65 Abnormal collagen structure resulting from lack of contribution of collagen type XIV in lungs of patients with idiopathic pulmonary fibrosis unknown. As FACITs regulate the structural organization of fibrillar collagens, it can be argued that lower proportions of COL14 in IPF lungs contribute to the reported imbalance between organized and disorganized fibrillar collagen in IPF [5]. More research correlating fibrillar collagen organization with FACITs such as COL14 will increase understanding of the involvement of COL14 in the development and/or progression of fibrotic responses. A recent study using mice deficient in COL14A1 found increased stiffness and abnormal collagen fibril organization in the corneas of COL14A1-knockout mice compared to wildtypes [12]. These observations parallel well-documented increases in the stiffness of lungs from patients with IPF [11]. Together with our observations reported here, it is tempting to speculate that COL14 protein levels in IPF lungs do not mirror the increase in other ECM proteins in lung tissue during fibrosis, thereby leading to more disorganized collagen fibers with higher stiffness in lungs of patients with IPF. ACKNOWLEDGEMENTS The stainings of COL14A1 on lung tissue analyzed in this manuscript were conducted as part of the HOLLAND (HistopathOLogy of Lung Aging aNd COPD) project. The HOLLAND project was initiated and supervised by Corry-Anke Brandsma, Wim Timens, and Janette Burgess, technical support was provided by Marjan ReindersLuinge, Anja Bakker and Theo Borghuis, and image analyses pipelines were developed by Theo Borghuis, Maunick Lefin Koloko Ngassie and Niek Bekker. MN, BNM, IHH and JKB receive unrestricted research funds from Boehringer Ingelheim. JKB also acknowledges support from the NWO (Aspasia 015.013.010). This work was supported by the Chan Zuckerberg Initiative, LLC Seed Network grant CZF2019-002438 “Lung Cell Atlas 1.0” 3
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