ABSTRACT
Most patients with acute pulmonary embolism (PE) are still treated as inpatients. This is a retrospective cohort study of patients with acute PE, diagnosed using V/P SPECT between 2007 and 2011. Patients were treated at home if they were hemodynamically stable, did not require oxygen or parenteral analgetics, had no contraindications to anticoagulant treatment and V/P SPECT showed an extension of the PE of less than 40%. The aim of the study was to evaluate the efficacy and safety of home treatment with our algorithm. During the study period 416 outpatients were diagnosed with acute symptomatic PE of whom in total 260 (62.5%) were discharged home from the emergency unit and another 47 (11%) within 24 h from admission. During 3 months follow-up one (0.3%) patient had a recurrent thrombotic event. Eleven (3.6%) patients had a major or clinically relevant bleed and the overall mortality was 2% (n = 6). There were no PE-related mortality. Home treatment should be considered and is safe in the majority of hemodynamically stable outpatients with small to medium size PE, quantified using V/P SPECT.
Subject(s)
Hemodynamics , Hemorrhage/chemically induced , Heparin, Low-Molecular-Weight , Pulmonary Embolism , Warfarin , Acute Disease , Adult , Ambulatory Care/methods , Ambulatory Care/statistics & numerical data , Anticoagulants/administration & dosage , Anticoagulants/adverse effects , Drug Monitoring , Female , Heparin, Low-Molecular-Weight/administration & dosage , Heparin, Low-Molecular-Weight/adverse effects , Home Care Services/statistics & numerical data , Humans , International Normalized Ratio , Male , Middle Aged , Outcome Assessment, Health Care , Pulmonary Embolism/diagnosis , Pulmonary Embolism/drug therapy , Pulmonary Embolism/mortality , Pulmonary Embolism/physiopathology , Retrospective Studies , Severity of Illness Index , Sweden/epidemiology , Tomography, Emission-Computed, Single-Photon/methods , Ventilation-Perfusion Ratio , Warfarin/administration & dosage , Warfarin/adverse effectsABSTRACT
A study undertaken in hard core pockets having C.P.R. >50% of urban slums to sensitize target couples for encouraging spacing methods and sterilizations showed 55.4% coverage of 1820 unprotected eligible couples. This coverage is attributed to involvement of Aganwadi workers, Mahila Mandals and home visits. The motivational strategies such as sensitization of Mahila Mondals, provision of MCH services and inter personal communications were found to be effective. The reasons for non-acceptance, such as desire to have male and female child in 17.8%, post insertion bleeding due to Cu-T in 13.9% and refusal by male partners in 13.36% were noted in eligible couples. These reasons could be removed by continued inter personal communications. Illiteracy rate of 76.30% in living children of sterilized women indicates need of implementing literacy programme.
Subject(s)
Health Education/statistics & numerical data , Health Knowledge, Attitudes, Practice , Poverty Areas , Sterilization, Reproductive/statistics & numerical data , Urban Population/statistics & numerical data , Adult , Female , Health Education/methods , Humans , India , Motivation , Socioeconomic FactorsABSTRACT
Proteinase 3 (PR3) is a neutrophil serine protease stored in the azurophil granules of the promyelocyte and its successors. The protease has been identified as an autoantigen for anti-neutrophil cytoplasmic autoantibodies (ANCA) occurring in patients with Wegener's granulomatosis. To characterize the biosynthesis and processing of human PR3 in a transgenic cellular model, cDNA encoding human pre-proproteinase 3 cloned from U-937 cells was transfected to the rat basophilic/mast cell line RBL-1 and the murine myeloblast-like cell line 32D c13. The stable expression of transgenic proteinase 3 was characterized by biosynthetic labeling, followed by immunoprecipitation, sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and fluorography. After pulse labeling for 30 min two proforms of PR3 (32 and 35 kDa), differing in carbohydrate content but with protein cores of identical size, were demonstrated. Chase of the label resulted in a processed 32-kDa form clearly visible in RBL, but only faintly in 32D cells, probably indicating delayed intracellular transfer in the latter cell line. Partial digestion with N-glycosidase F showed that both potential N-glycosylation sites on PR3 were occupied and conversion of the oligosaccharide side chains into complex forms was demonstrated by acquisition of resistance to endoglycosidase H. Translocation of PR3 to granules was shown by subcellular fractionation and immunocytochemistry. Enzymatic activation of PR3 was suggested by affinity to diisopropylfluorophosphate and removal of an amino-terminal propeptide. Cells transfected with PR3 showed positive immunofluorescence for ANCA-containing sera from patients with Wegener's granulomatosis. Our results show that human PR3 transfected to RBL or 32D cells is synthesized as a 29-kDa protein core glycosylated on two distinct sites. Oligosaccharide trimming and proteolytic processing occur and the protein is targeted for granular storage in a form antigenic for ANCA.
