Exploring the in vivo wound healing effects of a recombinant hemolin from the caterpillar Lonomia obliqua

 

Ana Claudia Sato^1, Rosemary Viola Bosch^1, Sonia Elisabete Alves Will^1, Miryam Paola Alvarez-Flores^1, Mauricio Barbugiani Goldfeder^1, Kerly Fernanda Mesquita Pasqualoto^1, Bárbara Athayde Vaz Galvão da Silva^1, Sonia Aparecida de Andrade^1, Ana Marisa Chudzinski-Tavassi^1.

 

1 Laboratory of Biochemistry and Biophysics, Butantan Institute, Av. Vital Brasil 1500, São Paulo, SP 05503-900, Brazil

 

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.

 

Key words: Hemolin; rLosac; Wound healing; Collagen

 

Funding

This work was supported by the State of São Paulo Research Foundation (FAPESP), grant no. 2013/06892-0, and CETICS-FAPESP, grant no. 2013/07467-1. RVB and BAVGS held scholarships from FAPESP. This work was also supported by the Edital Toxinologia CAPES no. 063/2010.

 

Received: July 21, 2016.

Revised: December 5, 2016.

Accepted: December 21, 2016.

 

Correspondence: ana.chudzinski@butantan.gov.br

 

Authors’ contributions

AMCT designed the research. ACS, RVB, SW performed the research and analyzed the data. SAA analyzed the data and wrote the paper. MBG and MPF expressed and purified the recombinant protein. MPF also wrote the paper. All authors read and approved the final manuscript.

 

Authors’ information

Laboratory of Biochemistry and Biophysics, Butantan Institute, São Paulo, SP, Brazil.

 

Competing interests

The authors declare that there are no competing interests.