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1.
Zootaxa ; 5256(6): 501-543, 2023 Mar 23.
Article in English | MEDLINE | ID: mdl-37044633

ABSTRACT

The South African fauna of Gymnobisiidae pseudoscorpions is revised. Originally containing only three species in a single genus (Gymnobisium Beier, 1931), results of this study show that there are eight distinct species of the genus within South Africa, five of which are new to science, namely G. capense sp. nov., G. cuneatum sp. nov., G. hogsbackense sp. nov., G. megalodontum sp. nov. and G. prionotogladiatum sp. nov. Three of these, namely G. cuneatum sp. nov., G. hogsbackense sp. nov., and G. inukshuk Harvey and Giribet, 2016 (which is a rare troglobite), are short-range endemics and threatened by habitat loss. Most of the other species, with the exception of G. quadrispinosum (Tullgren, 1907), have small distribution ranges. They are predominantly found inhabiting moist leaf litter of indigenous forests along the coastal provinces, indicating either a low dispersal ability or high niche specificity in these pseudoscorpions. The lack of dense, shaded vegetation between isolated forest patches seems to act as a dispersal barrier for many of the species.


Subject(s)
Arachnida , Animals , Arachnida/classification , Forests , South Africa , Animal Distribution
2.
Biochem J ; 202(1): 203-9, 1982 Jan 15.
Article in English | MEDLINE | ID: mdl-7082308

ABSTRACT

The interaction of rat uterine cytosol oestrogen-receptor complexes with the synthetic acceptor oligo(dT)--cellulose was studied. Differences in the stability of receptor complexes and their ability to bind to oligo(dT)--cellulose on storage at 4 degrees C or when exposed to increased temperatures indicated heterogeneity of steroid- and oligonucleotide-binding sites. Dilution, dialysis and (NH4)2SO4 precipitation increased the interaction of receptor complexes with oligo(dT)--cellulose (a step termed activation). This increase may be the result of the removal of low-molecular-weight cytosol components which inhibit receptor activation, dimerization to the 5 S form, which binds to oligo(dT)--cellulose, or interaction of 5 S receptor with the oligonucleotide. Cytosol oestradiol--receptor complexes exhibited biphasic dissociation kinetics. All these manipulations resulted in an increase in the proportion of the slow-dissociating component equivalent to the increase in receptor binding to oligo(dT)--cellulose. In contrast, addition of 10mM-sodium molybdate to cytosol decreased both oligo(dT)--cellulose binding and the proportion of receptor with slow dissociation kinetics. The inclusion of proteinase inhibitors did not affect interactions of receptor with oligo(dT)--cellulose nor the dissociation kinetics. These results suggest that oligo(dT)--cellulose binding may serve to quantify the proportion of cytosol receptor in an active form capable of nuclear interaction and to help to ascertain whether a receptor system is fully functional. This binding procedure could prove useful in the evaluation of oestrogen responsivity under normal and pathological conditions.


Subject(s)
Cellulose/analogs & derivatives , Oligodeoxyribonucleotides/metabolism , Oligonucleotides/metabolism , Receptors, Estrogen/metabolism , Uterus/metabolism , Animals , Binding Sites , Cellulose/metabolism , Cytosol/metabolism , Estradiol/metabolism , Female , In Vitro Techniques , Kinetics , Ligands , Molybdenum/pharmacology , Rats , Receptors, Estrogen/drug effects
3.
Biochem J ; 194(3): 667-71, 1981 Mar 15.
Article in English | MEDLINE | ID: mdl-7197925

ABSTRACT

The nuclear oestrogen receptor population in the rat uterus contained an unoccupied receptor component that bound oestradiol with the high affinity (Kd congruent to 0.5 nM) characteristic of oestrogen receptors. This unoccupied receptor was present at all phases of the oestrous cycle. Its content changed in parallel with that of the total nuclear receptor during the cycle. Oestradiol administration to the immature rat resulted in increases in the uterine content of long-term nuclear receptors (i.e., those still present 8 h after administration); these increases were due to occupied oestrogen receptors, since the content of unoccupied receptor was unchanged. Our previous experiments [White & Lim (1980) Biochem. J. 190, 833-837] have shown in contrast, that oestradiol administration results in an increase in the content of unoccupied nuclear receptor in the hypothalamus. However, as in the uterus, similar cyclic changes in the content of unoccupied nuclear receptor occurred in parallel with those of the total nuclear receptor population in the hypothalamus. Differences and similarities between the unoccupied nuclear receptor of the uterus and hypothalamus are briefly discussed.


Subject(s)
Estradiol/metabolism , Estrus , Hypothalamus/metabolism , Receptors, Estrogen/metabolism , Uterus/metabolism , Animals , Cell Nucleus/metabolism , Estradiol/pharmacology , Female , Pregnancy , Rats , Receptors, Estrogen/drug effects
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