Treatment efficacy of eyelid twitch muscle transposition surgery in senile entropion / 国际眼科杂志(Guoji Yanke Zazhi)

AlM:To explore treatment efficacy of the lower eyelid twitch muscle transposition surgery in senile entropion.METHODS:Fifty cases (86 eyes) of senile lower eyelid entropion patients underwent lower eyelid twitch muscle transposition correction surgery as the experimental group, and the other 42 cases (68 eyes) of senile lower eyelid entropion patients received orbicularis muscle shortening correction as controls group. The correction rate, double eyelid symmetry and overcorrection rate of patients were observed one week after surgery. The patients were followed up for 6~12mo to be observed the long-term recurrence rate, double eyelid symmetry and overcorrection rate.RESULTS: One week after operation, eyelid symmetry, overcorrection rate of experimental group and control group had significant difference (P<0. 05); After followed up for 6 ~12mo, eyelid symmetry, overcorrection rate of experimental group and control group had significant difference (P<0. 05). CONCLUSlON: Folding and orbicularis muscle shortening treatment of senile entropion was compared with the lower eyelid twitch muscle transposition surgery treatment of senile entropion, We can find that clinical results in double eyelid surgery symmetry and overcorrection rate are of obvious advantage.

The importance of Loop 7 for the activity of calcineurin.

Calcineurin (CN) is a heterodimer composed of a catalytic subunit (CNA) and a regulatory subunit (CNB). Loop 7 lies within the CNA catalytic domain. To investigate the role of Loop 7 in enzyme activity, we systematically examined all its residues by site-directed deletion mutation. Our results show that the Loop 7 residues are important for enzyme activity. Besides deleting residues V314, Y315 or N316, enzyme activity also increased dramatically when residues D313 or K318 were deleted. In contrast, almost all activity was lost when L312 or N317 were deleted. Ni2+ and Mn2+ were effective activators for all active mutants. However, whereas the wild-type enzyme was more efficiently activated by Ni2+ than by Mn2+ with 32P-labeled R(II) peptide as substrate, the reverse was true in all the mutants. We also found that the effect of Loop 7 on enzyme activity was substrate dependent, and involved interactions between Loop 7 residues and the unresolved part of the CN crystal structure near the auto-inhibitory domain and catalytic site.