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首页> 美国卫生研究院文献>The Journal of Biological Chemistry >Distinct domains in the matricellular protein Lonely heart are crucial for cardiac extracellular matrix formation and heart function in Drosophila
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Distinct domains in the matricellular protein Lonely heart are crucial for cardiac extracellular matrix formation and heart function in Drosophila

机译：母体细胞蛋白孤独域中的不同域对于果蝇中心脏细胞外基质的形成和心脏功能至关重要

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The biomechanical properties of extracellular matrices (ECMs) are critical to many biological processes, including cell–cell communication and cell migration and function. The correct balance between stiffness and elasticity is essential to the function of numerous tissues, including blood vessels and the lymphatic system, and depends on ECM constituents (the “matrisome”) and on their level of interconnection. However, despite its physiological relevance, the matrisome composition and organization remain poorly understood. Previously, we reported that the ADAMTS-like protein Lonely heart (Loh) is critical for recruiting the type IV collagen–like protein Pericardin to the cardiac ECM. Here, we utilized Drosophila as a simple and genetically amenable invertebrate model for studying Loh-mediated recruitment of tissue-specific ECM components such as Pericardin to the ECM. We focused on the functional relevance of distinct Loh domains to protein localization and Pericardin recruitment. Analysis of Loh deletion constructs revealed that one thrombospondin type 1 repeat (TSR1-1), which has an embedded WXXW motif, is critical for anchoring Loh to the ECM. Two other thrombospondin repeats, TSR1-2 and TSR1-4, the latter containing a CXXTCXXG motif, appeared to be dispensable for tethering Loh to the ECM but were crucial for proper interaction with and recruitment of Pericardin. Moreover, our results also suggested that Pericardin in the cardiac ECM primarily ensures the structural integrity of the heart, rather than increasing tissue flexibility. In conclusion, our work provides new insights into the roles of thrombospondin type 1 repeats and advances our understanding of cardiac ECM assembly and function.
机译：细胞外基质（ECM）的生物力学特性对许多生物过程至关重要，包括细胞间通讯以及细胞迁移和功能。刚度和弹性之间的正确平衡对于包括血管和淋巴系统在内的许多组织的功能至关重要，并且取决于ECM成分（“基质”）及其互连程度。然而，尽管其生理学相关性，但对基质的组成和组织仍知之甚少。以前，我们报道过ADAMTS样蛋白孤独的心脏（Loh）对于将IV型胶原样蛋白Pericardin募集到心脏ECM至关重要。在这里，我们将果蝇作为一种简单且在遗传学上可适应的无脊椎动物模型，用于研究Loh介导的组织特异性ECM成分（如Pericardin）向ECM的募集。我们专注于不同的Loh结构域与蛋白质定位和Pericardin募集的功能相关性。 Loh缺失构建体的分析表明，一个具有嵌入的WXXW主题的血小板反应蛋白1型重复序列（TSR1-1）对于将Loh锚定到ECM至关重要。 TSR1-2和TSR1-4的另外两个血小板反应蛋白重复序列​​（后者含有CXXTCXXG基序）对于将Loh束缚在ECM上似乎是必不可少的，但对于与Pericardin的正常相互作用和募集至关重要。此外，我们的研究结果还表明，心脏ECM中的心包素主要确保心脏的结构完整性，而不是增加组织的柔韧性。总而言之，我们的工作为重复1型血小板反应蛋白的作用提供了新的见识，并增进了我们对心脏ECM组装和功能的理解。

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