Endosome-lysosomes, ubiquitin and neurodegeneration

R. John Mayer, Carron Tipler, Jane Arnold, L. László, Abdulaziz Al-Khedhairy, James Lowe, Michael Landon

Research output: Contribution to journalArticle

34 Citations (Scopus)

Abstract

Before the advent of ubiquitin immunocytochemistry and immunogold electron microscopy, there was no known intracellular molecular commonality between neurodegenerative diseases. The application of antibodies which primarily detect ubiquitin protein conjugates has shown that all of the human and animal idiopathic and transmissible chronic neurodegenerative diseases, (including Alzheimer's disease (AD), Lewy body disease (LBD), amyotrophic lateral sclerosis (ALS), Creutzfeldt-Jakob disease (CJD) and scrapie) are related by some form of intraneuronal inclusion which contains ubiquitin protein conjugates. In addition, disorders such as Alzheimer's disease, CJD and sheep scrapie, are characterised by deposits of amyloid, arising through incomplete breakdown of membrane proteins which may be associated with cytoskeletal reorganisation. Although our knowledge about these diseases is increasing, they remain largely untreatable. Recently, attention has focussed on the mechanisms of production of different types of amyloid and the likely involvement within cells of the endosome-lysosome system, organelles which are immunopositive for ubiquitin protein conjugates. These organelles may be 'bioreactor' sites for the unfolding and partial degradation of membrane proteins to generate the amyloid materials or their precursors which subsequently become expelled from the cell, or are released from dead cells, and accumulate as pathological entities. Such common features of the disease processes give new direction to therapeutic intervention.

Original languageEnglish
Pages (from-to)261-269
Number of pages9
JournalAdvances in Experimental Medicine and Biology
Volume389
Publication statusPublished - 1996

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Endosomes
Ubiquitin
Lysosomes
Scrapie
Creutzfeldt-Jakob Syndrome
Amyloid
Neurodegenerative Diseases
Organelles
Alzheimer Disease
Membrane Proteins
Neurodegenerative diseases
Lewy Body Disease
Proteins
Amyloid Plaques
Amyotrophic Lateral Sclerosis
Bioreactors
Sheep
Electron Microscopy
Chronic Disease
Immunohistochemistry

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

Cite this

Mayer, R. J., Tipler, C., Arnold, J., László, L., Al-Khedhairy, A., Lowe, J., & Landon, M. (1996). Endosome-lysosomes, ubiquitin and neurodegeneration. Advances in Experimental Medicine and Biology, 389, 261-269.

Endosome-lysosomes, ubiquitin and neurodegeneration. / Mayer, R. John; Tipler, Carron; Arnold, Jane; László, L.; Al-Khedhairy, Abdulaziz; Lowe, James; Landon, Michael.

In: Advances in Experimental Medicine and Biology, Vol. 389, 1996, p. 261-269.

Research output: Contribution to journalArticle

Mayer, RJ, Tipler, C, Arnold, J, László, L, Al-Khedhairy, A, Lowe, J & Landon, M 1996, 'Endosome-lysosomes, ubiquitin and neurodegeneration', Advances in Experimental Medicine and Biology, vol. 389, pp. 261-269.
Mayer RJ, Tipler C, Arnold J, László L, Al-Khedhairy A, Lowe J et al. Endosome-lysosomes, ubiquitin and neurodegeneration. Advances in Experimental Medicine and Biology. 1996;389:261-269.
Mayer, R. John ; Tipler, Carron ; Arnold, Jane ; László, L. ; Al-Khedhairy, Abdulaziz ; Lowe, James ; Landon, Michael. / Endosome-lysosomes, ubiquitin and neurodegeneration. In: Advances in Experimental Medicine and Biology. 1996 ; Vol. 389. pp. 261-269.
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