A Highly Sensitive Immunoenzymometric Assay for the Determination of Angiogenin

Peer Reviewe

Preliminary Results for the Multi-Robot, Multi-Partner, Multi-Mission, Planetary Exploration Analogue Campaign on Mount Etna

This paper was initially intended to report on the outcome of the twice postponed demonstration mission of the ARCHES project. Due to the global COVID pandemic, it has been postponed from 2020, then 2021, to 2022. Nevertheless, the development of our concepts and integration has progressed rapidly, and some of the preliminary results are worthwhile to share with the community to drive the dialog on robotics planetary exploration strategies. This paper includes an overview of the planned 4-week campaign, as well as the vision and relevance of the missiontowards the planned official space missions. Furthermore, the cooperative aspect of the robotic teams, the scientific motivation, the sub task achievements are summarised

Finally! Insights into the ARCHES Lunar Planetary Exploration Analogue Campaign on Etna in summer 2022

This paper summarises the first outcomes of the space demonstration mission of the ARCHES project which could have been performed this year from 13 june until 10 july on Italy’s Mt. Etna in Sicily. After the second postponement related to COVID from the initially for 2020 planed campaign, we are now very happy to report, that the whole campaign with more than 65 participants for four weeks has been successfully conduced. In this short overview paper, we will refer to all other publication here on IAC22. This paper includes an overview of the performed 4-week campaign and the achieved mission goals and first results but also share our findings on the organisational and planning aspects

A 25 KDA ALPHA-2-MICROGLOBULIN-RELATED PROTEIN IS A COMPONENT OF THE 125-KDA FORM OF HUMAN GELATINASE

TRIEBEL S, BLASER J, REINKE H, Tschesche H. A 25 KDA ALPHA-2-MICROGLOBULIN-RELATED PROTEIN IS A COMPONENT OF THE 125-KDA FORM OF HUMAN GELATINASE. FEBS LETTERS. 1992;314(3):386-388.Besides the monomeric mammalian 95 kDa progelatinase, two additional forms, a disulfide-bridged 220 kDa dimer and a 125 kDa form were isolated from human PMN leukocytes. The 125 kDa progelatinase was identified as a covalently linked, disulfide-bridged hetrodimer formed of the monomer with a 25 kDa protein. This 25 kDa protein was isolated from gelatinase bound to the affinity support of gelatin-Sepharose and eluted by DTE-containing buffer. The amino acid sequence of tryptic peptides of this protein revealed homology with an alpha2-microglobulin-related protein from rats, a protein so far unknown in humans

FORMATION OF A COVALENT HG-CYS-BOND DURING MERCURIAL ACTIVATION OF PMNL PROCOLLAGENASE GIVES EVIDENCE OF A CYSTEINE-SWITCH MECHANISM

BLASER J, TRIEBEL S, REINKE H, Tschesche H. FORMATION OF A COVALENT HG-CYS-BOND DURING MERCURIAL ACTIVATION OF PMNL PROCOLLAGENASE GIVES EVIDENCE OF A CYSTEINE-SWITCH MECHANISM. FEBS LETTERS. 1992;313(1):59-61.A common method for the activation of mammalian metalloproteinases is the use of mercurial compounds. Activation of PMNL procollagenase by soluble mercurials takes place as a three-step mechanism with a final intermolecular loss of the PRCGVPD autoinhibitor region. In this study covalently bound mercury in the form of mercurial agarose was chosen to probe activation of PMNL procollagenase. Activation was not achieved, since the final intermolecular cleavage with removal of the PRCGVPD motif could not take place. An intermediate form of the enzyme was bound to the column. Its N-terminal sequence determination proved cleavage of the Asp64-Met65 peptide bond leaving the cysteine of the propeptide domain for covalent attachment to the mercurial agarose. This gives further evidence of a cysteine-switch mechanism involving Cys71

INACTIVATION OF HUMAN PLASMA CL-INHIBITOR BY HUMAN-PMN LEUKOCYTE MATRIX METALLOPROTEINASES

KNAUPER V, TRIEBEL S, REINKE H, Tschesche H. INACTIVATION OF HUMAN PLASMA CL-INHIBITOR BY HUMAN-PMN LEUKOCYTE MATRIX METALLOPROTEINASES. FEBS LETTERS. 1991;290(1-2):99-102.Highly purified human polymorphonuclear (PMN) leucocyte matrix metalloproteinases, collagenase and gelatinase, cleaved human plasma Cl-inhibitor at the carboxyl site of Ala439 (P6). This led to a concomitant loss of Cl-inhibitor activity. An additional cleavage site, at the carboxyl site of Ser441 (P4), was observed during PMN leucocyte gelatinase-induced inactivation, and a minor fragment of the plasma Cl-inhibitor was generated

MERCURIAL ACTIVATION OF HUMAN-PMN LEUKOCYTE TYPE-IV PROCOLLAGENASE (GELATINASE)

TRIEBEL S, BLASER J, REINKE H, KNAUPER V, Tschesche H. MERCURIAL ACTIVATION OF HUMAN-PMN LEUKOCYTE TYPE-IV PROCOLLAGENASE (GELATINASE). FEBS LETTERS. 1992;298(2-3):280-284.Autoproteolytic activation and processing of human polymorphonuclear leucocyte (PMNL) type IV procollagenase (gelatinase) was initiated by HgCl2 and was investigated by kinetic analysis and N-terminal sequence determination of the reaction products. In the first instance the propeptide domain was lost by subsequent cleavage of the Asp15-Leu16, Glu40-Met41, Leu52-Leu53 and Ala74-Met75 peptide bonds. The PRCGVPD sequence motif (residues Pro78-Asp84), which is conserved in all metalloproteinases and expected to be relevant for latency, remained uncleaved at the activated enzyme. The generated intermediate was further processed by three C-terminal cleavages. The Glu666-Leu667, Ala506-Glu507 and Ala398-Leu399 bonds were hydrolysed sucessively. From the fragmentation products we were able to conclude that three released fragment peptides contained unpaired free cysteine with the residues Cys497, Cys653, Cys683. Cleavage of the first C-terminal peptide bond resulted in the loss of one of the conserved Cys residues of the hemopexin-like domain, whereas the Cys residue of the PRCGVPD motif was retained at the fully active enzyme. The possibility of an entirely different activation mechanism for PMNL type IV procollagenase is discussed

The ARCHES Space-Analogue Demonstration Mission: Towards Heterogeneous Teams of Autonomous Robots for Collaborative Scientific Sampling in Planetary Exploration

Teams of mobile robots will play a crucial role in future missions to explore the surfaces of extraterrestrial bodies. Setting up infrastructure and taking scientific samples are expensive tasks when operating in distant, challenging, and unknown environments. In contrast to current single-robot space missions, future heterogeneous robotic teams will increase efficiency via enhanced autonomy and parallelization, improve robustness via functional redundancy, as well as benefit from complementary capabilities of the individual robots. In this letter, we present our heterogeneous robotic team, consisting of flying and driving robots that we plan to deploy on scientific sampling demonstration missions at a Moon-analogue site on Mt. Etna, Sicily, Italy in 2021 as part of the ARCHES project. We describe the robots' individual capabilities and their roles in two mission scenarios. We then present components and experiments on important tasks therein: automated task planning, high-level mission control, spectral rock analysis, radio-based localization, collaborative multi-robot 6D SLAM in Moon-analogue and Mars-like scenarios, and demonstrations of autonomous sample return

The ARCHES Moon-Analogue Demonstration Mission: Towards Teams of Autonomous Robots for Collaborative Scientific Sampling in Lunar Environments

Teams of mobile robots will play a crucial role in future missions to explore the surface of the Moon. Setting up infrastructure and taking scientific samples are expensive tasks when operating in such distant, challenging, and unknown environments. In contrast to current single-robot space missions, future heterogeneous robotic teams will increase efficiency via enhanced autonomy and parallelization, improve robustness via functional redundancy, as well as benefit from complementary capabilities of the individual robots. We present our heterogeneous robotic team, consisting of flying and driving robots that we plan to deploy on scientific sampling demonstration missions at a Moon-analogue site on Mt. Etna, Sicily, Italy in 2021 as part of the ARCHES project. We give a brief description of the robots' complementary capabilities and present their roles in two mission scenarios