Department of Otolaryngology, National Taiwan University Hospital, Taipei, Taiwan.
Department of Clinical Laboratory Sciences and Medical Biotechnology, College of Medicine, National Taiwan University, Taipei, Taiwan; Liver Disease Prevention and Treatment Research Foundation, Taiwan.
Hear Res. 2024 Nov;453:109134. doi: 10.1016/j.heares.2024.109134. Epub 2024 Oct 18.
Mutations in various type II transmembrane serine protease (TMPRSS) family members are associated with non-syndromic hearing loss, with some mechanisms still unclear. For instance, the mechanism underlying profound hearing loss and tectorial membrane (TM) malformations in hepsin/TMPRSS1 knockout (KO) mice remains elusive. In this study, we confirmed significantly elevated hearing thresholds and abnormal TM morphology in hepsin KO mice, characterized by enlarged TM with gaps and detachment from the spiral limbus. Transgenic mouse lines were created to express either wild-type or a serine protease-dead mutant of human hepsin in the KO background. The Tg68;KO line, expressing moderate levels of wild-type human hepsin in the cochlea, showed partial restoration of hearing function. Conversely, the Tg5;KO or TgRS;KO lines, with undetectable hepsin or protease-dead hepsin, did not show such improvement. Histological analyses revealed that Tg68;KO mice, but not Tg5;KO or TgRS;KO mice, had a more compact TM structure, partially attached to the spiral limbus. These results indicate that hepsin expression levels correlate with improvements in hearing and TM morphology, and its protease activity is critical for these effects. Hepsin's role was further examined by studying its relationship with α-tectorin (TECTA) and β-tectorin (TECTB), non-collagenous proteins crucial for TM formation. Hepsin was co-expressed with TECTA and TECTB in the developing cochlear epithelium. Immunostaining showed decreased levels of TECTA and TECTB in hepsin KO TM, partially restored in Tg68;KO mice. These findings suggest that hepsin is essential for proper TM morphogenesis and auditory function, potentially by proteolytic processing/maturation of TECTA and TECTB and their incorporation into the TM.
各种 II 型跨膜丝氨酸蛋白酶(TMPRSS)家族成员的突变与非综合征性听力损失有关,其部分机制仍不清楚。例如,hepsin/TMPRSS1 敲除(KO)小鼠的深度听力损失和盖膜(TM)畸形的机制仍不清楚。在这项研究中,我们证实了 hepsin KO 小鼠的听力阈值显著升高和 TM 形态异常,表现为 TM 增大、出现间隙和从螺旋边缘分离。我们创建了转基因小鼠品系,在 KO 背景下表达野生型或人 hepsin 的丝氨酸蛋白酶失活突变体。在耳蜗中表达中等水平野生型人 hepsin 的 Tg68;KO 线显示听力功能部分恢复。相反,hepsin 或蛋白酶失活的 hepsin 无法检测到的 Tg5;KO 或 TgRS;KO 线没有显示出这种改善。组织学分析表明,Tg68;KO 小鼠,而不是 Tg5;KO 或 TgRS;KO 小鼠,TM 结构更紧凑,部分附着在螺旋边缘。这些结果表明 hepsin 的表达水平与听力和 TM 形态的改善相关,其蛋白酶活性对这些影响至关重要。通过研究 hepsin 与α-tectorin(TECTA)和β-tectorin(TECTB)的关系进一步研究了其作用,这两种非胶原蛋白对 TM 形成至关重要。Hepsin 在发育中的耳蜗上皮细胞中与 TECTA 和 TECTB 共表达。免疫染色显示 hepsin KO TM 中的 TECTA 和 TECTB 水平降低,在 Tg68;KO 小鼠中部分恢复。这些发现表明 hepsin 对于 TM 的正常形态发生和听觉功能是必不可少的,可能通过 TECTA 和 TECTB 的蛋白水解加工/成熟及其掺入 TM 来实现。