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首页> 外文期刊>Cell and Tissue Research >The matriptase-prostasin proteolytic cascade in epithelial development and pathology.
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The matriptase-prostasin proteolytic cascade in epithelial development and pathology.

机译：脂蛋白-前列腺素蛋白水解级联在上皮发育和病理学中。

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摘要

The type II transmembrane serine protease matriptase has an essential role in the integrity and function of multiple epithelial tissues. In the epidermis, matriptase activates the glycosylphosphatidylinositol (GPI) anchored membrane serine protease prostasin to initiate a proteolytic cascade that is required for the development of the stratum corneum barrier function. Accordingly, mice deficient for matriptase phenocopy mice deficient for epidermal prostasin and present with impaired corneocyte differentiation, imparied lipid matrix formation, loss of profilaggrin processing and loss of tight junction formation and function. Together, these defects lead to a compromised epidermal barrier and result in fatal dehydration during the neonatal period. Proteolytic activity of the matriptase-prostasin cascade is regulated in the epidermis via inhibition by the Kunitz-type serine protease inhibitor hepatocyte growth factor activator inhibitor-1 (HAI-1). Importantly, targeted post-natal ablation of matriptase in mice perturbs the function of multiple adult tissues, indicating an ongoing requirement for matriptase proteolysis in the maintenance of diverse types of epithelia. Impaired matriptase proteolytic activity has been linked to human Autosomal Recessive Icthyosis with Hypotrichosis (ARIH), whereas aberrant matriptase activity has been implicated in Netherton's Syndrome. This review will summarize information pertaining to the role of matriptase in epithelial biology and will discuss recent advancements in our understanding of how matriptase activity is regulated and the down-stream effectors of matriptase proteolysis.
机译：II型跨膜丝氨酸蛋白酶Matriptase在多个上皮组织的完整性和功能中具有重要作用。在表皮中，matriptase激活糖基磷脂酰肌醇（GPI）锚定的膜丝氨酸蛋白酶prosastin，以启动形成角质层屏障功能所需的蛋白水解级联反应。因此，缺乏苹果酸蛋白酶表型的小鼠缺乏表皮前列腺素并且存在受损的角质细胞分化，受损的脂质基质形成，前凝乳素加工的丧失以及紧密连接形成和功能的丧失。这些缺陷共同导致表皮屏障受损，并导致新生儿期致命的脱水。逆转录酶-前列腺素蛋白级联的蛋白水解活性是通过抑制Kunitz型丝氨酸蛋白酶抑制剂肝细胞生长因子激活剂-1（HAI-1）来调节表皮中的。重要的是，在小鼠中进行有针对性的产后消融脱氧核糖核酸酶扰动了多个成年组织的功能，这表明在维持各种类型的上皮细胞中对脱氧核糖核酸酶蛋白水解的持续需求。脂蛋白磷酸酶的蛋白水解活性受损已与人类常染色体隐性鳞状细胞增多症伴hyporichosis（ARIH）相关，而异常的脂蛋白磷酸酶活性已被归类于Netherton综合征。这篇综述将总结有关matriptase在上皮生物学中的作用的信息，并将讨论我们在了解matriptase活性如何被调控以及matriptase蛋白水解的下游效应器方面的最新进展。

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