Computed tomographic features of pneumothorax secondary to a bronchopleural fistula in two dogs.

A bronchopleural fistula (BPF) can lead to continuous pneumothorax and is rarely reported clinically in dogs. This report describes computed tomographic (CT) findings in two dogs with BPFs and subsequent continuous pneumothoraces that necessitated thoracotomy. Both dogs had a peripheral BPF in the right caudal lung lobe.

Osteomyelitis of the coxofemoral joint due to Mycobacterium species in a feline renal transplant recipient.

A 4-year-old castrated male Russian Blue cat was evaluated for acute right hind limb lameness 18 months after receiving a renal transplant. Radiographs showed a subluxated right femoral head and lysis of the acetabulum and femoral neck. A femoral head and neck ostectomy was performed on the right coxofemoral joint.

Fox-2 splicing factor binds to a conserved intron motif to promote inclusion of protein 4.1R alternative exon 16.

Activation of protein 4.1R exon 16 (E16) inclusion during erythropoiesis represents a physiologically important splicing switch that increases 4.1R affinity for spectrin and actin.

Nuclear substructure reorganization during late-stage erythropoiesis is selective and does not involve caspase cleavage of major nuclear substructural proteins.

Enucleation, a rare feature of mammalian differentiation, occurs in 3 cell types: erythroblasts, lens epithelium, and keratinocytes. Previous investigations suggest that caspase activation functions in lens epithelial and keratinocyte enucleation, as well as in early erythropoiesis encompassing erythroid burst-forming unit (BFU-E) differentiation to proerythroblast. To determine whether caspase activation contributes to later erythropoiesis and whether nuclear substructures other than chromatin reorganize, we analyzed distributions of nuclear subcompartment proteins and assayed for caspase-induced cleavage of subcompartmental target proteins in mouse erythroblasts.

Mechanism of protein sorting during erythroblast enucleation: role of cytoskeletal connectivity.

During erythroblast enucleation, nuclei surrounded by plasma membrane separate from erythroblast cytoplasm. A key aspect of this process is sorting of erythroblast plasma membrane components to reticulocytes and expelled nuclei. Although it is known that cytoskeletal elements actin and spectrin partition to reticulocytes, little is understood about molecular mechanisms governing plasma membrane protein sorting.

Decrease in hnRNP A/B expression during erythropoiesis mediates a pre-mRNA splicing switch.

A physiologically important alternative pre-mRNA splicing switch, involving activation of protein 4.1R exon 16 (E16) splicing, is required for the establishment of proper mechanical integrity of the erythrocyte membrane during erythropoiesis. Here we identify a conserved exonic splicing silencer element (CE(16)) in E16 that interacts with hnRNP A/B proteins and plays a role in repression of E16 splicing during early erythropoiesis.