Quantitative and comparative studies of the vocal fold extracellular matrix II: Collagen
Quantitative and comparative studies of the vocal fold extracellular matrix II: Collagen
复制标题
DOI：
10.1177/000348940611500311
复制
发表时间：
2006-03-01
影响因子：
1.4
通讯作者：
Langer, R
中科院分区：
文献类型：
--
作者：
Hahn, MS;Kobler, JB;Langer, R
目的：研究人、狗、猪和雪貂声带中膜固有层的胶原含量和周转情况。方法：用组织羟脯氨酸定量的方法评价声带中膜固有层的胶原含量。定量组织学可以评估特定LP区域的胶原含量。结果：胶原占人LP总蛋白(TP)的43.4%+/-2.6%，男性高于女性约30%(p<；.024)。猪(占TP的52.6%+/-1.9%)和雪貂(占TP的29.8%+/-3.7%)和狗(占TP的45.3%+/-1.2%)的胶原含量与人(猪，P<；.016；雪貂，P<；.011)有显著差异。定量组织学表明，总胶原蛋白的分布在物种间存在显著差异。结论：人LP中胶原含量约为真皮的60%~70%。虽然犬LP的胶原蛋白水平与人类最相似，但定量组织学表明，人LP的胶原分布与猪LP最匹配。I型和III型胶原似乎是主要的LP胶原蛋白。胶原周转的空间差异似乎存在，这可能有助于正常的LP生理。
Objectives: This study examines the collagen content and turnover in the midmembranous vocal fold laminae propriae (LPs) of humans, dogs, pigs, and ferrets.Methods: The LP collagen levels were assessed by quantifying tissue hydroxyproline. Quantitative histology allowed evaluation of the collagen content in specific LP regions. Several collagen types and two markers of collagen turnover were examined immunohistochemically.Results: Collagen made up 43.4% +/- 2.6% of human LP total protein (TP), with men having approximately 30% higher collagen content than women (p < .024). The collagen levels in pigs (52.6% +/- 1.9% of TP) and ferrets (29.8% +/- 3.7% of TP), but not that in dogs (45.3% +/- 1.2% of TP), varied significantly from that in humans (pigs, p < .016; ferrets, p < .011). Quantitative histology indicated marked interspecies differences in total collagen distribution. Collagen types I, III, and IV were detected in the LP, and spatially complex staining patterns were observed for the two markers of collagen turnover studied.Conclusions: The collagen content of the human LP is approximately 60% to 70% of that of human dermis. Although canine LP collagen levels are most similar to those of humans, quantitative histology indicates that the collagen distribution of the human LP is best matched by the porcine LP. Collagen types I and III seem to be the dominant LP collagens. Spatial variations in collagen turnover appear to exist that may contribute to normal LP physiology.