Proposing a solution to the Articulata–Ecdysozoa controversy

Recent studies of animal radiation agree on monophyly of the Bilateria, but there is no consensus about the early radiation of the group. Protostomia and Deuterostomia are usually recognized, with two competing theories regarding the division of the Protostomia: one divides them into Spiralia and Cycloneuralia, the other into Lophotrochozoa and Ecdysozoa. The main discrepancy concerns the Arthropoda, which are placed with the Articulata within the Spiralia by the first group, and with the Cycloneuralia within the Ecdysozoa by the second. Here I propose that this discrepancy can be resolved by regarding the Ecdysozoa as the sister group of the Annelida within the Articulata. This implies that segmentation has been lost in phyla such as Nematoda and Priapula, but the Kinorhyncha may show a 'reduced segmentation' with serially arranged muscles associated with a ringed cuticle. Morphological, palaeontological and molecular implications of this theory are discussed. While many morphological and palaeontological data can be interpreted in accordance with the theory, the molecular data remain inconclusive.     

The use of a proteinaceous “cushion” with a polystyrene‐binding peptide tag to control the orientation and function of a target peptide adsorbed to a hydrophilic polystyrene surface

In immobilizing target biomolecules on a solid surface, it is essential (i) to orient the target moiety in a preferred direction and (ii) to avoid unwanted interactions of the target moiety including with the solid surface. The preferred orientation of the target moiety can be achieved by genetic conjugation of an affinity peptide tag specific to the immobilization surface. Herein, we report on a strategy for reducing the extent of direct interaction between the target moiety and surface in the immobilization of hexahistidine peptide (6His) and green fluorescent protein (GFP) on a hydrophilic polystyrene (PS) surface: Ribonuclease HII from Thermococcus kodakaraensis (cHII) was genetically inserted as a “cushion” between the PS‐affinity peptide tag and target moiety. The insertion of a cushion protein resulted in a considerably stronger immobilization of target biomolecules compared to conjugation with only a PS affinity peptide tag, resulting in a substantially enhanced accessibility of the detection antibody to the target 6His peptide. The fluorescent intensity of the GFP moiety was decreased by approximately 30% as the result of fusion with cHII and the PS‐affinity peptide tag but was fully retained in the immobilization on the PS surface irrespective of the increased binding force. Furthermore, the fusion of cHII did not impair the stability of the target GFP moiety. Accordingly, the use of a proteinaceous cushion appears to be promising for the immobilization of functional biomolecules on a solid surface. © 2016 American Institute of Chemical Engineers Biotechnol. Prog., 32:527–534, 2016     

Prepartum nausea and vomiting; a new approach to treatment

A controlled study of 101 patients indicated that a combination of amphetamine and Rauwolfia was effective in the treatment of prepartum nausea and vomiting. Good to excellent results were obtained in 53 (83 per cent) of 64 patients who received the combination. Five patients reported fair results; six were not benefited by the treatment. Only five of a control group of 37 patients who received placebos reported good results. In addition to relief of the symptoms of nausea and vomiting, concomitant emotional disturbances, notably anxiety and depression, were alleviated by the drug combination.     

Papilin in development; a pericellular protein with a homology to the ADAMTS metalloproteinases

Papilin is an extracellular matrix glycoprotein that we have found to be involved in, (1) thin matrix layers during gastrulation, (2) matrix associated with wandering, phagocytic hemocytes, (3) basement membranes and (4) space-filling matrix during Drosophila development. Determination of its cDNA sequence led to the identification of Caenorhabditis and mammalian papilins. A distinctly conserved 'papilin cassette' of domains at the amino-end of papilins is also the carboxyl-end of the ADAMTS subgroup of secreted, matrix-associated metalloproteinases; this cassette contains one thrombospondin type 1 (TSR) domain, a specific cysteine-rich domain and several partial TSR domains. In vitro, papilin non-competitively inhibits procollagen N-proteinase, an ADAMTS metalloproteinase. Inhibiting papilin synthesis in Drosophila or Caenorhabditis causes defective cell arrangements and embryonic death. Ectopic expression of papilin in Drosophila causes lethal abnormalities in muscle, Malpighian tubule and trachea formation. We suggest that papilin influences cell rearrangements and may modulate metalloproteinases during organogenesis.