title: Secapin, a bee venom peptide, exhibits anti-fibrinolytic, anti-elastolytic, and anti-microbial activities.
abstract: Bee venom contains a variety of peptide constituents that have various biological, toxicological, and pharmacological actions. However, the biological actions of secapin, a venom peptide in bee venom, remain largely unknown. Here, we provide the evidence that Asiatic honeybee (Apis cerana) secapin (AcSecapin-1) exhibits anti-fibrinolytic, anti-elastolytic, and anti-microbial activities. The recombinant mature AcSecapin-1 peptide was expressed in baculovirus-infected insect cells. AcSecapin-1 functions as a serine protease inhibitor-like peptide that has inhibitory effects against plasmin, elastases, microbial serine proteases, trypsin, and chymotrypsin. Consistent with these functions, AcSecapin-1 inhibited the plasmin-mediated degradation of fibrin to fibrin degradation products, thus indicating the role of AcSecapin-1 as an anti-fibrinolytic agent. AcSecapin-1 also inhibited both human neutrophil and porcine pancreatic elastases. Furthermore, AcSecapin-1 bound to bacterial and fungal surfaces and exhibited anti-microbial activity against fungi and gram-positive and gram-negative bacteria. Taken together, our data demonstrated that the bee venom peptide secapin has multifunctional roles as an anti-fibrinolytic agent during fibrinolysis and an anti-microbial agent in the innate immune response.
authors.affiliation: College of Natural Resources and Life Science, Dong-A University, Busan 604-714, Republic of Korea.
authors.forename: Kwang Sik
authors.initials: KS
authors.lastname: Lee
authors.affiliation: College of Natural Resources and Life Science, Dong-A University, Busan 604-714, Republic of Korea.
authors.forename: Bo Yeon
authors.initials: BY
authors.lastname: Kim
authors.affiliation: Department of Agricultural Biology, National Academy of Agricultural Science, Wanju 55365, Republic of Korea.
authors.forename: Hyung Joo
authors.initials: HJ
authors.lastname: Yoon
authors.affiliation: Department of Agricultural Biology, National Academy of Agricultural Science, Wanju 55365, Republic of Korea.
authors.forename: Yong Soo
authors.initials: YS
authors.lastname: Choi
authors.affiliation: College of Natural Resources and Life Science, Dong-A University, Busan 604-714, Republic of Korea. Electronic address: brjin@dau.ac.kr.
authors.forename: Byung Rae
authors.initials: BR
authors.lastname: Jin
mesh_terms: D000818:Animals; D000890:Anti-Infective Agents / Q000378:metabolism; D000933:Antifibrinolytic Agents / Q000378:metabolism; D016367:Baculoviridae / Q000235:genetics; D001514:Bee Venoms / Q000235:genetics / Q000378:metabolism*; D001516:Bees / Q000276:immunology*; D002460:Cell Line; D006801:Humans; D007113:Immunity, Innate; D019476:Insect Proteins / Q000235:genetics / Q000378:metabolism*; D019272:Leukocyte Elastase / Q000037:antagonists & inhibitors; D010196:Pancreatic Elastase / Q000037:antagonists & inhibitors; D013552:Swine
chemical_list: D000890:Anti-Infective Agents; D000933:Antifibrinolytic Agents; D001514:Bee Venoms; D019476:Insect Proteins; C029737:secapin; D010196:Pancreatic Elastase; D019272:Leukocyte Elastase
keywords: Anti-elastolytic agent; Anti-fibrinolytic agent; Anti-microbial peptide; Honeybee; Secapin; Venom