Collagen Fiber and Versican Distribution Within the Lamina Propria of Fetal Vocal Folds

Buhler, Rogerio Borghi; Sennes, Luiz Ubirajara; Mauad, Thaís; Melo, Erich Christiano Madruga de; Silva, Luiz Fernando F.; Saldiva, Paulo Hilário Nascimento

doi:10.1097/mlg.0b013e318159aa0d

Cited by 15 publications

(26 citation statements)

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“…Histological observations suggest adult lamina propria have a superficial, intermediate, and deep layer, each defined by their relative collagen and elastin content. Analogous studies of fetal lamina propria demonstrates an absence of distinguishable layers, suggesting that maturation of the vocal fold is at least in part dependent on the emergence of a trilayered lamina propria . Another study suggested the evolution from a monolayered lamina propria at birth to a trilayered structure by age 13 years .…”

Section: Introductionmentioning

confidence: 96%

“…Analogous studies of fetal lamina propria demonstrates an absence of distinguishable layers, suggesting that maturation of the vocal fold is at least in part dependent on the emergence of a trilayered lamina propria. 17 Another study suggested the evolution from a monolayered lamina propria at birth to a trilayered structure by age 13 years. 18 However, a study evaluating the utility of histopathology alone to differentiate layers within the lamina propria found that even senior pathologists were, at best, only capable of distinguishing 1-, 2-, and 3-layered lamina propria 76% of the time.…”

Section: Introductionmentioning

confidence: 99%

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Using attenuation coefficients from optical coherence tomography as markers of vocal fold maturation

et al. 2015

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Section: Introductionmentioning

confidence: 96%

Section: Introductionmentioning

confidence: 99%

Using attenuation coefficients from optical coherence tomography as markers of vocal fold maturation

et al. 2015

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“…In contrast to the trachea, the extracellular matrix of the vocal folds of the larynx (which lie just superior to the trachea) continues to be a popular research topic, including studies of collagen types, elastin, and proteoglycans [18][19][20][21][22][23][24][25][26][27][28][29][30][31][32][33][34][35][36]. However, despite the wide variety of trachea characterization efforts, ranging from camel trachea dimensions [37] to dolphin trachea biomechanics [38], and even speculation of airflow in dinosaur tracheas [39], very little is known about the distribution of key extracellular matrix components of the trachea.…”

Section: Introductionmentioning

confidence: 99%

Immunohistochemical characterization of the rabbit tracheal cartilages

Wemer¹,

Detamore²,

Weatherly³

2010

JBiSE

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The objective of this study was to immunohistochemically elucidate the major extracellular matrix constituents of rabbit tracheal cartilage. The impetus for this project is the need for crucial design and validation criteria for tissue engineering juxtaposed with the conspicuous lack of trachea extracellular matrix data in the literature. Tracheal tissue specimens were harvested from New Zealand White rabbits, and were immunostained for collagen I, collagen II, aggrecan and decorin; and a Verhoeff-Van Gieson stain was performed to visualize elastin. The most striking result was the highly organized relationship between distinct fibrous (containing collagen I, decorin and elastin) and hyaline-like (containing collagen II and aggrecan) regions of the tracheal wall. The tracheal cartilage stained strongly with collagen II throughout, with periodic bands of aggrecan in the tracheal arches, meaning that there were areas void of aggrecan immunostaining alternating with areas with strong aggrecan immunostaining. In contrast, the periphery of the cartilage and the perichondrium itself exhibited strong collagen I staining and no collagen II staining. Elastin fibers and decorin were also detected along the periphery of the cartilage in the perichondrium and corresponded highly with the distribution of collagen I staining. The body of the rabbit trachea is therefore composed of a hyaline-cartilage structure primarily made of collagen II and bands of aggrecan, surrounded by a fibrous region composed of elastin and collagen I, indicative of a flexible tissue with distinct regions of compressive integrity. This information will be a valuable reference to future tissue engineering efforts in the creation of a biosynthetic substitute for laryngotracheal reconstruction

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“…Similarly, variations were present in the expression of versican. Versican, a large proteoglycan, regulates the water content of tissues, participates in the assembly of different ECM components, and plays an important regulatory role in cell biology [20]. Because of its location, the CPM is subject to more trauma than most limb muscles [6] and is frequently exposed to physical and chemical stressors [5].…”

Section: Discussionmentioning

confidence: 99%

Extracellular Matrix Composition of the Cricopharyngeus Muscle

et al. 2011

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The aim of this study was to analyze the presence and distribution of total collagen, type I and type III collagen, elastic fibers, fibronectin, and versican in the endomysium of cricopharyngeus muscles from adults of various ages. The study was a cross-sectional analysis of human cricopharyngeus muscles. Twenty-seven muscles obtained from autopsies of men and women ranging in age from 28 to 92 years were analyzed with the Picrosirius method, oxidized Weigert resorcin-fuchsin, immunohistochemistry, and image analysis. Collagen had the highest density among the analyzed components. Elastic fibers surrounded each muscle cell; they were aligned longitudinally by their long axis and associated with traversing fibers, thereby forming a fiber network with embedded muscle cells. The fibronectin and versican contents varied widely among the specimens. We found no statistically significant differences between the proportion of extracellular matrix (ECM) components and factors such as gender and race. We conclude that the higher proportion of type I and type III collagen is compatible with the cricopharyngeus muscle's sphincteric behavior, and the arrangement of the elastic fibers may also contribute to the muscle's elasticity. We found no statistically significant correlation between the ECM components and age.

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Collagen Fiber and Versican Distribution Within the Lamina Propria of Fetal Vocal Folds

Abstract: Our findings suggest that collagen and versican distribution and arrangement within the lamina propria in the developing fetus are important for vocalization at birth.

Cited by 15 publications

References 20 publications

Using attenuation coefficients from optical coherence tomography as markers of vocal fold maturation

Using attenuation coefficients from optical coherence tomography as markers of vocal fold maturation

Immunohistochemical characterization of the rabbit tracheal cartilages

Extracellular Matrix Composition of the Cricopharyngeus Muscle

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