Use este identificador para citar ou linkar para este item: http://repositorio.ufc.br/handle/riufc/66422
Tipo: Artigo de Periódico
Título: Nile tilapia skin (Oreochromis niloticus) for burn treatment: ultrastructural analysis and quantitative assessment of collagen
Autor(es): Verde, Maria Elisa Quezado Lima
Ferreira Júnior, Antonio Ernando Carlos
Silva, Paulo Goberlânio de Barros
Miguel, Emilio de Castro
Mathor, Monica Beatriz
Lima Júnior, Edmar Maciel
Moraes Filho, Manoel Odorico de
Alves, Ana Paula Negreiros Nunes
Palavras-chave: Tissue engineering;Tilapia;Collagen;Burns;Biocompatible materials
Data do documento: 2021
Instituição/Editor/Publicador: Acta Histochemica
Citação: LIMA VERDE, Maria Elisa Quezado et al. Nile tilapia skin (Oreochromis niloticus) for burn treatment: ultrastructural analysis and quantitative assessment of collagen. Acta Histochemica, [s.l.], v. 123, n. 6, p. 1-8, 2021.
Abstract: Nile tilapia (Oreochromis niloticus) skin is a well-known biomaterial used as an occlusive dressing for burn treatment. It is also an inexpensive and important source of collagen. This study aims to describe the ultrastructural aspects of Nile tilapia skin, assess its collagen amount and organization, and compare quantitative methods of histochemical and immunohistochemical analysis (in all sterilization steps for use in burn dressings). One sample (0.5 × 0.5 cm) of ten different fish skins was divided in four groups: in natura skin (IN), chemical sterilization (CH), additional irradiation (30 kGy) (IR), and skins used in burn treatment (BT) to compare histochemical and immunohistochemical findings of collagen amount and describe ultrastructural aspects through scanning electron microscopy. The amount of type I collagen decreased during sterilization and clinical use owing to gradual reduction of immunostaining (anti-collagen-I) and decreasing fiber thickness of the collagen, when compared to type III (Picrosirius-red-polarized light). The collagen fibers were rearranged at each sterilization step, with a low collagen percentage and large structural disorganization in BT. The amount of type-I collagen was further reduced after BT (p < 0.05). Both the methods did not exhibit a quantified value difference (p = 0.247), and a positive correlation (r = 0.927; 95 % CI = 0.720–0.983) was observed between them, with concordance for collagen quantification in similar samples, presenting a low systematic error rate (Dalberg coefficient: 6.70). A significant amount of type-I collagen is still observed despite sterilization, although clinical application further reduces type I collagen. Its quantification can be performed both by immunohistochemistry and/or Picrosirius Red reliably.
URI: http://www.repositorio.ufc.br/handle/riufc/66422
ISSN: 0065-1281
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