Spontaneous Isolated Celiac Artery Dissection: A Case Report.

INTRODUCTION: Abdominal pain is a common chief complaint that can represent a wide breadth of diagnoses, ranging from benign to life-threatening. As our diagnostic tools become more sophisticated, we are able to better identify more causes of potentially life-threatening diseases. One such disease that is relatively unfamiliar to clinicians is spontaneous isolated celiac artery dissection (SICAD). CASE REPORT: We describe a case of a 46-year-old man who presented to our emergency department with a chief complaint of abdominal pain and was found to have a SICAD and was successfully treated with anticoagulation, antihypertensives, and observation. CONCLUSION: It is important for emergency physicians to keep this potentially life-threatening condition in mind and to know the appropriate first steps once identified.

Laforin, a dual specificity phosphatase involved in Lafora disease, is present mainly as monomeric form with full phosphatase activity.

Lafora Disease (LD) is a fatal neurodegenerative epileptic disorder that presents as a neurological deterioration with the accumulation of insoluble, intracellular, hyperphosphorylated carbohydrates called Lafora bodies (LBs). LD is caused by mutations in either the gene encoding laforin or malin. Laforin contains a dual specificity phosphatase domain and a carbohydrate-binding module, and is a member of the recently described family of glucan phosphatases. In the current study, we investigated the functional and physiological relevance of laforin dimerization. We purified recombinant human laforin and subjected the monomer and dimer fractions to denaturing gel electrophoresis, mass spectrometry, phosphatase assays, protein-protein interaction assays, and glucan binding assays. Our results demonstrate that laforin prevalently exists as a monomer with a small dimer fraction both in vitro and in vivo. Of mechanistic importance, laforin monomer and dimer possess equal phosphatase activity, and they both associate with malin and bind glucans to a similar extent. However, we found differences between the two states' ability to interact simultaneously with malin and carbohydrates. Furthermore, we tested other members of the glucan phosphatase family. Cumulatively, our data suggest that laforin monomer is the dominant form of the protein and that it contains phosphatase activity.