Absorption of albumin by the midgut of a lepidopteran larva

• Published in: Journal of insect physiology Vol. 51; no. 8; pp. 933 - 940
• Main Authors: Casartelli, Morena, Corti, Paola, Giovanna Leonardi, M., Fiandra, Luisa, Burlini, Nedda, Pennacchio, Francesco, Giordana, Barbara
• Format: Journal Article
• Language: English
• Published: England Elsevier Ltd 01.08.2005
• Subjects: albumins; Albumins - metabolism; Animals; Bombyx - metabolism; Bombyx mori; Bombyx mori larval midgut; Digestive System - metabolism; epithelial cells; FITC-albumin; fluorescent labeling; Intestinal Absorption; Intestinal Mucosa - metabolism; Larva - metabolism; larvae; Lepidoptera; midgut; Protein absorption; protein transcytosis; protein transport; silkworms; Transcytosis; transepithelial transport; Transcytosis; Bombyx mori larval midgut; FITC-albumin; Protein absorption
• ISSN: 0022-1910; 1879-1611
• DOI: 10.1016/j.jinsphys.2005.04.008

In the last decade, the study of peptide and protein absorption by the insect gut has received increasing attention because of the considerable impact this information may have on the development of new delivery strategies for insecticide macromolecules targeting haemocoelic receptors. Available experimental evidence in vivo suggests that, in insects, peptides and proteins can cross the intestinal barrier reaching the haemocoel, but the functional bases of this absorption pathway have not yet been thoroughly investigated. The current knowledge of the mechanisms involved in protein and polypeptide absorption in animals derives from the extensive studies performed in mammalian polarised epithelial cells, where the transcellular transport of proteins by transcytosis has been demonstrated. In this process, proteins are internalised at one pole of the cell and transported by cytoplasmic vesicular traffic to the opposite plasma membrane domain, where they are released with unchanged biological activity. Here we report data on albumin translocation across the isolated midgut of Bombyx mori caterpillars perfused in vitro. The functional properties of the transepithelial transport of this protein are described and, since absorption prevails over secretion, its lumen-to-haemolymph flux is characterised. Low-temperature incubations nearly abolish the transepithelial transport, while the peculiar physiological features of the larval midgut, i.e. the high lumen positive transepithelial voltage and the luminal alkaline pH, do not affect the flux. The obtained results indicate that albumin crosses B. mori larval midgut by transcytosis.