Cleft palate fistulas: a multivariate statistical analysis of prevalence, etiology, and surgical management

A retrospective, multivariate statistical analysis of 129 consecutive nonsyndromic patients undergoing cleft palate repair was performed to document the incidence of postoperative fistulas, to determine their cause, and to review methods of surgical management. Nasal-alveolar fistulas and/or anterior palatal fistulas that were intentionally not repaired were excluded from study. Cleft palate fistulas (CPFs) occurred in 30 of 129 patients (23 percent), although nearly a half were 1 to 2 mm in size. Extent of clefting, as estimated by the Veau classification, was significantly more severe in those patients who developed cleft palate fistula. Type of palate closure also influenced the frequency of cleft palate fistula. Forty-three percent of patients undergoing Wardill-type closures developed cleft palate fistula versus 10, 22, and 0 percent for Furlow, von Langenbeck, and Dorrance style closures, respectively. The fistula rate was similar in patients with (30 percent) and without (25 percent) intravelar veloplasty. Age at palate closure did not significantly affect the rate of fistulization; however, the surgeon performing the initial closure did not have an effect. Thirty-seven percent of patients developed recurrent cleft palate fistulas following initial fistula repair. Recurrence of cleft palate fistulas was not influenced by severity of cleft or type of original palate repair. Following end-stage management, a second cleft palate fistula recurrence occurred in 25 percent of patients. Continued open discussion of results of cleft palate repair is recommended.     

A Corynebacterium glutamicum gene encoding a two-domain protein similar to biotin carboxylases and biotin-carboxyl-carrier proteins

Following the analysis of transposon Tn5432-induced mutants of Corynebacterium glutamicum ATCC 13032, a gene encoding a protein with a biotin-binding motif was cloned. The DNA sequence of this gene revealed an open reading frame encoding 591 amino acids with a calculated mol. mass of 63.4 kDa. The protein is composed of two domains, an N-terminal biotin carboxylase and a C-terminal biotin-carboxyl-carrier protein, that are highly similar to corresponding subunits from prokaryotic and eukaryotic biotin enzymes. Over 70% identity was found to a protein from Mycobacterium leprae proposed to be part of an acyl-CoA carboxylase. Since it was not possible to inactivate the C. glutamicum gene, the gene most likely encodes a subunit of the essential acetyl-CoA carboxylase, which catalyzes the committed step in fatty acid synthesis. Received: 2 December 1995 / Accepted: 20 May 1996