Regeneration from seed affects species assembly in plant communities, and temperature is the most important environmental factor controlling the germination process. Thermal dependence of seed germination is thus associated with species occurrence in an ecosystem. Hence, we aimed to investigate the role of temperature on seed germination of ten tree species from the western Brazilian Amazon. Seeds were collected in the state of Rondônia, Brazil, and set to germinate under constant temperatures ranging from 10 to 40°C in germination chambers. We calculated germination capacity (G%), germination rate (GR50, reciprocal of germination time), and thermal parameters, such as cardinal temperatures and thermal time requirements. Most species had a large range of temperatures showing G% ≥80%, with optimal temperature varying from 20 to 40°C. Base temperature ranged from 6 to 12°C and ceiling temperatures were mainly >40°C. Astronium lecointei and Parkia nitida showed high germination capacity under temperatures of 35–40°C, while germination of Theobroma cacao dropped from 100% to zero under temperatures between 37 and 40°C. The climax species Cedrela fissilis had the slowest germination time (10 days) and highest thermal time requirement, while seeds of Enterolobium schomburgkii (a late-successional species) germinated within the first day of the experiment. Rapid recruitment of Amazon species could be favoured with treefall disturbance, which increases temperatures in the understory, but sharp limits might be found in the supra-optimal range of temperatures. Such patterns might indicate different regeneration strategies in the tropical rainforest, providing important information regarding seed germination among Amazon species.

Snakes of the genus Lachesis , commonly known as bushmasters, are the largest venomous snakes in the Americas. Because these snakes have their habitats in areas of remote forests they are difficult to find, and consequently there are few studies of Lachesis taxa in their natural ecosystems. Bushmasters are distributed in tropical forest areas of South and Central America. In Brazil they can be found in the Amazon Rainforest and the Atlantic Forest. Despite the low incidence of cases, laquetic envenoming causes severe permanent sequelae due to the high amount of inoculated venom. These accidents are characterized by local pain, hemorrhage and myonecrosis that can be confused with bothropic envenomings. However, victims of Lachesis bites develop symptoms characteristic of Lachesis envenoming, known as vagal syndrome. An important message of this bibliographic synthesis exercise is that, despite having the proteomic profiles of all the taxa of the genus available, very few structure-function correlation studies have been carried out. Therefore the motivation for this review was to fill a gap in the literature on the genus Lachesis , about which there is no recent review. Here we discuss data scattered in a number of original articles published in specialized journals, spanning the evolutionary history and extant phylogeographic distribution of the bushmasters, their venom composition and diet, as well as the pathophysiology of their bites to humans and the biological activities and possible biotechnological applicability of their venom toxins.

Background: Cathepsin D (CatD) is a lysosomal proteolytic enzyme expressed in almost all tissues and organs. This protease is a multifunctional enzyme responsible for essential biological processes such as cell cycle regulation, differentiation, migration, tissue remodeling, neuronal growth, ovulation, and apoptosis. The overexpression and hypersecretion of CatD have been correlated with cancer aggressiveness and tumor progression, stimulating cancer cell proliferation, fibroblast growth, and angiogenesis. In addition, some studies report its participation in neurodegenerative diseases and inflammatory processes. In this regard, the search for new inhibitors from natural products could be an alternative against the harmful effects of this enzyme. Methods: An investigation was carried out to analyze CatD interaction with snake venom toxins in an attempt to find inhibitory molecules. Interestingly, human CatD shows the ability to bind strongly to snake venom phospholipases A 2 (svPLA 2 ), forming a stable muti-enzymatic complex that maintains the catalytic activity of both CatD and PLA 2 . In addition, this complex remains active even under exposure to the specific