Angiogenesis Study Group, Oncology Area, Center for Biomedical Research of La Rioja (CIBIR), 26006 Logroño, Spain.
Curr Protein Pept Sci. 2013 Aug;14(5):429-43. doi: 10.2174/13892037113149990059.
Classical transmembrane receptors have been described for both adrenomedullin (AM) and proadrenomedullin N-terminal 20 peptide (PAMP). Through interactions with these membrane receptors, AM and PAMP exert a variety of endocrine, paracrine, and autocrine functions. In addition to these better known activities, recent publications have shown that both peptides can bind directly to the cytoskeleton resulting in important cellular physiological responses. In vitro and in vivo experiments show that the peptides bind to major components of the cytoskeleton: tubulin and kinesin for PAMP and a number of microtubule-associated proteins (MAPs) in the case of AM. Physiological experiments show that PAMP contributes to microtubule fluidity and increases kinesin speed. Lack of AM and PAMP results in hyperpolymerization of the cytoskeleton and a reduced motility of intracellular organelles. These data suggest that the cytoskeleton may have a novel function as an intracellular receptor, acting as the binding site and the signal transducer for specific peptide hormones such as PAMP.
经典跨膜受体已被描述为肾上腺髓质素 (AM) 和前肾上腺髓质素 N 端 20 肽 (PAMP) 的受体。通过与这些膜受体的相互作用，AM 和 PAMP 发挥各种内分泌、旁分泌和自分泌功能。除了这些更为人所知的作用外，最近的出版物表明，这两种肽都可以直接与细胞骨架结合，从而导致重要的细胞生理反应。体外和体内实验表明，这些肽与细胞骨架的主要成分结合：PAMP 与微管蛋白和驱动蛋白结合，而 AM 则与许多微管相关蛋白 (MAP) 结合。生理实验表明，PAMP 有助于微管流动性并增加驱动蛋白的速度。缺乏 AM 和 PAMP 会导致细胞骨架过度聚合，细胞内细胞器的运动能力降低。这些数据表明，细胞骨架可能具有作为细胞内受体的新功能，作为特定肽激素（如 PAMP）的结合位点和信号转导器。
