Inpatient aggression in community hospitals.

Physical violence is a frequent occurrence in acute community psychiatry units worldwide. Violent acts by patients cause many direct injuries and significantly degrade quality of care. The most accurate tools for predicting near-term violence on acute units rely on current clinical features rather than demographic risk factors. The efficacy of risk assessment strategies to lower incidence of violence on acute units is unknown. A range of behavioral and psychopharmacologic treatments have been shown to reduce violence among psychiatric inpatients.

Supraorbital approach for repair of open anterior skull base fracture.

To the authors' knowledge, this is the first report of the use of anterior orbitotomy via the supraorbital eyelid crease to repair a dural tear caused by an orbital roof fracture. When transorbital penetrating injuries occur in children, they are commonly caused by accidental falls onto pointed objects. The authors report on their experience with a 7-year-old girl who fell onto a blunt metal rod hanger that penetrated her left eyelid, traversed superior to the eye globe, and penetrated the orbital roof at a depth of 3-4 cm, lacerating the dura mater and entering the cerebrum. An anterior transpalpebral transorbital approach was used to perform the microsurgical anterior skull base and dural repair. The authors advocate the application of this approach to orbital roof fractures because it provides excellent access to the orbital roof, eliminates the need for more invasive craniotomy, results in a small and well-hidden scar in the eye crease, and overall offers a shorter recovery time with less psychological stress to the patient.

Stereotactic radiosurgery for a cardiac sarcoma: a case report.

Pulmonary artery intimal sarcoma is an uncommon tumor with a poor prognosis. We report a case of a 75-year-old man with a pulmonary artery sarcoma, recurrent following surgical resection. To palliate symptoms of this recurrence, he underwent CyberKnife stereotactic radiosurgery with a clinical and radiographic response of his treated disease. No acute or sub-acute toxicity was seen until the patient's death due to metastatic disease 10 weeks following treatment. The feasibility and short-term safety of this technique are reviewed, with emphasis on the stereotactic planning considerations, such as mediastinal organ movement and radiation tolerance.

The contribution of amino acid region ASP695-TYR698 of factor V to procofactor activation and factor Va function.

There is strong evidence that a functionally important cluster of amino acids is located on the COOH-terminal portion of the heavy chain of factor Va, between amino acid residues 680 and 709. To ascertain the importance of this region for cofactor activity, we have synthesized five overlapping peptides representing this amino acid stretch (10 amino acids each, HC1-HC5) and tested them for inhibition of prothrombinase assembly and function. Two peptides, HC3 (spanning amino acid region 690-699) and HC4 (containing amino acid residues 695-704), were found to be potent inhibitors of prothrombinase activity with IC(50) values of approximately 12 and approximately 10 microm, respectively. The two peptides were unable to interfere with the binding of factor Va to active site fluorescently labeled Glu-Gly-Arg human factor Xa, and kinetic analyses showed that HC3 and HC4 are competitive inhibitors of prothrombinase with respect to prothrombin with K(i) values of approximately 6.3 and approximately 5.3 microm, respectively. These data suggest that the peptides inhibit prothrombinase because they interfere with the incorporation of prothrombin into prothrombinase. The shared amino acid motif between HC3 and HC4 is composed of Asp(695)-Tyr-Asp-Tyr-Gln(699) (DYDYQ). A pentapeptide with this sequence inhibited both prothrombinase function with an IC(50) of 1.6 microm (with a K(D) for prothrombin of 850 nm), and activation of factor V by thrombin. Peptides HC3, HC4, and DYDYQ were also found to interact with immobilized thrombin. A recombinant factor V molecule with the mutations Asp(695) --> Lys, Tyr(696) --> Phe, Asp(697) --> Lys, and Tyr(698) --> Phe (factor V(2K2F)) was partially resistant to activation by thrombin but could be readily activated by RVV-V activator (factor Va(RVV)(2K2F)) and factor Xa (factor Va(Xa)(2K2F)). Factor Va(RVV)(2K2F) and factor Va(Xa)(2K2F) had impaired cofactor activity within prothrombinase in a system using purified reagents. Our data demonstrate for the first time that amino acid sequence 695-698 of factor Va heavy chain is important for procofactor activation and is required for optimum prothrombinase function. These data provide functional evidence for an essential and productive contribution of factor Va to the activity of prothrombinase.