Molecular machinery of starch digestion and glucose absorption along the midgut of Musca domestica. (August 2018)
- Record Type:
- Journal Article
- Title:
- Molecular machinery of starch digestion and glucose absorption along the midgut of Musca domestica. (August 2018)
- Main Title:
- Molecular machinery of starch digestion and glucose absorption along the midgut of Musca domestica
- Authors:
- Pimentel, André C.
Barroso, Ignacio G.
Ferreira, Jéssica M.J.
Dias, Renata O.
Ferreira, Clélia
Terra, Walter R. - Abstract:
- Graphical abstract: Highlights: Triplicate RNA-seq analyses were prepared from midgut sections and carcass. Enzymes and sugar transporters (SP) were searched in the reference genome. The expression of two amylases, three maltases, and 9 SPs were determined. MdSP1 (apical), MdSP7 (basal), and MdSP9 (apical) are up-regulated by starch. A model is proposed for the stepwise digestion and absorption of starch/glycogen. Abstract: Until now there is no molecular model of starch digestion and absorption of the resulting glucose molecules along the larval midgut of Musca domestica . For addressing to this, we used RNA-seq analyses from seven sections of the midgut and carcass to evaluate the expression level of the genes coding for amylases, maltases and sugar transporters (SP). An amylase related protein (Amyrel) and two amylase sequences, one soluble and one with a predicted GPI-anchor, were identified. Three highly expressed maltase genes were correlated with biochemically characterized maltases: one soluble, other glycocalyx-associated, and another membrane-bound. SPs were checked as being apical or basal by proteomics of microvillar preparations and those up-regulated by starch were identified by real time PCR. From the 9 SP sequences with high expression in midgut, two are putative sugar sensors (MdSP4 and MdSP5), one is probably a trehalose transporter (MdSP8), whereas MdSP1-3, MdSP6, and MdSP9 are supposed to transport glucose into cells, and MdSP7 from cells to hemolymph.Graphical abstract: Highlights: Triplicate RNA-seq analyses were prepared from midgut sections and carcass. Enzymes and sugar transporters (SP) were searched in the reference genome. The expression of two amylases, three maltases, and 9 SPs were determined. MdSP1 (apical), MdSP7 (basal), and MdSP9 (apical) are up-regulated by starch. A model is proposed for the stepwise digestion and absorption of starch/glycogen. Abstract: Until now there is no molecular model of starch digestion and absorption of the resulting glucose molecules along the larval midgut of Musca domestica . For addressing to this, we used RNA-seq analyses from seven sections of the midgut and carcass to evaluate the expression level of the genes coding for amylases, maltases and sugar transporters (SP). An amylase related protein (Amyrel) and two amylase sequences, one soluble and one with a predicted GPI-anchor, were identified. Three highly expressed maltase genes were correlated with biochemically characterized maltases: one soluble, other glycocalyx-associated, and another membrane-bound. SPs were checked as being apical or basal by proteomics of microvillar preparations and those up-regulated by starch were identified by real time PCR. From the 9 SP sequences with high expression in midgut, two are putative sugar sensors (MdSP4 and MdSP5), one is probably a trehalose transporter (MdSP8), whereas MdSP1-3, MdSP6, and MdSP9 are supposed to transport glucose into cells, and MdSP7 from cells to hemolymph. MdSP1, MdSP7, and MdSP9 are up-regulated by starch. Based on the data, starch is at first digested by amylase and maltases at anterior midgut, with the resulting glucose units absorbed at middle midgut. At this region, low pH, lysozyme, and cathepsin D open the ingested bacteria and fungi cells, freeing sugars and glycogen. This and the remaining dietary starch are digested by amylase and maltases at the end of middle midgut and up to the middle part of the posterior midgut, with resulting sugars being absorbed along the posterior midgut. … (more)
- Is Part Of:
- Journal of insect physiology. Volume 109(2018)
- Journal:
- Journal of insect physiology
- Issue:
- Volume 109(2018)
- Issue Display:
- Volume 109, Issue 2018 (2018)
- Year:
- 2018
- Volume:
- 109
- Issue:
- 2018
- Issue Sort Value:
- 2018-0109-2018-0000
- Page Start:
- 11
- Page End:
- 20
- Publication Date:
- 2018-08
- Subjects:
- Amylase -- Maltase -- Sugar transporters -- α-Glucosidase -- Amyrel -- Transporter up-regulation
Insects -- Physiology -- Periodicals
Insectes -- Physiologie -- Périodiques
Insects -- Physiology
Periodicals
571.157 - Journal URLs:
- http://www.sciencedirect.com/science/journal/00221910 ↗
http://www.journals.elsevier.com/journal-of-insect-physiology/ ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.jinsphys.2018.05.009 ↗
- Languages:
- English
- ISSNs:
- 0022-1910
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 5007.500000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 12398.xml