulum (ER), regulate calcium concentrations inside the cell. They remain closed, keeping the cytosolic calcium levels low at a resting state.
Various transmembrane receptors, such as G protein-coupled receptors (GPCRs), elicit a response to extracellular signals by increasing cytosolic calcium. Activated GPCRs...
Various transmembrane receptors, such as G protein-coupled receptors (GPCRs), elicit a response to extracellular signals by increasing cytosolic calcium. Activated GPCRs...
3.4K
Smooth Muscle Contraction
2.5K
Smooth muscle contraction is a complex process vital for various bodily functions, from maintaining blood vessel tension to facilitating the movement of food through the digestive tract. Unlike striated muscles, smooth muscle contraction begins more slowly and lasts longer.
The onset of contraction is triggered by an increase in calcium ions within the sarcoplasm, similar to the process in striated muscle. However, smooth muscles have a relatively smaller reservoir of the sarcoplasmic...
The onset of contraction is triggered by an increase in calcium ions within the sarcoplasm, similar to the process in striated muscle. However, smooth muscles have a relatively smaller reservoir of the sarcoplasmic...
2.5K
Structure of Cadherins
3.3K
The cadherins were one of the first cell adhesion molecules discovered; the term “cadherins” is based on their calcium-dependent adhering properties. The first cadherins discovered on the epithelial, neuronal, and placental cells were named E-cadherin, P-cadherin, and N-cadherin, respectively. These classical cadherins share sequence and structural similarities. Other cadherins, including those involved in cell signaling, are grouped into non-classical cadherins. This...
3.3K


