Fixation strength of rotator cuff repairs with suture anchors and the transosseous suture technique.

The strength of classic transosseous suture repair of rotator cuff tendons was compared with similar repairs with four "third-generation" suture anchors. Results demonstrate the repair construct selected had a significant influence on failure at ultimate load (p = 0.005). Among the anchors tested the Statak design was significantly stronger than the other three. Furthermore Statak, Harpoon, and Superanchor designs were all significantly stronger than the Revo screw. No significant difference was seen between the strength of repairs performed with the Statak, the Harpoon, or the Superanchor compared with the transosseous suture technique. The transosseous suture technique was significantly stronger than repairs performed with the Revo. We conclude suture anchor design has evolved to a point where initial fixation of torn rotator cuff tendons is equivalent to more traditional techniques using only sutures.

Delayed hypersensitivity reaction of the knee after injection of arthroscopy portals with bupivacaine (marcaine)

The number of arthroscopic procedures performed annually for the management of intraarticular injuries has grown at an exponential rate. Whether done with the patient under general anesthesia or local anesthesia supplemented with intravenous sedation, it is common practice to postoperatively inject each portal as well as the joint with a local anesthetic to provide pain relief in the transition to the recovery room and discharge after outpatient surgery. To our knowledge, no previous reports of localized urticaria and delayed hypersensitivity reaction have been reported in the postarthroscopy setting. We are reporting a case of delayed hypersensitivity reaction and urticaria of the knee that presented after bupivacaine (Marcaine) injection of arthroscopic portals after routine meniscectomy.

Detection of platelet-activating factor during traumatic shock.

The purpose of this study was to determine if platelet-activating factor (PAF) is formed in the peritoneal fluid of rats following traumatic shock. Anesthetized rats subjected to Noble-Collip drum trauma developed a lethal shock state characterized by a mean survival time of 80 +/- 16 min and a final mean arterial blood pressure of 54 +/- 7 mm Hg compared with 117 +/- 14 mm Hg in sham-shock control rats. Peritoneal fluid from traumatized and PAF-infused rats analyzed by high performance liquid chromatography (HPLC) contained a phospholipid which had a similar retention time as authentic PAF, but was absent in sham shock rats. Furthermore, aliquots of this chromatographic peak aggregated washed rabbit platelets, and the aggregation was blocked by a specific PAF receptor antagonist, CV-6209. Moreover, extraction of peritoneal fluid from traumatized rats aggregated washed rabbit platelets and this activity increased nearly four-fold in traumatized rats compared to sham shock rats. These findings are consistent with the formation of PAF in traumatic shock, and along with previous data of PAF antagonists ameliorating traumatic shock, support a role of platelet-activating factor in the pathogenesis of traumatic shock.

Significance of production of peptide leukotrienes in murine traumatic shock.

We studied the formation of a leukotriene metabolite in plasma and bile during traumatic shock. Anesthetized rats subjected to Noble-Collip drum trauma developed a lethal shock state characterized by a survival time of 1.9 +/- 0.3 h, a 4.5-fold increase in plasma cathepsin D activity, and a reduction in mean arterial blood pressure to 45 +/- 2 mmHg compared with 108 +/- 5 mmHg in sham-shock controls. Plasma and bile samples were analyzed by reverse-phase high-pressure liquid chromatography (HPLC) for peptide leukotrienes (e.g., LTC4, LTD4, and LTE4), and their retention times were confirmed by co-elution with radioactive standards, radioimmunoassay (RIA), and UV spectrophotometry. No leukotrienes or metabolites were found in plasma. The major peptide leukotriene from bile was eluted between LTC4 and LTD4 and corresponds to a metabolite of LTE4, N-acetyl-LTE4, which is also produced during endotoxin shock. The metabolite increased nearly sevenfold in traumatic shock compared with sham trauma. The identity of the metabolite was confirmed by UV scan, which revealed a spectrum consistent with a peptide leukotriene and similar to that of previously reported spectra for N-acetyl-LTE4. In conclusion, peptide leukotrienes are rapidly cleared from the blood and appear in the bile as N-acetyl-LTE4, a metabolite of the peptide leukotrienes. These findings support a role of the peptide leukotrienes in the pathogenesis of traumatic shock.

Purification of biotinidase from human plasma and its activity on biotinyl peptides.

Biotinidase catalyzes the hydrolysis of N epsilon-biotinyllysine (biocytin) to form biotin and free lysine. The enzyme has been purified 4800-fold from outdated human plasma and was determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis to have a molecular weight of (76 +/- 2) X 10(3). The same molecular weight was found by molecular sieve chromatography under nondenaturing conditions, indicating biotinidase is a monomer. This value is in contrast to a molecular weight of 115 000 determined by Pispa [Pispa, J. (1965) Ann. Med. Exp. Biol. Fenn., Suppl. 5, 5-39] with an impure biotinidase. The Km for biocytin was 6.2 X 10(-6) M, and biotinidase was found to be sensitive to phenylmethanesulfonamide and iodoacetamide in agreement with earlier studies by Knappe and co-workers [Knappe, J., Brümmer, W., & Bierderbick, K. (1963) Biochem. Z. 338, 599-613], who suggested that serine hydroxyl groups and sulfhydryl groups are essential for enzymatic activity. The specificity of biotinidase was examined by using synthetic and natural biotinyl peptides isolated by specific proteolytic cleavage of the biotinyl subunit of transcarboxylase. It was found that the rate of hydrolysis of biocytin was 83-fold higher than that found for biotin-containing peptides 5-13 residues in length. Removal of methionine from either side of the conserved region around the biocytin did not greatly alter the rate of cleavage. Increasing the peptide to 65-123 residues in length decreased the rate 1200-fold compared to that of biocytin.(ABSTRACT TRUNCATED AT 250 WORDS)