Comparison between pars intercerebralis neurosecretory cells of Glossina and those of other higher Diptera

Three types of the A-neurosecretory cells (NSCs) were found in the pars intercerebralis (PI) of the adult brain of four species of tsetse flies (Glossina palpalis, G. pallidipes, G. austeni and G. morsitans). The typical formula of their composition is: 8 A1-, 14 A2- and 4 A3-cells. After permanganate oxidation, the neurosecretory materials (NSMs) of Al- and A3-cells are rich in strong acid groups. The A2-NSM contains both strong and weak acid groups after this treatment; besides, it retains a weak affinity to acid dyes. In addition to the A-cells, the PI of Glossina species seems to include a number of NSCs of the type B.
The data obtained indicate a great similarity of the NSC composition in the PI of Glossina and other related higher dipterans.
In addition to the NSCs, giant neurons and particular cells with large cytoplasmic inclusions were also found in the PI of Glossina. The cells with large cytoplasmic inclusions correspond apparently to vacuolated cells previously observed in the brain of some flies. It is suggested that the considerable complication in reproductive biology which took place in tsetse flies had no effect on the composition of the NSCs in their PI when compared to that in related species with more ordinary cycles of reproduction.     

Polyamines spermidine and spermine as modulators of calcium-dependent immune processes

The polyamines spermidine and spermine are ubiquitous in animal cells and have been shown to bind to cell membranes. At least two types of immune processes, secretion of active substances during inflammation and lymphocyte activation in cellular immunity, involve cell membranes and calcium ions. Although these processes are activated by polyvalent substances, spermidine and spermine appear to inhibit them. This action of polyamines is discussed in the context of regulating both cell membrane fluidity and calcium fluxes.     

Polyamines permit the preparation of stable Physarum core particles which have a structure similar to those from higher eukaryotes

The inherent instability of Physarum nucleosome core particles prepared by micrococcal nuclease digestion in Na⁺/Ca²⁺ buffers can be overcome by the addition of 0.15 mM spermine and 0.5 mM spermidine. Neutron scattering, circular dichroism, nuclease digestion and thermal denaturation studies carried out on these stable monosomes show them to be very similar to those obtained from higher eukaryotes.     

Production of recombinant proteins by microbes and higher organisms

Large proteins are usually expressed in a eukaryotic system while smaller ones are expressed in prokaryotic systems. For proteins that require glycosylation, mammalian cells, fungi or the baculovirus system is chosen. The least expensive, easiest and quickest expression of proteins can be carried out in Escherichia coli. However, this bacterium cannot express very large proteins. Also, for S–S rich proteins, and proteins that require post-translational modifications, E. coli is not the system of choice. The two most utilized yeasts are Saccharomyces cerevisiae and Pichia pastoris. Yeasts can produce high yields of proteins at low cost, proteins larger than 50 kD can be produced, signal sequences can be removed, and glycosylation can be carried out. The baculoviral system can carry out more complex post-translational modifications of proteins. The most popular system for producing recombinant mammalian glycosylated proteins is that of mammalian cells. Genetically modified animals secrete recombinant proteins in their milk, blood or urine. Similarly, transgenic plants such as Arabidopsis thaliana and others can generate many recombinant proteins.     

A 64,000 dalton matrix protein of human cytomegalovirus induces in vitro immune responses similar to those of whole viral antigen

Human cytomegalovirus contains approximately 30 to 35 structural polypeptides. Although antibodies to several of these proteins are made during natural infection, their relationship to T cell recognition of this virus and subsequent control of infection is poorly understood. We have purified one of these proteins (HCMVgp64) that is found in abundance in infected cell lysates in order to delineate the relationship of single viral proteins to the immune response caused by the virus. HCMVgp64 induced T cell reactivity only in individuals with serologic evidence of past infection. In addition, HCMVgp64 elicited similar in vitro immune reactions as the whole virus including T cell proliferation, interleukin 2 production, and receptor expression as well as interferon production. These studies suggest that single proteins of HCMV such as HCMVgp64 are capable of inducing T cell responses and may be important in the development of immune reactivity to HCMV.     

Color vision of ancestral organisms of higher primates

The color vision of mammals is controlled by photosensitive proteins called opsins. Most mammals have dichromatic color vision, but hominoids and Old World (OW) monkeys enjoy trichromatic vision, having the blue-, green-, and red-sensitive opsin genes. Most New World (NW) monkeys are either dichromatic or trichromatic, depending on the sex and genotype. Trichromacy in higher primates is believed to have evolved to facilitate the detection of yellow and red fruits against dappled foliage, but the process of evolutionary change from dichromacy to trichromacy is not well understood. Using the parsimony and the newly developed Bayesian methods, we inferred the amino acid sequences of opsins of ancestral organisms of higher primates. The results suggest that the ancestors of OW and NW monkeys lacked the green gene and that the green gene later evolved from the red gene. The fact that the red/green opsin gene has survived the long nocturnal stage of mammalian evolution and that it is under strong purifying selection in organisms that live in dark environments suggests that this gene has another important function in addition to color vision, probably the control of circadian rhythms.      

Histones synthesized for use in early development of Xenopus laevis are stored as a complex with antigenic properties similar to those of the octamer core of nucleosomes

Serum of patients with systemic lupus erythematosus (SLE) contains crossreacting autoantibodies which recognize histones in nucleosomes or when they are induced to form octamers in solution in the presence of 2 M NaCl, but not when they are dissociated free in solution at physiological ionic strength. We have found that histones stored in eggs of Xenopus laevis for use in rapid nuclear synthesis during early development react with this antibody. This reaction has been observed by radioimmunoassay, inhibition of chromatin assembly by the extracts in the presence of antibody, and, in a preliminary result, by identification of a histone-antibody complex bound to protein A- sepharose. Further evidence that the extract antigen corresponds to the stored histone pool comes from sedimentation and charge fractionation experiments where the chromatin assembly activity and antigen (measured by radioimmunoassay) were found to cofractionate. BEcause the extract histones are not bound to DNA, our results suggest that they are stored as a soluble complex in a conformation similar or identical to the octameric core of the nucleosome. Our data suggest that the histones in this complex are bound to an anionic factor or factors which presumably replaces the DNA in shielding the positive charges on the histones.     

Identification of ribosomal proteins specific to higher eukaryotic organisms

This report describes the identification of a novel protein named PS1D (Genbank accession number ), which is composed of an S1-like RNA-binding domain, a (cysteine)x3-(histidine) CCCH-zinc finger, and a very basic carboxyl domain. PS1D is expressed as two isoforms, probably resulting from the alternative splicing of mRNA. The long PS1D isoform differs from the short one by the presence of 48 additional amino acids at its amino-terminal extremity. Analysis of PS1D subcellular distribution by cell fractionation reveals that this protein belongs to the core of the eukaryotic 60S ribosomal subunit. Interestingly, PS1D protein is a highly conserved protein among mammalians as murine, human, and simian PS1D homologues share more than 95% identity. In contrast, no homologous protein is found in lower eukaryotes such as yeast and Caenorhabditis elegans. These observations indicate that PS1D is the first eukaryotic ribosomal protein that is specific to higher eukaryotes.     

Current theories on gene structure of higher organisms]

A review of history of studies on gene structure and molecular-genetic data obtained during the last years are presented. The complicate structure of genes in eukaryotes and different ways of gene activity regulation are demonstrated.     

A possible aid to survival of the marine coccolithophorid Cricosphaera and similar organisms

An examination has been made of clones of Cricosphaera from the Plymouth culture collection. These organisms are biflagellate motile coccolithophorids which, in culture, produce non-motile filamentous benthic phases similar to forms included in the Chrysotilaceae (e.g. Apistonema).

Cricosphaera carterae (Plymouth No. 17) produces, in liquid culture, motile cells invested with several layers of characteristically patterned scales and one layer of coccoliths. The scales are of three types, (I) small oval scales, (II) medium-sized round scales and (III) large oval scales which are always associated with coccoliths.

Growth on agar produces Apistonema-like cells which, although lacking scales of Types I and III, have a greatly thickened investment of closely packed Type II scales. Other Apistonema type clones, previously believed to be covered in mucilage, are similarly ensheathed by thick layers of scales which are thought to aid the benthic phases in withstanding dry conditions.