Extrarenal angiomyolipoma in uterine cervix: rare presentation in unusual site

Angiomyolipoma is a benign neoplasm composed of variable admixture of blood vessels, smooth muscle cells and adipose tissue. Cervical angiomyolipoma are extremely rare and to the best of our knowledge only five cases of angiomyolipoma in cervix have been reported in the literature till date. Authors are presenting a case of angiomyolipoma arising from the uterine cervix. 43 years old female presented with mass descending per vagina for 6 months. This case had no association with tuberous sclerosis. Microscopic examination showed an ill-defined polypoidal, non-encapsulated lesion covered by keratinized stratified epithelium. The lesion is made up of three components, predominantly by fascicles of spindle shaped cells, varying sized blood vessels and multiple foci of mature adipocytes with no evidence of atypia or increased mitotic activity. Smooth muscle component showed strong immunoreactivity to SMA and absence of elastic fibres in the blood vessels were confirmed by histochemistry. Non-vascular smooth muscle cells were negative for HMB-45 in contrast to renal and other extra-renal angiomyolipoma in which HMB-45 immunoreactivity in seen in these cells. To conclude, the differential diagnosis of lower abdominal mass and dysfunctional uterine bleeding should include the angiomyolipoma, even though the uterine cervix is an extremely rare location where they occur.

In vitro characterization of jellyfish venom fibrin(ogen)olytic enzymes from Nemopilema nomurai

Background: Because jellyfish are capable of provoking envenomation in humans, they are considered hazardous organisms. Although the effects of their toxins are a matter of concern, information on the venom components, biological activity and pathological mechanisms are still scarce. Therefore, the aim of the present study was to investigate a serine protease component of Nemopilema nomurai jellyfish venom (NnV) and unveil its characteristics. Methods: To determine the relationship between fibrinolytic activity of NnV and the serine protease, fibrin zymography was performed using metalloprotease and serine protease inhibitors. The biochemical characterization of serine proteases of NnV were determined by the amidolytic assay. Fractions with fibrinolytic activity were obtained by DEAE cation exchange column. Results: NnV displayed fibrinolytic activities with molecular masses of approximately 70, 35, 30, and 28 kDa. The fibrinolytic activity of NnV was completely obliterated by phenylmethylsulfonyl fluoride, a prototype serine protease inhibitor. Based on amidolytic assays using chromogenic substrates specific for various kinds of serine proteases, NnV predominantly manifested a chymotrypsin-like feature. Its activity was completely eliminated at low pH (< 6) and high temperatures (> 37 °C). Some metal ions (Co2+, Cu2+, Zn2+ and Ni2+) strongly suppressed its fibrinolytic activity, while others (Ca2+ and Mg2+) failed to do so. Isolation of a serine protease with fibrionolytic activity from NnV revealed that only p3 showed the fibrinolytic activity, which was completely inhibited by PMSF. Conclusion: The present study showed that N. nomurai jellyfish venom has a chymotrypsin-like serine protease with fibrinolytic activity. Such information might be useful for developing clinical management of jellyfish envenomation and pharmacological agents with therapeutic potential for thrombotic diseases in the future.(AU)

In vitro characterization of jellyfish venom fibrin(ogen)olytic enzymes from Nemopilema nomurai

Abstract Background: Because jellyfish are capable of provoking envenomation in humans, they are considered hazardous organisms. Although the effects of their toxins are a matter of concern, information on the venom components, biological activity and pathological mechanisms are still scarce. Therefore, the aim of the present study was to investigate a serine protease component of Nemopilema nomurai jellyfish venom (NnV) and unveil its characteristics. Methods: To determine the relationship between fibrinolytic activity of NnV and the serine protease, fibrin zymography was performed using metalloprotease and serine protease inhibitors. The biochemical characterization of serine proteases of NnV were determined by the amidolytic assay. Fractions with fibrinolytic activity were obtained by DEAE cation exchange column. Results: NnV displayed fibrinolytic activities with molecular masses of approximately 70, 35, 30, and 28 kDa. The fibrinolytic activity of NnV was completely obliterated by phenylmethylsulfonyl fluoride, a prototype serine protease inhibitor. Based on amidolytic assays using chromogenic substrates specific for various kinds of serine proteases, NnV predominantly manifested a chymotrypsin-like feature. Its activity was completely eliminated at low pH ( 6) and high temperatures (> 37 °C). Some metal ions (Co2+, Cu2+, Zn2+ and Ni2+) strongly suppressed its fibrinolytic activity, while others (Ca2+ and Mg2+) failed to do so. Isolation of a serine protease with fibrionolytic activity from NnV revealed that only p3 showed the fibrinolytic activity, which was completely inhibited by PMSF. Conclusion: The present study showed that N. nomurai jellyfish venom has a chymotrypsin-like serine protease with fibrinolytic activity. Such information might be useful for developing clinical management of jellyfish envenomation and pharmacological agents with therapeutic potential for thrombotic diseases in the future.