The small subunit of Hemilipin2, a new heterodimeric phospholipase A2 from Hemiscorpius lepturus scorpion venom, mediates the antiangiogenic effect of the whole protein

详细信息    查看全文

• 作者：Imen Jridi^a ; ^b ; ¹ ; Ivana Catacchio^c ; ¹ ; Hafed Majdoub^d ; Delavar Shahbazzadeh^e ; Mohamed El Ayeb^b ; Maria Antonia Frassanito^f ; Antonio Solimando^c ; Domenico Ribatti^g ; Angelo Vacca^c ; ² ; Lamia Borchani^b ; ² ; ^{Lamia.borchani@pasteur.rns.tn}
• 关键词：Angiogenesis ; Hemiscorpius lepturus sPLA2 group III ; Small subunit ; HUVEC ; HPAEC
• 刊名：Toxicon
• 出版年：2017
• 出版时间：February 2017
• 年：2017
• 卷：126
• 期：Complete
• 页码：38-46
• 全文大小：3286 K
• 卷排序：126

文摘

Hemilipin2 is heterodimeric secreted phospholipase A2 (sPLA2) purified from Hemiscorpius lepturus scorpion. Hemilipin2's large and small subunits have a molecular mass of 12866 and 2461 a.m.u. respectively. Hemilipin2’s large subunit has no homology with other sPLA2s group III. Hemilipin2 could form a subgroup of group III sPLA2. Hemilipin2 exhibits an anti-angiogenesis activity on cells migration, adhesion and vessel length, and in vivo on CAM model. The antiangiogenic effect appears to be independent from the catalytic activity and seemingly held by the small subunit.