Diverticulum of the atrium is a rare and controversial clinical entity, and in the present case a left atrial diverticulum was associated with severe mitral regurgitation (MR). A 68-year-old female with the diagnosis of MR was referred for further cardiac evaluation. Echocardiography revealed severe MR and an accessory cavity behind an enlarged left atrium. She underwent surgical valve replacement, but excision of the diverticulum was not done because its rupture seemed unlikely. A follow-up computed tomography performed 8 months postoperatively demonstrated disappearance of the diverticulum. The etiology of this atrial diverticulum is not clear, but the patient's MR may have played a role in its development.

Plakoglobin is a member of a protein family with a repeated amino acid motif, the armadillo repeat, and is a cytoplasmic protein found in both adherens junctions and desmosomes. Plakoglobin has been shown to form distinct complexes with cadherins or desmosomal cadherins. Also, plakoglobin has been shown to complex with APC, the tumor suppressor gene product. Recently we isolated a cDNA clone encoding plakoglobin lacking the fourth armadillo repeat of the original 13-repeat protein [Ozawa et al. (1995) J. Biochem. 118, 836-840]. In this study, we established an in vitro assay system to study the molecular interaction of plakoglobin with cadherins, the APC gene product, and alpha-catenin. Establishment of the system and cloning of an alternate form of plakoglobin cDNA allowed us to examine the biological activity of plakoglobin lacking the fourth armadillo repeat. Experiments with the bacterially expressed 12-repeat plakoglobin revealed that the protein binds to E-cadherin, desmoglein (Dsg2), and APC with lower affinity than the 13-repeat form does. Consistent with the observation that the affinity of alpha-catenin for these two alternate forms was similar, we found amino acid residues 104 to 145 of plakoglobin, the residues present in both isoforms, are sufficient for its binding to alpha-catenin.

A case of infective endocarditis (IE) caused by a rare pathogen, Gemella morbillorum, is presented. Because of persistent low-grade fever after dental treatment, the patient was given oral antibiotics. Whereas he was diagnosed as having aortic regurgitation by a cardiologist, and IE was not suggested unfortunately. After long-term chemotherapy over five months, he was aware of nocturnal dyspnea and Gemella morbillorum was detected by blood culture. Then, he was treated with intravenous administration of Penicillin-G, and underwent surgical operation for valve replacement. No cases of IE due to this organism have been reported in Japan. (Internal Medicine 33: 628-631, 1994)

The low density lipoprotein receptor-related protein (LRP) is a multifunctional endocytic receptor with the ability to bind and endocytose several structurally and functionally distinct ligands. The 39 kDa receptor-associated protein (RAP) is an endoplasmic reticulum (ER) resident protein, which is believed to function intracellularly as a molecular chaperone for LRP and to regulate its ligand binding activity along the secretory pathway. Mouse heparin binding protein-44 (HBP-44) is a homologue of human RAP. Using a recombinant form of HBP-44 expressed in Escherichia coli cells as a highly specific ligand for LRP, we demonstrated that HBP-44 coated on cell culture plates mediates the cell-substratum adhesion of mouse 3T3 fibroblasts in a dose-dependent manner, with 50% attachment at the concentration of 0.2 micrograms/ml. Ligand blot analysis with HBP-44 of whole cell extracts and the materials precipitated by anti-LRP antibodies revealed that the receptor for HBP-44 on NIH/3T3 cells was LRP. The results suggest that LRP serves as a cell adhesion receptor in some cells.