Cytochemical localization of terminal N-acetyl-D-galactosamine residues in cellular compartments of intestinal goblet cells: implications for the topology of O-glycosylation - PubMed (original) (raw)

Cytochemical localization of terminal N-acetyl-D-galactosamine residues in cellular compartments of intestinal goblet cells: implications for the topology of O-glycosylation

J Roth. J Cell Biol. 1984 Feb.

Abstract

The O-linked oligosaccharides of mucin-type glycoproteins contain N-acetyl-D-galactosamine (GalNAc) that is not found in N-linked glycoproteins. Because Helix pomatia lectin interacts with terminal GalNAc, we used this lectin, bound to particles of colloidal gold, to localize such sugar residues in subcellular compartments of intestinal goblet cells. When thin sections of low temperature Lowicryl K4M embedded duodenum or colon were incubated with Helix pomatia lectin-gold complexes, no labeling could be detected over the cisternal space of the nuclear envelope and the rough endoplasmic reticulum. A uniform labeling was observed over the first and several subsequent cis Golgi cisternae and over the last (duodenal goblet cells) or the two last (colonic goblet cells) trans Golgi cisternae as well as forming and mature mucin droplets. However, essentially no labeling was detected over several cisternae in the central (medial) region of the Golgi apparatus. The results strongly suggest that core O-glycosylation takes place in cis Golgi cisternae but not in the rough endoplasmic reticulum. The heterogenous labeling for GalNAc residues in the Golgi apparatus is taken as evidence that termination of certain O-oligosaccharide chains by GalNAc occurs in trans Golgi cisternae.

PubMed Disclaimer

Cited by

The Exploitation of the Glycosylation Pattern in Asthma: How We Alter Ancestral Pathways to Develop New Treatments.
Muchowicz A, Bartoszewicz A, Zaslona Z. Muchowicz A, et al. Biomolecules. 2024 Apr 24;14(5):513. doi: 10.3390/biom14050513. Biomolecules. 2024. PMID: 38785919 Free PMC article. Review.
Lectin histochemistry of posterior lingual glands of developing rats.
Harada K, Miki K, Tanaka S, Kogo M, Wakisaka S. Harada K, et al. Sci Rep. 2023 Jun 26;13(1):10365. doi: 10.1038/s41598-023-36154-9. Sci Rep. 2023. PMID: 37365173 Free PMC article.
Serotonin 5-HT2C Receptor Cys23Ser Single Nucleotide Polymorphism Associates with Receptor Function and Localization In Vitro.
Land MA, Chapman HL, Davis-Reyes BD, Felsing DE, Allen JA, Moeller FG, Elferink LA, Cunningham KA, Anastasio NC. Land MA, et al. Sci Rep. 2019 Nov 13;9(1):16737. doi: 10.1038/s41598-019-53124-2. Sci Rep. 2019. PMID: 31723224 Free PMC article.
From glycophenotyping by (plant) lectin histochemistry to defining functionality of glycans by pairing with endogenous lectins.
Kaltner H, García Caballero G, Ludwig AK, Manning JC, Gabius HJ. Kaltner H, et al. Histochem Cell Biol. 2018 Jun;149(6):547-568. doi: 10.1007/s00418-018-1676-7. Epub 2018 May 5. Histochem Cell Biol. 2018. PMID: 29730795 Review.
Disruption of Golgi morphology and altered protein glycosylation in PLA2G6-associated neurodegeneration.
Davids M, Kane MS, He M, Wolfe LA, Li X, Raihan MA, Chao KR, Bone WP, Boerkoel CF, Gahl WA, Toro C. Davids M, et al. J Med Genet. 2016 Mar;53(3):180-9. doi: 10.1136/jmedgenet-2015-103338. Epub 2015 Dec 14. J Med Genet. 2016. PMID: 26668131 Free PMC article.

References

1. J Biol Chem. 1979 Nov 25;254(22):11655-63 - PubMed
1. Proc Natl Acad Sci U S A. 1972 Nov;69(11):3268-72 - PubMed
1. J Biol Chem. 1980 Feb 10;255(3):1000-7 - PubMed
1. Arch Biochem Biophys. 1980 Jan;199(1):249-58 - PubMed
1. J Biol Chem. 1980 Mar 25;255(6):2325-31 - PubMed

Cytochemical localization of terminal N-acetyl-D-galactosamine residues in cellular compartments of intestinal goblet cells: implications for the topology of O-glycosylation - PubMed (original) (raw)