scholarly journals The Fine Structure ofCaenorhabditis elegans N-Glycans

2002 ◽  
Vol 277 (51) ◽  
pp. 49143-49157 ◽  
Author(s):  
John F. Cipollo ◽  
Catherine E. Costello ◽  
Carlos B. Hirschberg

We report the fine structure of a nearly contiguous series ofN-glycans from the soil nematodeCaenorhabditis elegans.Five major classes are revealed including high mannose, mammalian-type complex, hybrid, fuco-pausimannosidic (five mannose residues or fewer substituted with fucose), and phosphocholine oligosaccharides. The high mannose, complex, and hybridN-glycan series show a high degree of conservation with the mammalian biosynthetic pathways. The fuco-pausimannosidic glycans contain a novel terminal fucose substitution of mannose. The phosphocholine oligosaccharides are high mannose type and are multiply substituted with phosphocholine. Although phosphocholine oligosaccharides are known immunomodulators in human nematode and trematode infections,C. elegansis unique as a non-parasitic nematode containing phosphocholineN-glycans. Therefore, studies inC. elegansshould aid in the elucidation of the biosynthetic pathway(s) of this class of biomedically relevant compounds. Results presented here show thatC. eleganshas a functional orthologue for nearly every known enzyme found to be deficient in congenital disorders of glycosylation types I and II. This nematode is well characterized genetically and developmentally. Therefore, elucidation of itsN-glycome, as shown in this report, may place it among the useful systems used to investigate human disorders of glycoconjugate synthesis such as the congenital disorders of glycosylation syndromes.

2021 ◽  
Author(s):  
Hannes E Bülow ◽  
Maisha Rahman ◽  
Nelson J. Ramirez-Suarez ◽  
Carlos A Diaz-Balzac

N-glycans are molecularly diverse sugars borne by over 70% of proteins transiting the secretory pathway and have been implicated in protein folding, stability, and localization. Mutations in genes important for N-glycosylation result in congenital disorders of glycosylation that are often associated with intellectual disability. Here, we show that structurally distinct N-glycans regulate the activity of an extracellular protein complex involved in patterning of somatosensory dendrites in Caenorhabditis elegans. Specifically, aman-2/Golgi alpha-mannosidase II, a conserved key enzyme in the biosynthesis of specific N-glycans regulates the activity of the Menorin adhesion complex without obviously affecting protein stability and localization of its components. AMAN-2 functions cell-autonomously to ensure decoration of the neuronal transmembrane receptor DMA-1/LRR-TM with high-mannose/hybrid N-glycans. Moreover, distinct types of N-glycans on specific N-glycosylation sites regulate the DMA-1/LRR-TM receptor, which together with three other extracellular proteins forms the Menorin adhesion complex. In summary, specific N-glycan structures regulate dendrite patterning by coordinating the activity of an extracellular adhesion complex suggesting that the molecular diversity of N-glycans can contribute to developmental specificity in the nervous system.


Author(s):  
Patryk Lipiński ◽  
Joanna Cielecka-Kuszyk ◽  
Elżbieta Czarnowska ◽  
Anna Bogdańska ◽  
Piotr Socha ◽  
...  

Author(s):  
Alexandre Raynor ◽  
Catherine Vincent-Delorme ◽  
Anne-Sophie Alaix ◽  
Sophie Cholet ◽  
Thierry Dupré ◽  
...  

2015 ◽  
Vol 2015 ◽  
pp. 1-9 ◽  
Author(s):  
Tohru Fujiwara ◽  
Hideo Harigae

Heme is a prosthetic group comprising ferrous iron (Fe2+) and protoporphyrin IX and is an essential cofactor in various biological processes such as oxygen transport (hemoglobin) and storage (myoglobin) and electron transfer (respiratory cytochromes) in addition to its role as a structural component of hemoproteins. Heme biosynthesis is induced during erythroid differentiation and is coordinated with the expression of genes involved in globin formation and iron acquisition/transport. However, erythroid and nonerythroid cells exhibit distinct differences in the heme biosynthetic pathway regulation. Defects of heme biosynthesis in developing erythroblasts can have profound medical implications, as represented by sideroblastic anemia. This review will focus on the biology of heme in mammalian erythroid cells, including the heme biosynthetic pathway as well as the regulatory role of heme and human disorders that arise from defective heme synthesis.


2017 ◽  
Vol 21 ◽  
pp. e139-e140
Author(s):  
R. Calvo Medina ◽  
A. Calvo-Cillan ◽  
M. Sanchez Muñoz ◽  
M. mantecon Barranco ◽  
M.A. Aviles-tirado ◽  
...  

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