Display options
Cite
Herman EM, Lamb CJ. Arabinogalactan-rich glycoproteins are localized on the cell surface and in intravacuolar multivesicular bodies. Plant Physiol. 1992;98(1):264-72doi: 10.1104/pp.98.1.264.
Herman, E. M., & Lamb, C. J. (1992). Arabinogalactan-rich glycoproteins are localized on the cell surface and in intravacuolar multivesicular bodies. Plant physiology, 98(1), 264-72. https://doi.org/10.1104/pp.98.1.264
Herman, E M, and Lamb, C J. "Arabinogalactan-rich glycoproteins are localized on the cell surface and in intravacuolar multivesicular bodies." Plant physiology vol. 98,1 (1992): 264-72. doi: https://doi.org/10.1104/pp.98.1.264
Herman EM, Lamb CJ. Arabinogalactan-rich glycoproteins are localized on the cell surface and in intravacuolar multivesicular bodies. Plant Physiol. 1992 Jan;98(1):264-72. doi: 10.1104/pp.98.1.264. PMID: 16668623; PMCID: PMC1080178.
Copy Download .nbib Format: NLM
Share it on

Plant Physiol. 1992 Jan;98(1):264-72. doi: 10.1104/pp.98.1.264.

Arabinogalactan-rich glycoproteins are localized on the cell surface and in intravacuolar multivesicular bodies.

Plant physiology

E M Herman, C J Lamb

Affiliations

  1. Plant Molecular Biology Laboratory, United States Department of Agriculture, Agricultural Research Service, Beltsville, Maryland 20705.

PMID: 16668623 PMCID: PMC1080178 DOI: 10.1104/pp.98.1.264

Abstract

We investigated the subcellular distribution of antigenic sites immunoreactive to the monoclonal antibody 16.4B4 (PM Norman, VPM Wingate, MS Fitter, CJ Lamb [1986] Planta 167: 452-459) in tobacco (Nicotiana tabacum) leaf cells. This antibody is directed against a glycan epitope in a family of plasma membrane arabinogalactan proteins of 135 to 180 kilodaltons, elaborated from a polypeptide of relative molecular mass 50 kilodaltons (PM Norman, P Kjellbom, DJ Bradley, MG Hahn, CJ Lamb [1990] Planta 181: 365-373). We demonstrated by immunogold electron microscopy that the epitope reactive with monoclonal antibody 16.4B4 is localized on the cell surface in the leaf parenchyma cell periplast. The 16.4B4 antigen is also localized in multivesicular invaginations of the plasma membrane also known as plasmalemmasomes, implying a biochemical and, hence, functional interrelationship between these structures. Monoclonal antibody 16.4B4 also labels intracellular multivesicular bodies that appear to represent internalized plasmalemmasomes. Antibody reactivity was also observed in partially degraded multivesicular bodies sequestered within the central vacuole. We propose that the subcellular distribution of the epitope reactive with monoclonal antibody 16.4B4 defines a plasmalemmasome (or multivesicular body-mediated) pathway for the internalization of the periplasmic matrix for vacuolar mediated disposal. The multivesicular bodies appear to be equivalent to the well-characterized endosomes and multivesicular bodies of animal cells involved in the internalization and lysosome-mediated degradation of extracellular materials.

References

  1. Plant Cell. 1989 Oct;1(10):1003-1009 - PubMed
  2. Science. 1979 Sep 14;205(4411):1144-7 - PubMed
  3. J Cell Biol. 1989 May;108(5):1967-77 - PubMed
  4. J Cell Biol. 1983 Jan;96(1):1-27 - PubMed
  5. Eur J Cell Biol. 1981 Jun;24(2):226-35 - PubMed
  6. Cytobios. 1973 Sep-Oct;8(29):57-62 - PubMed

Publication Types