Naslov
What do we know and what do we not know about antinociceptive action of botolinum toxin?

Autori
Lacković, Zdravko

Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni

Izvornik
39th International Danaube Symposium ; Journal of Neural Transmission 114 ; 2007 / Riederer, Peter ; Gerlach, Manfred - Beč : New York (NY) : Springer, 2007, CXI-CXI

Skup
39th International Danaube Symposium for Neurological Science and Continuing Education

Mjesto i datum
Würzburg, Njemačka, 02.06.2007. - 05.06.2007

Vrsta sudjelovanja
Pozvano predavanje

Vrsta recenzije
Nije recenziran

Ključne riječi
botulinum toxin; pain; nociception

Sažetak
RATIONALE: Active, proteolytic fragment of botulinum neurotoxin-A (BTX-A) enters cholinergic nerve endings via synaptic vesicle protein SV2. Proteolytic cleavage by BTX-A of nine amino acids from the C-terminal of SNAP-25 disables its function, preventing vesicle release and causing prolonged muscle weakness. This is the basis of botulism toxicity as well as usefulness of small doses of BTX-A in treating pathological consequences of hyperactivity of peripheral cholinergic nerve endings. OBJECTIVES: There is more and more evidence from human and animal experiments that BTX-A my have antinociceptive effect. Most hypotheses assume that BTX-A inhibits not only the exocytosis of acetylcholine but also of neurotransmitters like neuropeptides from nociceptive nerve endings. MATERIALS AND METHODS: Starting from on literature review and our own results we analyze whether mentioned hypothesis can explain experimental and clinical data collected up to now. RESULTS Why antinociceptive effect BTX-A lasts for weeks in experimental animals and for months in human ? Why BTX-A relieves inflammatory and neuropathic pain but not acute nociceptive pain? Why BTX-A has reduces formalin but not in carrageenan induced inflammation. How is possible that in some experimental models BTX-A reduces pain when injected on contralateral site? CONCLUSION: Those are some of the questions that can not be explained by the hypothesis that antinociceptive activity of BTX-A is mediated solely by cleavage of SNAP25 at peripheral ending of sensory nerves. Even more the assumption that cleavage of SNAP25 is the only molecular action of BTX-A can explain only some of the questions listed here. Supported by Croatian Ministry of Education, Science and Sport, and Deutscher Akademischer Austausch Dienst.

Izvorni jezik
Engleski

POVEZANOST RADA