There are records of glands that produce sexual pheromones that are released into the environment or applied directly on sexual partners. Within Opiliones (Arachnida), several harvestmen in the suborder Laniatores have sexually dimorphic glands on legs I and IV, the mode of use of which is recorded only in two species but their function is unknown: while walking, males rub the glands against the substrate or against their body. Here we test an alternative and non-exclusive hypothesis that the glands present on the legs of male Gryne perlata (Cosmetidae) produce contact pheromones used in mating. We predicted that males would touch the females with the gland openings or with other male body parts previously rubbed by these glands. We also predicted that there are chemoreceptors on those parts of the females where males touch them. We analyzed 13 videos of G. perlata mating, a species in which the males have glands on legs I and IV of unknown function. We also analyzed 14 videos of Discocyrtus pectinifemur (Gonyleptidae) mating as a control, a species that lacks these glands. Finally, we looked for chemoreceptors on the legs of female G. perlata using a scanning electron microscope. During copulation, males of both species rubbed the legs of females with their first pair of legs, but not with the regions of these legs where the openings of the glands are. The fourth pair of legs were only used to support the body. Rubbing other body parts of the female by males with their glands was not observed during mating. Setae on the legs of the female did not have tip pores and therefore do not seem to be chemoreceptors. We therefore did not find any evidence that these sexually dimorphic glands in G. perlata release contact pheromones during mating., Jéssica M. Dias, Rodrigo H. Willemart., and Obsahuje bibliografii
Dactylopius coccus is a sessile scale insect living on cladodes of Opuntia ficus indica which has commercial importance as a source of carminic acid. We herein present behavioural evidence of the existence of a sex pheromone in D. coccus, based on olfactometric experiments using both biological sources of odours and collected chemical extracts.
Many biological processes involve globular transport proteins belonging to a family called lipocalins. The prominent feature in lipocalin structure is their specific tertiary conformation forming eight-stranded beta barrel with capacity to bind various ligands inside. The importance of lipocalins is evident from the list of vital substances (Hydrophobic ligands including vitamin A, steroids, bilins, lipids, pheromones etc.) that these proteins transport and from their high expression levels in various tissues. Among wide spectrum of lipocalins, Major Urinary Proteins (Mup) and Odorant Binding Proteins (Obp) are well known for their capacity to bind and carry odorants / pheromones and have been studied to detail in various mammalian models including mice, rats, and hamsters. However, many lipocalins (also including Mups) have previously been described with respect to their protective function in mammalian organism where they transport potentially harmful molecules to a degradation site (e. g. lysozomes) or straight out of the body. As most of lipocalins share similar tertiary structure, their potential role in both transport and excretion processes may be additive or complementary. In addition to a role of lipocalins in chemical communication this review presents lipocalins from the point of view of the "toxic waste hypothesis". This hypothesis assumes that members of lipocalins that are linked to a metabolic degradation of their ligands were an ideal source for natural selection during evolution due to an ability of potential receivers to detect lipocalin ligands levels as a signal by other individuals.
The presence of large amounts of proteins in mammal urine is usually associated with a pathological condition and indicates serious renal lesions. However, there are few species with obligate proteinuria indicating that they must derive some benefit from this condition. Urinary proteins have been most extensively studied in the house mouse and the rat, and findings to date indicate that their function in intraspecific communication is complex and not yet fully understood. Other proteins of the same protein family as MUPs have been also found in urine of some other rodent species, and still less is known about these. In this study we demonstrate the existence of urinary lipocalins in Mastomys coucha for the first time. Our results support the hypothesis that urinary proteins may play an important role in chemical communication, and level of polymorphism of these proteins in different rodents may help us to understand their specific function.