Oxidized galectin-1 advances the functional recovery after peripheral nerve injury.
Oxidized galectin-1 has been shown to promote axonal regeneration from transected-nerve sites in an in vitro dorsal root ganglion (DRG) explant model as well as in in vivo peripheral nerve axotomy models. The present study provides evidence that oxidized galectin-1 advances the restoration of nerve function after peripheral nerve injury. The sciatic nerve of adult rats was transected and the distal nerve was frozen after being sutured into a proximal site with four epineurial stitches. An osmotic pump delivered oxidized galectin-1 peripherally to the surgical site. Functional recovery was assessed by measurement of the degree of toe spread of the hind paw for 3 months after the sciatic nerve lesion. The recovery curves of toe spread in the test group showed a statistically significant improvement of functional recovery after day 21 by the application of oxidized recombinant human galectin-1 (rhGAL-1/Ox) compared to the control group. This functional recovery was supported by histological analysis performed by light microscopic examination. The regenerating myelinated fibers at the site 21 mm distal to the nerve-transected site were quantitatively examined at 100 days after the operation. The frequency distribution of myelinated fiber diameters showed that exogenous rhGAL-1/Ox increased the number and diameter of regenerating myelinated fibers; the number of medium-sized (6-11 microm in diameter) fibers increased significantly (P<0.05). These results indicate that oxidized galectin-1 promotes the restoration of nerve function after peripheral nerve injury. Thus, rhGAL-1/Ox may be a factor for functional restoration of injured peripheral nerves.
Kadoya
Toshihiko
T
CMC R&D Laboratories, Pharmaceutical Division, Kirin Brewery Co. Ltd., Hagiwara, Takasaki, Gunma 370-0013, Japan. tkadoya@kirin.co.jp
Oyanagi
Kiyomitsu
K
Kawakami
Emiko
E
Hasegawa
Mitsuhiro
M
Inagaki
Yoshimasa
Y
Sohma
Yoshiaki
Y
Horie
Hidenori
H
D000818:Animals; D004195:Disease Models, Animal; D037483:Galectin 1 / Q000235:genetics / Q000378:metabolism / Q000494:pharmacology*; D008297:Male; D009413:Nerve Fibers, Myelinated / Q000187:drug effects / Q000378:metabolism; D009414:Nerve Growth Factors / Q000235:genetics / Q000378:metabolism / Q000494:pharmacology; D009416:Nerve Regeneration / Q000187:drug effects* / Q000502:physiology; D010084:Oxidation-Reduction; D010243:Paralysis / Q000188:drug therapy / Q000209:etiology / Q000503:physiopathology; D059348:Peripheral Nerve Injuries; D010525:Peripheral Nerves / Q000187:drug effects* / Q000378:metabolism; D051381:Rats; D017207:Rats, Sprague-Dawley; D011993:Recombinant Fusion Proteins / Q000494:pharmacology; D020127:Recovery of Function / Q000187:drug effects* / Q000502:physiology; D012584:Sciatic Nerve / Q000187:drug effects* / Q000378:metabolism; D020426:Sciatic Neuropathy / Q000188:drug therapy* / Q000378:metabolism / Q000503:physiopathology; D014034:Toes / Q000294:innervation / Q000503:physiopathology; D016896:Treatment Outcome
D037483:Galectin 1; C445499:LGALS1 protein, human; D009414:Nerve Growth Factors; D011993:Recombinant Fusion Proteins