Crystalline Light Chain Casts and Hypercalcemia Induced Acute Kidney Injury: A Rare Presentation of Multiple Myeloma.

The most common cause of acute kidney injury (AKI) in multiple myeloma is light-chain cast nephropathy (LCCN), which consists of a light chain and Tamm-Horsfall protein (THP). We herein report a 46-year-old woman with hypercalcemia and AKI. A renal biopsy showed crystalline casts, which were consistent with lambda light chains but not THP. Hydration therapy and treatment to lower her serum calcium concentration were initiated immediately. She subsequently received bortezomib-based anti-myeloma therapy and recovered successfully. This was a rare case of LCCN, suggesting that hypercalcemia may play a role in the development of crystalline LCCN.

Aqueous gel formation from sodium salts of cellobiose lipids.

Cellobiose lipids (CLs) are asymmetric bolaform biosurfactants, which are produced by Cryptococcus humicola JCM 10251 and have fungicidal activity. In this study, the sodium salts of CLs (CLNa) were prepared to improve aqueous solubility of the CLs, and their surface and gelation properties in aqueous solutions were examined by surface tension, rheology, and freeze-fracture transmission electron microscopy (FF-TEM) measurements. The surface tension measurements revealed that the CLNa have high surface activity: CMC1 and γCMC1 are 0.1 mg/mL and 34.7 mN/m, respectively. It was also found that the CLNa form giant micelles above their CMC, whose average size is 116.6 ± 31.9 nm. Unlike conventional surfactants, the surface tension reduced further with an increase in concentration and the aqueous solution became viscous at the minimum gelation concentration (MGC: 5.0 mg/mL). In rheological studies, the obtained gels proved to be rather soft and their sol-gel temperature was found to be approximately 50℃. FF-TEM observation of the gels showed 3D supramolecular structures with an entangled fibrous network. Since the present CLNa aqueous gels have a degree of fungicidal activity, they could be useful for novel multifunctional soft materials applicable to the food and cosmetic industries.

L-Glutamate secretion by the N-terminal domain of the Corynebacterium glutamicum NCgl1221 mechanosensitive channel.

The Corynebacterium glutamicum NCgl1221 mechanosensitive channel mediates L-glutamate secretion by sensing changes in membrane tension caused by treatments such as biotin limitation and penicillin. The NCgl1221 protein has an N-terminal domain (1-286 a.a.) homologous to the Escherichia coli MscS and a long C-terminal domain (287-533 a.a.) of unknown function. In order to investigate the role of the C-terminal domain in L-glutamate secretion, we constructed a series of C-terminally truncated mutants of NCgl1221. We found that the N-terminal domain, homologous to E. coli MscS, retained the ability to cause L-glutamate secretion in response to the treatment. Electrophysiological analysis confirmed that the N-terminal domain mediated L-glutamate secretion. 3D homology modeling has suggested that the N-terminal domain of NCgl1221 has an extra loop structure (221-232 a.a.) that is not found in most other MscS proteins. The mutant NCgl1221, deleted for this loop structure, lost the ability to secrete L-glutamate. In addition, we found that mutant NCgl1221 lacking the C-terminal extracytoplasmic domain (420-533 a.a.) produced L-glutamate without any inducing treatment. These results suggest that the N-terminal domain is necessary and sufficient for the excretion of L-glutamate in response to inducing treatment, and that the C-terminal extracytoplasmic domain has a negative regulatory role in L-glutamate production.