An elderly-onset neuroblastoma concomitant with minimal change nephrotic syndrome: the first autopsy case report.

BACKGROUND: Neuroblastoma is a well-known embryonal cancer; however, adult-onset neuroblastomas are rare. The systemic symptoms are related to catecholamine excretion or intraabdominal mass effects. Only two cases of neuroblastoma with nephrotic syndrome have previously been reported. We herein present the first autopsy case of neuroblastoma in an older individual associated with minimal change nephrotic syndrome. CASE PRESENTATION: A 63-year-old man was admitted to our hospital for investigation of general fatigue. His renal function was normal and his urine was negative for protein. A computed tomography scan showed a renal tumor and intraabdominal lymph node swelling. Approximately 4 months after admission, he suddenly developed acute renal failure and severe proteinuria, and hemodialysis was instituted. A computed tomography scan revealed an increase in the size of the renal tumor and lymph nodes. He died 1 month later and an autopsy was performed. The tumor exhibited diffuse proliferation of tumor cells with scant cytoplasm, namely small blue cell tumor with rosette formation. As a result of immunohistochemical study, a neuroblastoma was diagnosed. Despite the patient's severe renal failure, most glomeruli showed no remarkable changes. The tubular epithelium exhibited detachment and vacuolation. Electron microscopic study of the glomeruli showed diffuse effacement of the foot processes. These features indicate a diagnosis of minimal change nephrotic syndrome with acute tubular injury. CONCLUSIONS: Minimal change nephrotic syndrome is the most common renal manifestation associated with lymphoproliferative malignancies. We here present an extremely rare case of adult-onset neuroblastoma with minimal change nephrotic syndrome.

NMR analyses of the interaction between the FYVE domain of early endosome antigen 1 (EEA1) and phosphoinositide embedded in a lipid bilayer.

Phosphoinositides (PIs) are crucial lipid components of membranes and are involved in a number of cellular processes through interactions with their effector proteins. Recently, we have established a lipid-protein nanoscale bilayer (nanodisc) containing PIs, hereafter referred to as PI-nanodisc and demonstrated that it could be used for both qualitative and quantitative evaluations of protein-membrane interactions. Here, we report further NMR analyses for obtaining structural insights at the residue-specific level between PI-binding effector protein and PI-nanodisc, using the FYVE domain of early endosome antigen 1 (EEA1), denoted as EEA1 FYVE, and PI(3)P-nanodisc as a model system. We performed a combination of the NMR analyses including chemical shift perturbation, transferred cross-saturation, and paramagnetic relaxation enhancement experiments. These enabled an identification of the interaction surface, structural change, and relative orientation of EEA1 FYVE to the PI(3)P-incorporated lipid bilayer, substantiating that NMR analyses of protein-membrane interactions using nanodisc makes it possible to show the residue-specific interactions in the lipid bilayer environment.

Phosphoinositide-incorporated lipid-protein nanodiscs: A tool for studying protein-lipid interactions.

Phosphatidylinositol (PtdIns) is phosphorylated at D-3, D-4, and/or D-5 of the inositol ring to produce seven distinct lipid second messengers known as phosphoinositides (PIs). The PI level is temporally and spatially controlled at the cytosolic face of the cellular membrane. Effectors containing PI-binding domains (e.g., PH, PX, FYVE, ENTH, FERM) associate with specific PIs. This process is crucial for the localization of a variety of cell-signaling proteins, thereby regulating intracellular membrane trafficking, cell growth and survival, cytoskeletal organization, and so on. However, quantitative assessments of protein-PI interactions are generally difficult due to insolubility of PIs in aqueous solution. Here we incorporated PIs into a lipid-protein nanoscale bilayer (nanodisc), which is applied for studying the protein-PI interactions using pull-down binding assay, fluorescence polarization, and nuclear magnetic resonance studies, each facilitating fast, quantitative, and residue-specific evaluation of the protein-PI interactions. Therefore, the PI-incorporated nanodisc could be used as a versatile tool for studying the protein-lipid interactions by various biochemical and biophysical techniques.

Molecular characterization the YABBY gene family in Oryza sativa and expression analysis of OsYABBY1.

Members of the YABBY gene family have a general role that promotes abaxial cell fate in a model eudicot, Arabidopsis thaliana. To understand the function of YABBY genes in monocots, we have isolated all YABBY genes in Oryza sativa (rice), and revealed the spatial and temporal expression pattern of one of these genes, OsYABBY1. In rice, eight YABBY genes constitute a small gene family and are classified into four groups according to sequence similarity, exon-intron structure, and organ-specific expression patterns. OsYABBY1 shows unique spatial expression patterns that have not previously been reported for other YABBY genes, so far. OsYABBY1 is expressed in putative precursor cells of both the mestome sheath in the large vascular bundle and the abaxial sclerenchyma in the leaves. In the flower, OsYABBY1 is specifically expressed in the palea and lemma from their inception, and is confined to several cell layers of these organs in the later developmental stages. The OsYABBY1-expressing domains are closely associated with cells that subsequently differentiate into sclerenchymatous cells. These findings suggest that the function of OsYABBY1 is involved in regulating the differentiation of a few specific cell types and is unrelated to polar regulation of lateral organ development.