Fine structure of the retrocerebral organ in the rotifer Trichocerca similis (Monogononta)

The retrocerebral organ (RCO) is a complex glandular system that is widely distributed across species of phylum Rotifera (sensu stricto). This system is hypothesized to secrete mucus that aids in benthic locomotion, adhesion, and/or reproduction. Unfortunately, the ultrastructure of the RCO is mostly unknown, having only been partially examined in one species. We used transmission electron microscopy and confocal laser scanning microscopy to describe the RCO in the planktonic freshwater rotifer Trichocerca similis. Results reveal the RCO to be a singular syncytial organ composed of a posterior glandular region, an expansive reservoir, and an anterior duct. The glandular portion has an active synthetic cytoplasm with paired nuclei, abundant rER, ribosomes, Golgi, and mitochondria. Electron-dense secretion granules accumulate at the anterior end of the gland and undergo homotypic fusion to create larger, more electron-lucent granules with numerous mesh-like contents that gradually fuse into tubular secretions that accumulate in the reservoir. Ultrastructure of these secretions suggests they may be hydrated glycoproteins. Cross-striated longitudinal muscles form a partial sleeve around the reservoir and may function to squeeze the secretions through the single cytoplasmic duct that penetrates the cerebral ganglion. A review of the RCOs from other rotifers suggests that further ultrastructural analyses are required before attempting to discern their functions and homologies.

Automated summary

The retrocerebral organ (RCO) is a singular syncytial organ composed of a posterior glandular region, an expansive reservoir, and an anterior duct. The glandular portion has an active synthetic cytoplasm with paired nuclei, abundant rER, ribosomes, Golgi, and mitochondria. Granules from the gland undergo homotypic fusion to form tubular secretions that accumulate in the reservoir. The ultrastructure suggests these secretions may be hydrated glycoproteins.