[Omentopexy in Peritoneal Catheter Malfunction].

Among the various problems associated with peritoneal dialysis, besides infectious causes, the risk of catheter malfunction plays a significant role in conditioning the continuation of the method, accounting for up to 15-18% of the total causes of dialysis drop-out. When non-invasive maneuvers, such as the use of laxatives to stimulate intestinal peristalsis or heparin and/or urokinase have no effect, videolaparoscopy is the only method that directly detects the precise causes of peritoneal catheter malfunction. Those found are, with decreasing frequency, the winding of the catheter between the intestinal loops and the omentum (wrapping), the dislocation of the catheter, the combination of wrapping and dislocation, the occlusion of the catheter by a fibrin plug, the adhesions between the intestine and abdominal wall, the occlusion of the catheter by epiploic appendages or adnexal tissue and, occasionally, the presence of a new formation of endoperitoneal tissue enveloping and obstructing the peritoneal catheter. We report the case of a young patient of African ethnicity who, only five days after catheter placement, experienced malfunction. A videolaparoscopy revealed wrapping with invagination of omental tissue inside the catheter. After omental debridement, a proper peritoneal cavity washout with heparin was resumed, and after a couple of weeks, APD was initiated. About a month later, a new malfunction without signs of coprostasis or problems with the abdominal radiogram was observed. However, a subsequent catheterography confirmed the blockage of drainage. This was followed by another catheterography and omentopexy, with definitive solution of the Tenckhoff malfunction.

[A case of AL amyloidosis with fulminant evolution].

Amyloidosis represents a heterogeneous group of pathologies characterized by the deposit, in the form of fibrils, in the various organs and tissues of the body, of abnormal proteins; the deposits made up of these fibrils are called amyloid or amyloid substance. AL amyloidosis, also called "light chains", is a primary form characterized by deposits of light chains of monoclonal immunoglobulins, proteins that are produced by the bone marrow with the aim of protecting the body from pathological processes; for unknown reasons, these immunoglobulins, once fulfilled their function, do not dissolve but, on the contrary, they transform into amyloid fibrils and accumulate progressively, transported by the bloodstream, in the various organs and tissues. Below we report the case of a 77-year-old Caucasian male patient hospitalized at our Operative Unit for nephrotic syndrome and creatinine increase in the last couple of months, compared to previous normal tests. The patient underwent a renal biopsy and a bone marrow smear with evidence of AL amyloidosis (or primary amyloidosis) and of the presence, at serum immunofixation, of small IgG multiple myeloma k. Treated with bortezomib (1 mg/m 2 ) and soldesam (10 mg) first and with lenalidomid after, the patient had a clinical course burdened by symptomatic hypotension, due to severe dysautonomia. He had to start replacement treatment with haemodiafiltration for terminal kidney disease two months after the onset of illness. He died 4 months after the first hospitalization for nephrotic syndrome.