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PubMed · 9715143

The recurrent appendix: comment.

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E Penington. 1998. The recurrent appendix: comment.. https://doi.org/10.1111/j.1445-2197.1998.tb02113.x

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Characterization of a novel transcript of prostaglandin endoperoxide H synthase 1 with a tissue-specific profile of expression.

The enzyme prostaglandin endoperoxide H synthase (PGHS) has a pivotal role in the prostanoid biosynthetic pathway because it catalyses the formation of prostaglandin H(2) (PGH(2)), the common precursor of prostanoids. Two PGHS isoforms have been reported, PGHS-1 and PGHS-2, which have 61% identity (at the amino acid level) and 73% similarity (at the nucleotide level) between the two human enzymes. Transcription of the PGHS-1 gene leads to the formation of two transcripts (2.8 and 5.1 kb); two transcripts of 2.8 and 4.5 kb are produced from the PGHS-2 gene. By Northern blot analysis with the entire coding region of human PGHS-1, 2.8 and 5.1 kb transcripts as well as a novel 4.5 kb transcript were detected in the human megakaryoblastic cell line MEG-01. We designed a strategy to characterize the 4.5 kb PGHS transcript. Probes specific for each PGHS-1 and PGHS-2 were designed on the basis of the 3' untranslated region (3' UTR), where no similarity is present. The 4.5 kb transcript was detected only with the PGHS-1-specific 3' UTR probes and not with the PGHS-2-specific 3' UTR probe. To investigate the origin of the 4.5 kb PGHS-1 transcript, the remaining 947 bp of the 5.1 kb PGHS-1 transcript was generated by 3' rapid amplification of cDNA ends (3' RACE) and sequenced. A non-canonical polyadenylation signal (AAGAAA) located upstream of a potential cleavage site (CA) was found and could generate the 4.5 kb PGHS-1 transcript. Analysis of the sequence also produced several possible G/U-rich elements downstream of the potential cleavage site. An RNA dot-blot with 50 different human tissues was probed with the 4.5 and 5.1 kb PGHS-1-specific probes. A signal for the 4.5 kb PGHS-1 transcript was detected in the bladder and appendix. Signals of lower intensity were detected in the colon, bone marrow, small intestine, uterus, prostate, peripheral leucocyte, lymph node and stomach. In conclusion, our results suggest that the cell line MEG-01, the bladder and the appendix contain a new PGHS-1 transcript of 4.5 kb that can be produced from the PGHS-1 gene and we provide a better strategy for distinguishing PGHS-1 transcripts from PGHS-2.

Appendix

Y-appendicoplasty: a technique to minimize stomal complications in antegrade continence enema.

PURPOSE: The antegrade continence enema (ACE) is an effective method of treatment of fecal incontinence and constipation. However, the original procedure described is not easy to perform and is associated with a high complication rate, especially stomal stenosis-necrosis (55%). Even with introduction of orthotopic appendicostomy, composite series still report an incidence of 30% with stomal problems. The authors report a virtually complication-free simple modification, the Y-appendicoplasty. METHODS: The base of the appendix is imbricated into cecum by 2 successive rows of interrupted seromuscular stitches. A small Y-shaped incision is made on the abdominal wall at McBurney's point, and 3 triangular skin flaps are raised. The appendix is brought out of the skin incision. The tip is excised, and 3 vertical cuts are made 120 degrees apart. The 3 appendiceal flaps thus created are interdigitated with the skin flaps using interrupted sutures. RESULTS: Twelve children underwent Y-appendicoplasty and orthotopic appendicostomy. Mean operating time was 1 hour. None experienced stomal complications that required intervention. Control of fecal continence with ACE ranged from excellent to good. CONCLUSION: Y-appendicoplasty and orthotopic appendicostomy minimizes complications for ACE and is easy to perform.

Appendix