A chelation-directed self-sorting synthesis of a series of cationic heterometallic coordination cages (HCCs) with tunable sizes is described. Two complexation modes were found in the cage-forming process. Metal-anchoring host-guest behavior and size-selective in-cage catalytic activities were found for the HCCs.

The purpose of this study was to explore the clinical and serological features of patients with pneumomediastinum (PNM) and dermatomyositis-associated interstitial lung disease (DM-ILD). A total of 93 patients (68 with classic DM and 25 with clinically amyopathic DM [CADM]) were recruited. Clinical and laboratory data were collected retrospectively. Anti-melanoma differentiation-associated gene 5 (MDA5) antibodies were detected using enzyme-linked immunosorbent assay (ELISA). Variables were compared between patients with and those without PNM. Multivariate analysis was performed using a multivariate logistic regression model. A total of 11 patients developed spontaneous PNM. During the follow-up period, 6 patients died of respiratory failure. No differences in sex, age at the onset of DM, serum ferritin levels, and C-reactive protein (CRP) levels were observed between DM patients with and without PNM. Compared with DM patients without PNM, those with PNM had significantly higher frequencies of rapidly progressive ILD (RP-ILD) (63.6 vs 24.4 %, P = 0.01), anti-MDA5 antibodies (90.9 vs 52.4 %, P = 0.02), CADM diagnoses (63.6 vs 22.0 %, P = 0.007) and cutaneous ulcers (36.4 vs 11 %, P = 0.04), but significantly lower creatine kinase (CK) levels (58.5 vs 284 U/l, P = 0.04). The multivariate analysis indicated that cutaneous ulcer was the only independent risk factor for the occurrence of PNM in DM (OR = 5.98, 95 % confidence interval [CI] 1.12-31.98, P = 0.037). PNM is a refractory complication and tends to occur in DM patients with RP-ILD, anti-MDA5 antibody, CADM diagnosis, and low CK level, and especially in patients with cutaneous ulcers.

The study aims to comprehensively assess the profiles of myositis-specific autoantibodies (MSAs) in Chinese patients with polymyositis (PM)/dermatomyositis (DM) and compare them with a Japanese cohort. One hundred forty-five Chinese patients (68 classic DM, 25 clinically amyopathic DM [CADM], and 52 PM) and 165 Japanese patients (56 classic DM, 52 CADM, and 57 PM) were recruited. MSAs were measured with immunoprecipitation, enzyme-linked immunosorbent assay, or immunoprecipitation-immunoblotting. MSA frequencies were compared. The overall frequency of anti-melanoma differentiation-associated gene 5 (MDA5) antibodies was significantly higher in the Chinese patients than in the Japanese cohort (36.6 % [53/145] versus 15.8 % [26/165], respectively, P < 0.001), whereas the frequencies of anti-signal recognition particle (SRP) antibodies (1.4 % [2/145] versus 7.9 % [13/165], respectively, P = 0.008) and anti-aminoacyl-transfer RNA synthetase (anti-ARS) antibodies (27.6 % [40/145] versus 40 % [66/165], respectively, P = 0.02,) were significantly lower. The significantly lower frequency of anti-ARS antibodies and significantly higher frequency of anti-MDA5 antibodies in the Chinese patients were observed in the classic DM subset (14.7 % [10/68] versus 46.4 % [26/56], respectively, P < 0.001, and 45.6 % [31/68] versus 5.4 % [3/56], respectively, P < 0.001) and CADM subset (8.0 % [2/25] versus 28.8 % [15/52], respectively, P = 0.04, and 88.0 % [22/25] versus 44.2 % [23/52], respectively, P = 0.0002), but not in the PM subset. The first detailed profile of MSAs in Chinese patients with PM/DM was established. The differences in MSA frequencies in the Chinese cohort and Japanese cohort suggest underlying genetic and/or environmental differences between these two populations. Key Messages • A significantly higher frequency of anti-melanoma differentiation-associated gene 5 (MDA5) antibodies was observed in Chinese patients with polymyositis/dermatomyositis (PM/DM) than in Japanese patients. • Our findings suggest that distinct genetic and/or local environmental factors affect Chinese and Japanese patients with PM/DM, who have been considered a "homogeneous" population in previous studies.

No abstract

Glycoproteins are involved in the development of many diseases, while the type and content of N-glycoproteins in the cartilage of osteoarthritis (OA) and Kashin–Beck disease (KBD) are still unclear. This research aims to identify N-glycoproteins in knee cartilage patients with OA and KBD compared with normal control (N) adults. The cartilage samples were collected from gender- and age-matched OA (n = 9), KBD (n = 9) patients, and N (n = 9) adults. Glycoproteomics and label-free liquid chromatography-tandem mass spectrometry (LC-MS/MS) obtained N-glycoproteins of KBD and OA. A total of 594 N-glycoproteins and 1146 N-glycosylation peptides were identified. The identified data were further compared and analyzed with Gene Ontology (GO), Kyoto Encyclopedia of Genes and Genomes (KEGG), and Protein–Protein Interactions (PPI). Pairwise comparison of the glycoproteins detected in the three groups showed that integrin beta-1 (ITGB1), collagen alpha-1 (II) chain (COL2A1), collagen alpha-1 (VII) chain (COL7A1), carbohydrate sulfotransferase 3 (CHST-3), carbohydrate sulfotransferase 4 (CHST-4), thrombospondin 2 (THBS2), bone morphogenetic protein 8A (BMP8A), tenascin-C (TNC), lysosome-associated membrane protein (LAMP2), and beta-glucuronidase (GUSB) were significantly differentially expressed. GO results suggested N-glycoproteins mainly belonged to protein metabolic process, single-multicellular and multicellular organism process, cell adhesion, biological adhesion, and multicellular organism development. KEGG and PPI results revealed that key N-glycoproteins were closely related to pathways for OA and KBD, such as phagosome, ECM-receptor interaction, lysosome, focal adhesion, protein digestion, and absorption. These results reflected glycoprotein expression for OA and KBD in the process of ECM degradation, material transport, cell–cell or cell–ECM interaction, and information transduction. These key significantly differentially expressed N-glycoproteins and pathways lead to the degeneration and degradation of the cartilage of OA and KBD mainly by disrupting the synthesis and catabolism of basic components of ECM and chondrocytes and interfering with the transfer of material or information. The key N-glycoproteins or pathways in this research are potential targets for pathological mechanisms and therapies of OA and KBD.