The innervation of some proboscis structures involved in feeding behavior of the blowfly (Calliphora vicina)

The microtopology of the motoneurons involved in protraction and retraction of the proboscis of the blowfly (Calliphora vicina) has been studied. In addition, taste input from the labellar hairs was investigated. As a result of this study it appears that protraction movements are controlled by two while retraction movements are guided by three motoneurons on each side. The neurons in each group apear to be in ipsicontralateral communication with each other. The musculi protractores fulcri (MPF) probably contain a proprioceptive cell group which projects to the MPF motoneurons. It is proposed that the proboscis motor system can be modulated by proprioception as well as by chemosensory labellar input. Neurosecretory cells may be involved in adjusting muscle power.     

Action of phospholipases on the cytoplasmic membrane of Escherichia coli. Stimulation by melittin

The emission maximum of the single tryptophan residue of melittin was measured in the presence of phosphatidylethanolamine liposomes and Escherichia coli cytoplasmic membranes. In both cases, the fluorescence maximum was shifted to shorter wavelengths indicating a transfer of the indole ring to an apolar environment. E. coli membranes were labelled in position 2 of their phospholipids with [¹⁴C]oleic acid. These membranes were used for measuring the activity of an endogenous phospholipase A₂. A slow hydrolysis is observed, which can be accelerated by adding melittin. The extent of the stimulation depends on the molar ratio of melittin to membrane phospholipid. Under suitable conditions, the initial rate of hydrolysis is six to seven times higher in the presence than in the absence of melittin. The action of the phospholipase A₂ from bee venom is also stimulated by melittin. An identical stimulation was observed with either E. coli membranes or pure phosphatidylethanolamine liposomes as substrate.     

Immunocytochemical localization of the elongation factor Tu in E. coli cells

The localization of the elongation factor Tu (EF-Tu) in ultrathin cryosections of E. coli cells was determined with the electron microscope using a highly specific immunological labelling technique. EF-Tu is distributed almost homogeneously throughout the cytoplasm. Although it has often been suggested that EF-Tu could be part of a putative prokaryotic cytoskeleton, we did not find any evidence for supramolecular assemblies, such as fibres or filaments, containing a large amount of EF-Tu. EF-Tu was not observed in association with the outer cell membrane and periplasmic space. A topological relationship with the inner membrane is not apparent in our micrographs. In cells in which the EF-Tu level is raised significantly, the protein piles up in discrete cell regions.     

Monoclonal anti-mouse macrophage antibodies recognize the globular portions of C1q, a subcomponent of the first component of complement

One of seven monoclonal antibodies generated against mouse macrophages (M phi) was found to recognize isolated heterologous C1q. This antibody was shown to be cytotoxic and to react in a strain-independent way with mouse M phi derived from bone marrow cells as well as with M phi from the peritoneal cavity; it did not react, however, with mouse granulocytes, thymocytes, or T and B lymphocytes. The hemolytic activity of fluid phase C1q was inhibited to 50% at a 2 X 10(-4) dilution of hybridoma supernatant, whereas a 100-fold higher concentration was required to inhibit C1q bound to immune complexes ( EAC1q ) to the same extent. It was demonstrated that this antibody recognizes the isolated globular, Fc-binding portions of the C1q molecule and reacts with the A and B chains. Because M phi have been shown to synthesize C1q, the Fc-recognizing subcomponent of the first component of complement, evidence was provided that endogeneous C1q can serve as an Fc receptor on M phi during secretion. This fact was demonstrated by a dose-dependent inhibition of Fc-receptor activity for EIgG by the F(ab')2 fragment of this monoclonal antibody. These experiments further support the concept that C1q produced by M phi functions on the surface as an Fc-recognizing molecule before it is released and incorporated into the macromolecular complex of serum C1.