Developing patient safety system using WHO tool in hospitals in Oman.

OBJECTIVE: Oman is progressively implementing the Patient Safety Friendly Hospital Initiative (PSFHI), a tool formulated by the World Health Organization (WHO) to achieve optimal patient safety in hospitals. This paper describes its implementation in selected government and private hospitals in Oman and analyses the performance of four hospitals whose implementations of PSFHI were assessed by WHO. DESIGN: The PSFHI initiative was launched in 11 hospitals in Oman during 2016. The enrolled hospitals implemented a 1-year plan composed of several steps such as formation of steering committees, working groups, full orientation about the standards, training of staff, documents development and community involvement. One year later, four hospitals which were the earliest to join the initiative were subjected to WHO assessment. SETTING: Secondary level government and private hospitals. INTERVENTION(S): The WHO-PSFHI standards. MAIN OUTCOME MEASURE: Hospitals' adherence to the standards. RESULTS: Three of the four hospitals (one government and two private) scored level two. One government hospital scored level three, earning it the distinction of being the first hospital in the Eastern Mediterranean Region to reach level three in the very first assessment. CONCLUSIONS: Implementation of PSFHI in selected hospitals of Oman had successful outcomes in improving patient's safety.

[Intracardiac thrombosis in Behçet disease: clinical presentation and outcome of three cases]. / Thrombose intracardiaque au cours de la maladie de Behçet : étude de trois observations.

BACKGROUND: Behçet's disease is recognized as a multisystem disorder that affects mainly young adults in Mediterranean, Middle Eastern, and Far Eastern countries. The diagnosis is very difficult because there is no laboratory test. Clinical features - such as orogenital aphtae, ocular and skin lesions, arthritis, and neurologic, gastrointestinal, vascular, and pulmonary symptoms - are helpful for diagnosis. Various cardiovascular manifestations, such as pancarditis, acute myocardial infarction, conduction system disturbances, and valvular diseases, have been reported but are rare. Intracardiac thrombus formation, as seen in our patients, is exceptional even among cardiovascular cases of Behçet's. OBSERVATIONS: We report three cases of intracardiac thrombosis among 204 patients followed for Behçet's disease within our unit over a period of 7 years. We report outcomes after corticosteroid, cyclophosphamide, and oral anticoagulant therapy. DISCUSSION: Cardiovascular involvement has been reported in 7 % to 29 % of patients with Behçet's syndrome. Intracardiac thrombosis is extremely rare and the right heart is the most common site of involvement. The first symptoms and signs of the disease frequently precede systemic organ manifestations. CONCLUSION: Diagnosis of Behçet's disease might be considered if a patient presents with a mass in the right-sided cardiac chambers, even in the absence of the characteristic clinical features of the condition. This is particularly applicable if the patient is a young male from the Mediterranean basin or the Middle East. We suggest that the treatment could include colchicine, anticoagulant therapy, and corticosteroids and discuss immunosuppressive therapy.

[Thrombosis of the inferior vena cava revealing primary antiphospholipid syndrome: a case report]. / Thrombose de la veine cave inférieure sur syndrome primaire des antiphospholipides : à propos d'un cas.

Thrombosis of the inferior vena cava is a rare clinical expression of primary antiphospholipid syndrome. This case clearly illustrates the clinical manifestations, work-up findings and management principles of thrombosis of the inferior vena cava in primary antiphospholipid syndrome before the stage of complication. The patient was a 24-year-old female with a history of recurrent deep venous thrombosis. She was admitted to the department of internal medicine for dyspnea and pain of the right hypochondria. Physical examination disclosed an edematous ascitic syndrome. The scanner coupled with Doppler ultrasonography showed thrombosis of the inferior vena cava. On these radiological findings, an immunological work-up was requested, which showed the presence of antiphospholipid antibodies.

Localized scleroderma: a series of 52 patients.

BACKGROUND: Localized scleroderma also called morphea is a skin disorder of undetermined cause. The widely recognized Mayo Clinic Classification identifies 5 main morphea types: plaque, generalized, bullous, linear and deep. Whether each of these distinct types has a particular clinical course or is associated with some patient-related features is still unclear. METHODS: We report here a retrospective series of patients with localized scleroderma with an attempt to identify features related to the type of lesion involved. The medical records of all patients with a diagnosis of localized scleroderma were reviewed by skilled practitioners. Lesions were classified according to the Mayo Clinic Classification. The relationship between each lesion type and various clinical features was tested by non-parametrical methods. RESULTS: The sample of 52 patients included 43 females and 9 males. Median age at onset was 30 y (range 1-76). Frequencies of patients according to morphea types were: plaque morphea 41 (78.8%) (including morphea en plaque 30 (57.7%) and atrophoderma of Pasini-Pierini 11 (21.1%)), linear scleroderma 14 (26.9%). Nine patients (17.3%) had both types of localized scleroderma. Median age at onset was lower in patients with linear scleroderma (8 y (range 3-44)) than in others (36 y (range 1-77)) (p=0.0003). Head involvement was more common in patients with linear scleroderma (37.5%) than in other subtypes (11.1%) (p=0.05). Atrophoderma of Pasini-Pierini was never located at the head. Systemic symptoms, antinuclear antibodies and the rheumatic factor were not associated with localized scleroderma types or subtypes. CONCLUSION: These results suggest that morphea types, in adults are not associated with distinct patient features except for age at disease onset (lower) and the localization on the head (more frequent), in patients with lesions of the linear type.

Neutrophil proteinase cathepsin G is proteolytically active on the human platelet glycoprotein Ib-IX receptor: characterization of the cleavage sites within the glycoprotein Ib alpha subunit.

The proteolytic activity of the neutrophil serine-proteinase cathepsin G (CG) on platelet adherence receptors, the glycoprotein (GP) Ib-IX complex and the integrin alpha IIb beta 3, has been investigated. In the range 50 to 200 nmol/l, CG is a potent platelet agonist which induces shape change, granule exocytosis and aggregation. Investigation of the proteolysis of the receptors' subunits during the course of platelet activation by CG was performed by immunoblot analysis of platelet proteins using a panel of specific antibodies. Exposure of platelets for 3 min at 37 degrees C to CG at a concentration that induces full cell activation resulted in an extensive cleavage of the N-terminal region of the extracellular domain of GPIb alpha, the largest (relative molecular mass, M(r), 143,000) of the three subunits constituting the GPIb-IX complex. In contrast, no detectable proteolytic modification of the two other subunits, GPIb beta and GPIX, was detected. Similarly, we observed that neither of the two subunits of the alpha IIb beta 3 receptor were proteolytically modified by CG. Cleavage of GPIb alpha by CG leaves a remnant of the polypeptide chain with M(r) approx. 106,000 in the plasma membrane, while releasing into the extracellular milieu the N-terminal domain with M(r) in the range 40,000 to 46,000. N-terminal sequencing of the CG-derived fragments of GPIb alpha indicated that the Leu275-Tyr276 peptide bond was the primary cleavage site for this proteinase. Proteolysis of GPIb alpha was already detectable at concentrations of CG as low as 25 nmol/l, while with 200 nmol/l the cleavage was detected as soon as 10 s after exposure of platelets to the proteinase. Comparison of the kinetics and concentration dependency for the proteolysis of GPIb alpha and for the activation of platelets by CG showed that cleavage of the GPIb-IX receptor is an early event that accompanies exocytosis and aggregation. Quantitative evaluation of the conversion of GPIb alpha into its membrane fragment indicated that, under optimal conditions, a maximum of approx. 50% of the total GPIb alpha can be affected by proteolysis. However, this proteolysis was > 90% complete when platelets were in the presence of the potent antagonist prostacyclin, suggesting that cellular redistribution of the GPIb-IX receptor may also occur during activation by CG. These results thus indicate that the very early phase of platelet activation by CG is accompanied by extensive modifications in the structure and expression of the GPIb-IX receptor, an effect that might be of functional significance for the interaction of platelets with the vessel wall.

Regulation of the structure and activity of platelet adhesion receptors by leukocyte proteinases.

Two major membrane receptors implicated in the adhesive properties of blood platelets are the GPIb-IX complex, a receptor for subendothelial von Willebrand factor, and the alpha IIb beta 3 integrin, the receptor for plasma fibrinogen. We have evaluated how the biological activities of these receptors can be potentially modulated through limited proteolysis when platelets are exposed to the serine-proteinases secreted by activated polymorphonuclear neutrophils, i.e., leukocyte elastase (EL) and cathepsin G (CG). CG can activate the alpha IIb beta 3 integrin through intracellular metabolic pathways, but has no direct proteolytic activity on the receptor subunits. By contrast, EL does not activate the platelet metabolism, but specifically cleaves a short peptide sequence within the alpha IIb subunit, and this cleavage occurs in parallel with an up-regulation of the activity of the fibrinogen receptor. On another hand, both EL and CG cleave the amino-terminal portion of the GPIb alpha subunit of the GPIb-IX receptor, eliminating the binding site for von Willebrand factor and diminishing the capacity of platelets to interact with this adhesion protein. Thus, neutrophil proteinases have the potential to regulate the activity of platelet adhesion receptors, and such experimental observations may prove to be relevant in vivo in various pathological conditions.