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Immunolocalization of LM2 arabinogalactan protein epitope associated with endomembranes of plant cells

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Summary

Arabinogalactan proteins (AGPs) are proteoglycans detected in high amounts at plant cell surfaces; however, details of their subcellular localization are largely unknown. Immunolocalization studies with the anti-AGP monoclonal antibody LM2 have indicated that this AGP epitope is associated with secretory compartments such as endoplasmic reticulum and Golgi apparatus within plant cells actively producing and secreting AGPs. The LM2 epitope contains a β-linked glucuronic acid residue and occurs in the polysaccharide moiety of AGPs. We have localized this AGP epitope also to the tonoplast and to cytoplasmic strands. Endomembrane association of AGPs was confirmed with two other monoclonal antibodies, JIM13 and MAC207, both reacting with carbohydrate AGP epitopes containing GlcpA-β(1→3)-D-GalpA-α(1→2)-L-Rha residues. Immunocytochemistry is supported by biochemical analysis which shows that LM2 reacts with the microsomal fraction and also with low-molecular-weight material of the detergent phase after Triton X-114 phase separation prepared from maize roots. Our results indicate that some AGP epitopes are closely associated with endomembranes.

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Abbreviations

AGP:

arabinogalactan protein

ER:

endoplasmic reticulum

GlcA:

glucuronic acid

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Dedicated to Professor Walter Gustav Url on the occasion of his 70th birthday

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Šamaj, J., Šamajová, O., Peters, M. et al. Immunolocalization of LM2 arabinogalactan protein epitope associated with endomembranes of plant cells. Protoplasma 212, 186–196 (2000). https://doi.org/10.1007/BF01282919

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