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1.
J. venom. anim. toxins incl. trop. dis ; 22: [1-8], 2016. ilus, graf
Article in English | LILACS, VETINDEX | ID: biblio-1484658

ABSTRACT

Hemolin proteins are cell adhesion molecules from lepidopterans involved in a wide range of cell interactions concerning their adhesion properties. However, hemolins roles in cell proliferation and wound healing are not fully elucidated. It has been recently reported that rLosac, a recombinant hemolin from the caterpillar Lonomia obliqua, presents antiapoptotic activity and is capable of improving in vitro wound healing. Therefore, this study aimed to explore rLosacs in vivo effects using a skin wound healing model in rats. Methods Circular full-thickness wounds in the rat dorsum skin were treated either with rLosac, or with saline (control), allowing healing by keeping the wounds occluded and moist. During the wound healing, the following tissue regeneration parameters were evaluated: wound closure and collagen content. Furthermore, tissue sections were subjected to histological and immunohistochemical analyses. Results The rLosac treatment has demonstrated its capacity to improve wound healing, as reflected in findings of a larger number of activated fibroblasts, proliferation of epithelial cells, increase of collagen type 1, and decrease of inflammatory infiltrate. Conclusion The findings have indicated the rLosac protein as a very promising molecule for the development of new wound-healing formulations.


Subject(s)
Wound Healing , Apoptosis Regulatory Proteins/analysis , Apoptosis Regulatory Proteins/adverse effects , Lepidoptera/chemistry
2.
Article in English | LILACS, VETINDEX | ID: biblio-954806

ABSTRACT

Background Hemolin proteins are cell adhesion molecules from lepidopterans involved in a wide range of cell interactions concerning their adhesion properties. However, hemolin's roles in cell proliferation and wound healing are not fully elucidated. It has been recently reported that rLosac, a recombinant hemolin from the caterpillar Lonomia obliqua, presents antiapoptotic activity and is capable of improving in vitro wound healing. Therefore, this study aimed to explore rLosac's in vivo effects using a skin wound healing model in rats. Methods Circular full-thickness wounds in the rat dorsum skin were treated either with rLosac, or with saline (control), allowing healing by keeping the wounds occluded and moist. During the wound healing, the following tissue regeneration parameters were evaluated: wound closure and collagen content. Furthermore, tissue sections were subjected to histological and immunohistochemical analyses. Results The rLosac treatment has demonstrated its capacity to improve wound healing, as reflected in findings of a larger number of activated fibroblasts, proliferation of epithelial cells, increase of collagen type 1, and decrease of inflammatory infiltrate. Conclusion The findings have indicated the rLosac protein as a very promising molecule for the development of new wound-healing formulations.(AU)


Subject(s)
Skin/injuries , Wound Healing , Wounds and Injuries , Proteins , Cell Proliferation , Epithelial Cells , Lepidoptera
3.
São PAulo; s.n; 22 set. 2008. [155] p. ilus, graf, tab.
Thesis in Portuguese | LILACS | ID: lil-508063

ABSTRACT

Em eucariotos, a formação das subunidades ribossomais envolve múltiplos fatores, responsáveis pelas etapas de maturação dos rRNAs e por sua associação a proteínas ribossomais. A via de processamento de pré-rRNA é bastante complexa e inclui várias etapas de modificação de nucleotídeos e clivagens endo- e exonucleolíticas. As modificações de nucleotídeos são dirigidas por snoRNPs, formados por snoRNAs e proteínas, que são divididos em duas classes gerais, de box H/ACA (pseudouridilação) e de box C/O (metilação). Dentre os snoRNP de box C/D esta o U3, que embora apresente as sequências características e se associe a proteínas desse grupo de snoRNPs, não dirige metilações no rRNA, mas sim as clivagens iniciais no pré-rRNA 35S. O snoRNA U3 de Saccharomyces cerevisiae é codificado por dois genes que contêm introns, snR17A e snR17B. Embora a via de montagem do snoRNP U3 ainda não tenha sido determinada com precisão, sabe-se que algumas proteínas do core de box C/O ligam-se ao pré-snoRNA U3 co-transcricionalmente, afetando o splicing e o processamento da extremidade 3´ deste snoRNA...


Subject(s)
DNA , In Vitro Techniques , Saccharomyces cerevisiae Proteins/analysis , Saccharomyces cerevisiae Proteins/isolation & purification , RNA, Ribosomal/analysis , RNA, Ribosomal/isolation & purification , Ribosomes/genetics , Saccharomyces cerevisiae/growth & development , Saccharomyces cerevisiae/genetics , Culture Media , Escherichia coli/cytology , Escherichia coli/isolation & purification , Polymerase Chain Reaction/methods , Polymerase Chain Reaction , Blotting, Western/methods , Blotting, Western
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