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1.
J Clin Pharm Ther ; 43(6): 910-913, 2018 Dec.
Article in English | MEDLINE | ID: mdl-29956355

ABSTRACT

WHAT IS KNOWN AND OBJECTIVE: Candida catenulata is a fungus commonly found in Australian cheeses. C. catenulata has been identified as the causative pathogen for one report of onychomycosis and one report of candidaemia. CASE DESCRIPTION: A 37-year-old male underwent surgery for an incarcerated umbilical hernia repair and bowel obstruction and presented with severe abdominal pain and ascitic fluid draining from the surgical site. C. catenulata was isolated in blood cultures. The patient was treated with antifungal therapy for approximately 6 weeks. WHAT IS NEW AND CONCLUSION: To our knowledge, this is the first case describing successful treatment of possible fungal endocarditis caused by C. catenulata.


Subject(s)
Antifungal Agents/administration & dosage , Candidemia/drug therapy , Endocarditis/drug therapy , Fluconazole/administration & dosage , Abdominal Pain/etiology , Administration, Oral , Adult , Candida/isolation & purification , Candidemia/diagnosis , Candidemia/microbiology , Endocarditis/diagnosis , Endocarditis/microbiology , Fluconazole/therapeutic use , Hernia, Umbilical/surgery , Humans , Intestinal Obstruction/surgery , Liver Cirrhosis/pathology , Male , Treatment Outcome
2.
Cell Mol Life Sci ; 61(15): 1926-34, 2004 Aug.
Article in English | MEDLINE | ID: mdl-15289934

ABSTRACT

The tumor suppressor function of PTEN is attributed to its phospholipid phosphatase activity that dephosphorylates the plasma membrane phosphatidylinositol-(3,4,5)-triphosphate [PtdIns(3,4,5)P3]. Implicit in this notion is that PTEN needs to be targeted to the plasma membrane to dephosphorylate PtdIns(3,4,5)P3. However, the recruitment of PTEN to the plasma membrane is not fully understood. Here, we demonstrate PTEN accumulation in the detergent-insoluble fraction of neuronal cells in response to treatment by the proteasome inhibitor lactacystin. First, lactacystin induces apoptosis and the activation of caspase-3 in cultured cortical neurons. Second, PTEN undergoes proteolysis to form a truncated 50-kDa form that lacks parts of its C-terminal tail. Third, the truncated PTEN is stably associated with the detergent-insoluble fraction in which the plasma membrane marker protein flotillin-1 resides. Taken together, our results suggest that truncation and accumulation of PTEN to the detergent-insoluble membrane fraction are two events associated with the apoptotic signals of the proteasome inhibitor in cortical neurons.


Subject(s)
Acetylcysteine/analogs & derivatives , Acetylcysteine/metabolism , Apoptosis/physiology , Neurons/metabolism , Protein Tyrosine Phosphatases/metabolism , Tumor Suppressor Proteins/metabolism , Acetylcysteine/pharmacology , Animals , Apoptosis/drug effects , Cell Membrane/metabolism , Cerebral Cortex/metabolism , Cysteine Endopeptidases , Cysteine Proteinase Inhibitors/pharmacology , Mice , Multienzyme Complexes/antagonists & inhibitors , PTEN Phosphohydrolase , Proteasome Endopeptidase Complex
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