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L A Sznyter

Publications and source records attributed to L A Sznyter.

5 recordsLinked to original sources
PubMed2001

The incidence of carcinoma in cytologically benign thyroid cysts.

BACKGROUND: The management of cytologically benign thyroid cysts is controversial. Treatment options include observation, chemical sclerosis, and surgery. This study was undertaken to determine the incidence of carcinoma in cytologically benign thyroid cysts that recur after complete aspiration and to determine the indications for surgery in these patients. METHODS: The medical records of 1189 consecutive patients undergoing thyroid surgery between July 1995 and November 2000 were reviewed. In 34 patients the indication for surgery was a thyroid cyst with benign cytologic findings that refilled at least once after complete aspiration. These patients were selected for further study. RESULTS: The 26 women and 8 men had a median age of 42 years. Fine-needle aspiration cytology was consistent with a benign cyst in all these cases. Final pathologic findings revealed the nodule to be a papillary carcinoma in 4 patients (12%). In another 4 patients (12%) an incidental microscopic papillary carcinoma, separate from the cyst, was identified on final pathologic findings. In all 4 patients with papillary carcinoma the cyst size was greater than 3 cm (range, 3.4 to 5.0 cm). CONCLUSIONS: The incidence of malignancy in cytologically benign thyroid cysts that recur after aspiration is high enough to warrant surgical excision, especially if the cyst is greater than 3 cm in size.

Adult↗
PubMed1991

Characterization of the cloned BamHI restriction modification system: its nucleotide sequence, properties of the methylase, and expression in heterologous hosts.

The BamHI restriction modification system was previously cloned into E. coli and maintained with an extra copy of the methylase gene on a high copy vector (Brooks et al., (1989) Nucl. Acids Res. 17, 979-997). The nucleotide sequence of a 3014 bp region containing the endonuclease (R) and methylase (M) genes has now been determined. The sequence predicts a methylase protein of 423 amino acids, Mr 49,527, and an endonuclease protein of 213 amino acids, Mr 24,570. Between the two genes is a small open reading frame capable of encoding a 102 amino acid protein, Mr 13,351. The M. BamHI enzyme has been purified from a high expression clone, its amino terminal sequence determined, and the nature of its substrate modification studied. The BamHI methylase modifies the internal C within its recognition sequence at the N4 position. Comparisons of the deduced amino acid sequence of M. BamHI have been made with those available for other DNA methylases: among them, several contain five distinct regions, 12 to 22 amino acids in length, of pronounced sequence similarity. Finally, stability and expression of the BamHI system in both E. coli and B. subtilis have been studied. The results suggest R and M expression are carefully regulated in a 'natural' host like B. subtilis.

Amino Acid Sequence↗
PubMed1989

Cloning the BamHI restriction modification system.

BamHI, a Type II restriction modification system from Bacillus amyloliquefaciensH recognizes the sequence GGATCC. The methylase and endonuclease genes have been cloned into E. coli in separate steps; the clone is able to restrict unmodified phage. Although within the clone the methylase and endonuclease genes are present on the same pACYC184 vector, the system can be maintained in E. coli only with an additional copy of the methylase gene present on a separate vector. The initial selection for BamHI methylase activity also yielded a second BamHI methylase gene which is not homologous in DNA sequence and hybridizes to different genomic restriction fragments than does the endonuclease-linked methylase gene. Finally, the interaction of the BamHI system with the E. coli Dam and the Mcr A and B functions, have been studied and are reported here.

Amino Acid Sequence↗
PubMed1987

Nucleotide sequence of the DdeI restriction-modification system and characterization of the methylase protein.

The DdeI restriction-modification system was previously cloned and has been maintained in E. coli on two separate and compatible plasmids (1). The nucleotide sequence of the endonuclease and methylase genes has now been determined; it predicts proteins of 240 amino acids, Mr = 27,808, and 415 amino acids, Mr = 47,081, respectively. Inspection of the DNA sequence shows that the 3' end of the methylase gene had been deleted during cloning. The clone containing the complete methylase gene was made and compared to that containing the truncated gene; only clones containing the truncated form support the endonuclease gene in E. coli. Bal-31 deletion studies show that methylase expression in the Dde clones is also dependent upon orientation of the gene with respect to pBR322. The truncated and complete forms of the methylase protein were purified and compared; the truncated form appears to be more stable and active in vitro. Finally, comparison of the deduced amino acid sequence of M. DdeI with that of other known cytosine methylases shows significant regions of homology.

Amino Acid Sequence↗