A Multi-Robot Cooperation Framework for Sewing Personalized Stent Grafts

This paper presents a multi-robot system for manufacturing personalized medical stent grafts. The proposed system adopts a modular design, which includes: a (personalized) mandrel module, a bimanual sewing module, and a vision module. The mandrel module incorporates the personalized geometry of patients, while the bimanual sewing module adopts a learning-by-demonstration approach to transfer human hand-sewing skills to the robots. The human demonstrations were firstly observed by the vision module and then encoded using a statistical model to generate the reference motion trajectories. During autonomous robot sewing, the vision module plays the role of coordinating multi-robot collaboration. Experiment results show that the robots can adapt to generalized stent designs. The proposed system can also be used for other manipulation tasks, especially for flexible production of customized products and where bimanual or multi-robot cooperation is required.Comment: 10 pages, 12 figures, accepted by IEEE Transactions on Industrial Informatics, Key words: modularity, medical device customization, multi-robot system, robot learning, visual servoing, robot sewin

mS100a7a15, calpain-1 and mature IL-1α are induced in IMQ-induced psoriasis model.

<p><b>(A)</b> Quantification of mS100a7a15 mRNA expression of skin from normal and imiquimod-induced psoriatic mouse backs at 5 days. <b>(B)</b> Immunoblot of mS100a7a15, IL-1α and calpain-1 in skin extracts from normal and imiquimod-induced psoriatic mouse backs. <b>(C)</b> HE staining and immunohistochemical analysis of mS100a7a15, calpain-1 in skin tissues as described in fig 4A. The scale bars represent 100 μm. All data are representative of three independent experiments with n = 6 and are means ± SEM. <i>P</i> values were determined by two-tailed t test. *** <i>P</i><0.001.</p

Proteolysis of IL-1α induced by hS100A7 is dependent on calpain-1.

<p><b>(A)</b> Quantification of IL-1α protein expression treated with hS100A7 (50 ng/ml) in the absence or presence of SB202190 (p38 MAPK inhibitor, 15 μM), PD151746 (calpain-1 inhibitor, 15 μM) in NHEKs. <b>(B)</b> Mature IL-1α protein expression induced by hS100A7 at 6 hours after calpain-1 was silenced by siRNA. <b>(C and D)</b> Calpain-1 protein and mRNA expression determined by westernblot at different time points after treated with hS100A7 (50 ng/ml) in NHEKs. <b>(E)</b> Calpain-1 expression after blocking p38 MAPK activity by SB202190 (15 μM) in NHEKs. <b>(F)</b> The model shows that hS100A7 induces mature IL-1α expression via RAGE-p38 MAPK-calpain-1 signal pathway. All data are representative of three independent experiments with n = 3 and are means ± SEM. <i>P</i> values were determined by two-tailed t test. *** <i>P</i><0.001.</p

P38 MAPK and RAGE are critical to mature IL-1α production induced by hS100A7.

<p><b>(A)</b> Immunoblot of proteins by different times treated with hS100A7 (50 ng/ml) in NHEKs. <b>(B)</b> Quantification of IL-1α protein expression in NHEKs treated with hS100A7 (50 ng/ml) in the absence or presence of SB202190 (p38 MAPK inhibitor, 15 μM), SP600125 (JNK inhibitor, 15 μM), caspase-8 inhibitor, (20 μM), and LY294002 (AKT inhibitor, 20 μM). The recombinant IL-1α protein (20 ng) showed as a positive control. <b>(C)</b> Mature IL-1α protein expression induced by hS100A7 after p38 MAPK was silenced by siRNA. <b>(D)</b> Mature IL-1α protein expression and p38 activation induced by hS100A7 after RAGE was silenced by siRNA. Each experiment was repeated as least three times.</p

IL-17a induces hS100A7 or mS100a7a15 expression <i>in vitro</i> and <i>in vivo</i>.

<p><b>(A)</b> Quantification of hS100A7 mRNA expression in undifferentiated NHEKs stimulated by different cytokines. TNFα = 50 ng/ml, IL17A = 50 ng/ml, IL22 = 50 ng/ml, IL23 = 15 ng/ml, IL33 = 20 ng/ml, IL36γ = 30 ng/ml. <b>(B and C)</b> mS100a7a15 mRNA and protein expression in mouse skin after IL-17a was neutralized by IL-17a-neutralizing antibody in imiquimod-induced mouse model. All data are representative of two independent experiments with n = 3–6 and are means ± SEM. <i>P</i> values were determined by two-tailed t test or one-way ANOVA. * <i>P</i><0.05, *** <i>P</i><0.001.</p

PD151746 ameliorates epidermal hyperplasia in IMQ-treated mice.

<p><b>(A)</b> HE staining of skin in wild-type mouse treated by imiquimod (25 mg) in the absence or presence of PD151746 (10 mg) at 5 days. The scale bars represent 100 μm. <b>(B)</b> Epidermal thickness was measured by Image J. <b>(C)</b> Protein expression on mouse back skin as described in fig 5A by westernblot at 5 days. <b>(D)</b> IL-1α mRNA level was measured by real time PCR as shown in fig 5A. All data are representative of three independent experiments with n = 6 and are means ± SEM. <i>P</i> values were determined by one-way ANOVA. n.s., no significance. * <i>P</i><0.05, ** <i>P</i><0.01.</p

hS100A7 induces mature IL-1α expression in normal human epidermal keratinocytes.

<p><b>(A)</b> IL-1α and IL-1β mRNA levels were measured by real time PCR after incubated with indicated concentrations hS100A7 at 6 hours. <b>(B)</b> Immunoblot of IL-1α treated with hS100A7 (50 ng/ml) at 6 hours or recombinant IL-1α protein (30 ng) by western blot in NHEKs. <b>(C)</b> Immunoblot of IL-1β treated with hS100A7 (50 ng/ml) at 6 hours or irradiated with broad-band UVB 4 mW/cm² by western blot in NHEKs. (<b>D</b>) NHEK cells were incubated with hS100A7 (50 ng/ml) and concentrations of IL-1α in the supernatants were determined by ELISA after 5 hours. (<b>E</b>) Psoriatic epidermis was extracted by RAPI lysis buffer, IL-1α protein level was determined by western blot. All data are representative of three independent experiments with n = 3 and are means ± SEM. <i>P</i> values were determined by two-tailed t test. *** <i>P</i><0.001.</p

The identification of the lipopeptide from <i>Staphylococcus epidermidis.</i>

<p><b>A.</b> The analysis of the lipopeptide from <i>S.epidermidis</i> by thin-layer chromatography. Duplicate samples were loaded on TLC plate and molecules with different hydrophobicity were separated. Water was used to show hydrophobicity of lipopeptides and ninhydrin was used to show that the lipopeptide contains amino acids. The arrows indicate LP01. <b>B.</b> Q-TOF MS/MS analysis of lipopeptide in positive-ion model. Q-TOF MS/MS analysis showed that the amino acid sequence of the lipopeptide was DIISTIGDLVKWIIDTVIIDATE. <b>C&D.</b> Two possible structures of the lipopeptide. Aspartic acid (D¹) at N-terminus and lysine (K¹¹) are two amino acids with free NH₃⁺, and free -COOH of heneicosanoic acid might react with NH₃⁺ to form CO–NH. Thereby heneicosanoic acid may bind to ¹D or ¹¹K of the peptide chain.</p

LP01 protects mice from <i>S.aureus</i> infection.

<p><b>A.</b> Photograph of skin lesions caused by <i>S.aureus</i> at 3 days after <i>S.aureus</i> injection. <b>B.</b> ImageJ analysis of the lesional size of A. <b>C.</b> ImageJ analysis of the lesional size of PBS- or scrambled lipopeptide-treated mice. Local <i>S.aureus</i> survival in skin (<b>D and E</b>) and systemic <i>S.aureus</i> survival in liver (<b>F</b>) and spleen (<b>G</b>) of PBS- or scrambled lipopeptide- or LP01- pretreated mice. **<i>P</i><0.01; ***<i>P</i><0.001. <i>P</i> values were determined by two-tailed t test or two-way ANOVA. All data are the means ± SEM of <i>n</i> = 6 and representative of two independent experiments.</p

Luminescent Organometallic Complexes Built upon the Nonemissive Azophenine

Azophenine, C₆H₂(NPh)₂(NHPh)₂, is renowned to be nonemissive in solution or in the solid state at 298 and 77 K. It was rendered luminescent in solution at room temperature without using any cyclization strategy of the N^∧N end by anchoring two or four <i>trans</i>-RCCPt­(PBu₃)₂(CC) units (R = hexa-<i>n</i>-hexyltruxene (<b>Tru</b>)) on the azophenine. Complexes of the general formulas C₆H₂(NC₆H₄CCSiMe₃)₂(NH<b>PtTru</b>)₂ (<b>DiPtTruQ</b>) and C₆H₂(N<b>PtTru</b>)₂(NH<b>PtTru</b>)₂(<b>TertPtTruQ</b>), where <b>Pt</b> = <i>trans</i>-C₆H₄CCPt­(PBu₃)₂CC, exhibit fluorescence (420 nm) and phosphorescence (512 nm) bands arising from upper localized ππ*/C₆H₄CC to <b>Tru</b>CC charge transfer singlet and triplet excited states in 2MeTHF at 298 and 77 K. This latter assignment is based on DFT computations (B3LYP). Moreover, <b>DiPtTru</b> and <b>TertPtTru</b> exhibit low-energy absorption bands with maxima in the 470–485 nm range extending all the way to 600–650 nm. These spectral features are associated with charge transfer (CT) excited states: namely, <b>TruPt</b> → <b>Q</b> (<b>Q</b> = C₆H₂N₂(NH)₂). No emission band (fluorescence or phosphorescence) associated with these CT states has been detected at 298 K, but weak fluorescence bands (λ_max ∼750 nm) decaying on the picosecond time scale have been observed in both cases. Biexponential decays were also often noted and likely reflect the presence of the possible conformers associated with the two possible dihedral angles made by the C₆H₄ plane and the central C₆H₂N₂(NH)₂ core. No evidence for electron transfer between the <b>TruPt</b> arms and <b>Q</b> was observed