OBJECTIVES: Collagen influences the biomechanical properties of vocal folds. Altered collagen morphology has been implicated in dysphonia associated with aging and scarring. Documenting the morphological properties of native collagen in healthy vocal folds is essential to understand the structural and functional alterations to collagen with aging and disease. Our primary objective was to quantify the morphological properties of collagen in the vocal fold lamina propria. Our secondary exploratory objective was to investigate the effects of pepsin exposure on the morphological properties of collagen in the lamina propria. STUDY DESIGN: Experimental, in vitro study with porcine model. METHODS: Lamina propria was dissected from 26 vocal folds and imaged with atomic force microscopy (AFM). Morphological data on d-periodicity, diameter, and roughness of collagen fibers were obtained. To investigate the effects of pepsin exposure on collagen morphology, vocal fold surface was exposed to pepsin or sham challenge before lamina propria dissection and AFM imaging. RESULTS: The d-periodicity, diameter, and roughness values for native vocal fold collagen are consistent with literature reports of collagen fibers in other body tissues. Pepsin exposure on vocal fold surface did not appear to change the morphological properties of collagen fibers in the lamina propria. CONCLUSIONS: Quantitative data on collagen morphology were obtained at nanoscale resolution. Documenting collagen morphology in healthy vocal folds is critical for understanding the physiological changes to collagen with aging and scarring and for designing biomaterials that match the native topography of lamina propria.
OBJECTIVES: Collagen influences the biomechanical properties of vocal folds. Altered collagen morphology has been implicated in dysphonia associated with aging and scarring. Documenting the morphological properties of native collagen in healthy vocal folds is essential to understand the structural and functional alterations to collagen with aging and disease. Our primary objective was to quantify the morphological properties of collagen in the vocal fold lamina propria. Our secondary exploratory objective was to investigate the effects of pepsin exposure on the morphological properties of collagen in the lamina propria. STUDY DESIGN: Experimental, in vitro study with porcine model. METHODS: Lamina propria was dissected from 26 vocal folds and imaged with atomic force microscopy (AFM). Morphological data on d-periodicity, diameter, and roughness of collagen fibers were obtained. To investigate the effects of pepsin exposure on collagen morphology, vocal fold surface was exposed to pepsin or sham challenge before lamina propria dissection and AFM imaging. RESULTS: The d-periodicity, diameter, and roughness values for native vocal fold collagen are consistent with literature reports of collagen fibers in other body tissues. Pepsin exposure on vocal fold surface did not appear to change the morphological properties of collagen fibers in the lamina propria. CONCLUSIONS: Quantitative data on collagen morphology were obtained at nanoscale resolution. Documenting collagen morphology in healthy vocal folds is critical for understanding the physiological changes to collagen with aging and scarring and for designing biomaterials that match the native topography of lamina propria.
Authors: Mariah S Hahn; Benjamin A Teply; Molly M Stevens; Steven M Zeitels; Robert Langer Journal: Biomaterials Date: 2005-09-09 Impact factor: 12.479
Authors: Hossein K Heris; Amir K Miri; Nageswara R Ghattamaneni; Nicole Y K Li; Susan L Thibeault; Paul W Wiseman; Luc Mongeau Journal: J Biomech Date: 2015-01-21 Impact factor: 2.712