Motor nerve sprouting and neuromuscular junction remodeling of orbicularis oculi muscles from patients with blepharospasm treated with botulinum neurotoxin type A

Toxicon ◽  
2018 ◽  
Vol 156 ◽  
pp. S40
Author(s):  
Brigitte Girard ◽  
Aurélie Couesnon ◽  
Michel-Robert Popoff ◽  
Jordi Molgó
2013 ◽  
Vol 48 (1) ◽  
pp. 120-127 ◽  
Author(s):  
Cesare Colasante ◽  
Ornella Rossetto ◽  
Laura Morbiato ◽  
Marco Pirazzini ◽  
Jordi Molgó ◽  
...  

2015 ◽  
Vol 7 (2) ◽  
Author(s):  
Marco Orsini ◽  
Marco Antonio Araujo Leite ◽  
Tae Mo Chung ◽  
Wladimir Bocca ◽  
Jano Alves De Souza ◽  
...  

This paper reviews the current and most neurological (central nervous system, CNS) uses of the botulinum neurotoxin type A. The effect of these toxins at neuromuscular junction lends themselves to neurological diseases of muscle overactivity, particularly abnormalities of muscle control. There are seven serotypes of the toxin, each with a specific activity at the molecular level. Currently, serotypes A (in two preparations) and B are available for clinical purpose, and they have proved to be safe and effective for the treatment of dystonia, spasticity, headache, and other CNS disorders in which muscle hyperactivity gives rise to symptoms. Although initially thought to inhibit acetylcholine release only at the neuromuscular junction, botulinum toxins are now recognized to inhibit acetylcholine release at autonomic cholinergic nerve terminals, as well as peripheral release of neuro-transmitters involved in pain regulation. Its effects are transient and nondestructive, and largely limited to the area in which it is administered. These effects are also graded according to the dose, allowing individualized treatment of patients and disorders. It may also prove to be useful in the control of autonomic dysfunction and sialorrhea. In over 20 years of use in humans, botulinum toxin has accumulated a considerable safety record, and in many cases represents relief for thousands of patients unaided by other therapy.


Toxicon ◽  
2021 ◽  
Vol 190 ◽  
pp. S70
Author(s):  
Sudhakar R. Subramaniam ◽  
Greg Nicholson ◽  
Brian B. Cai ◽  
Amy D. Brideau-Andersen ◽  
Ron S. Broide

Toxicon ◽  
2021 ◽  
Vol 190 ◽  
pp. S63
Author(s):  
Susana Rosa ◽  
Bruno Guimarães ◽  
Joana Martins ◽  
José Luís Mesquita ◽  
Margarida Freitas ◽  
...  

2000 ◽  
Vol 68 (5) ◽  
pp. 2587-2593 ◽  
Author(s):  
John A. Chaddock ◽  
John R. Purkiss ◽  
Lorna M. Friis ◽  
Janice D. Broadbridge ◽  
Michael J. Duggan ◽  
...  

ABSTRACT Clostridial neurotoxins potently and specifically inhibit neurotransmitter release in defined cell types by a mechanism that involves cleavage of specific components of the vesicle docking/fusion complex, the SNARE complex. A derivative of the type A neurotoxin fromClostridium botulinum (termed LHN/A) that retains catalytic activity can be prepared by proteolysis. The LHN/A, however, lacks the putative native binding domain (HC) of the neurotoxin and is thus unable to bind to neurons and effect inhibition of neurotransmitter release. Here we report the chemical conjugation of LHN/A to an alternative cell-binding ligand, wheat germ agglutinin (WGA). When applied to a variety of cell lines, including those that are ordinarily resistant to the effects of neurotoxin, WGA-LHN/A conjugate potently inhibits secretory responses in those cells. Inhibition of release is demonstrated to be ligand mediated and dose dependent and to occur via a mechanism involving endopeptidase-dependent cleavage of the natural botulinum neurotoxin type A substrate. These data confirm that the function of the HC domain of C. botulinumneurotoxin type A is limited to binding to cell surface moieties. The data also demonstrate that the endopeptidase and translocation functions of the neurotoxin are effective in a range of cell types, including those of nonneuronal origin. These observations lead to the conclusion that a clostridial endopeptidase conjugate that can be used to investigate SNARE-mediated processes in a variety of cells has been successfully generated.


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