Sexual dimorphism in the pyrgomorphid grasshopper Phymateus morbillosus: from wing morphometry and flight behaviour to flight physiology and endocrinology

Abstract In the field, adult males of the grasshopper Phymateus morbillosus are able to fly for up to 1 min and cover up to c. 100 m, whereas females, although fully winged, are apparently unable to get airborne. Morphometric data indicate that the males are lighter, have longer wings, a higher ratio of flight muscles to body mass, and a lower wing load value than females. It was investigated whether this inability of females to fly is related to fuel storage, flight muscle enzymatic design and/or the presence and quantitative capacity of the endocrine system to mobilize fuels. In both sexes, readily available potential energy substrates are present in the haemolymph in similar concentrations, and the amount of glycogen in flight muscles and fat bodies does not differ significantly between males and females. Mass-specific activities of the enzymes GAPDH (glycolysis), HOAD (fatty acid oxidation) and MDH (citric acid cycle) in flight muscles are significantly lower in females compared with males, and mitochondria are less abundant in the flight muscles of females. There is no significant difference between the ability of the two sexes to oxidize various important substrates. Both sexes contain three adipokinetic peptides in their corpora cardiaca; the amount of each peptide in female grasshoppers is higher than in males.
Thus, despite some differences listed above, both sexes appear to have sufficient substrates and the necessary endocrine complement to engage in flight. It seems more likely, from the morphometric data above, that the chief reason for flightlessness is that P. morbillosus females cannot produce sufficient lift for flight; alternatively, the neuronal functioning associated with the flight muscles may be impaired in females.     

A familial mutation in the testis-determining gene SRY shared by both sexes

A familial mutation in SRY, the gene coding for the testis-determining factor TDF, was identified in an XY female with gonadal dysgenesis, her father, her two brothers and her uncle. The mutation consists of a T to C transition in the region of the SRY gene coding for a protein motif known as the high mobility group (HMG) box, a protein domain known to confer DNA-binding specificity on the SRY protein. This point mutation results in the substitution, at amino acid position 109, of a serine residue for phenylalanine, a conserved aromatic residue in almost all HMG box motifs known. This F109S mutation was not found in 176 male controls. When recombinant wildtype SRY and SRY^F109S mutant protein were tested in vitro for binding to the target site AAC AAAG, no differences in DNA-binding activity were observed. These results imply that the F109S mutation either is a rare neutral sequence variant, or produces an SRY protein with slightly altered in vivo activity, the resulting sex phenotype depending on the genetic back-ground or environmental factors.This paper is dedicated by G. S. to Professor Ulrich Wolf on the occasion of his 60th birthday     

A detailed study of the periodate oxidation of sialic acids in glycoproteins

Periodate oxidation of terminalN-acetyl- andN-glycoloylneuraminic acid residues in the mucins from edible bird nest substance and pig submandibular gland, respectively, can be carried out under conditions which exclusively give rise to the formation of the C-7 analogues of these sialic acids. In contrast, the C-8 compounds can be obtained in a maximum yield of about 40%. Under identical conditions,N-glycoloylneuraminic acid is oxidized about 1.5 times faster than theN-acetylated derivative. After release of the sialic acids by acid hydrolysis, the characterization of the oxidation products was carried out by TLC, by GLC and GLC-MS of the corresponding pertrimethylsilyl derivatives, and by 500-MHz¹H-NMR spectroscopy. In addition, molar response factors for GLC analysis and extinction coefficients in the orcinol/Fe³⁺/HCl assay were determined.     

Characterisation of neuropeptides of the AKH/RPCH-family from corpora cardiaca of Coleoptera

Summary Extracts of corpora cardiaca from two members of the family Tenebrionidae,Zophobas rugipes andTenebrio molitor, from one member of the Chrysomelidae,Leptinotarsa decemlineata, and from three members of the Scarabaeidae,Pachnoda marginata, P. sinuata andMelolontha hippocastani, were assayed for adipokinetic and hypertrehalosaemic activity in acceptor locusts (Locusta migratoria) and cockroaches (Periplaneta americana), respectively. All corpus cardiacum material tested, except that from the cockchafer,M. hippocastani, gave positive bioassay results. Biological activities of corpus cardiacum extracts from all species investigated can be resolved on reversed-phase high performance liquid chromatography (RP-HPLC). Gland extracts from the two tenebrionid species each show a single peak of biological activity associated with a single peak of UV absorbance having an identical retention time in both species. The two biologically active fractions from the corpora cardiaca of the potato beetle,L. decemlineata, coelute with exogenous (synthetic) hypertrehalosaemic hormones I and II of the American cockroach. The two species of the genusPachnoda contain two active compounds in their glands; compound I of each species is more abundant and elutes just ahead of the (synthetic) hypertrehalosaemic hormone of the cockroachBlaberus discoidalis. The gland material ofM. hippocastani exhibits and absorbance peak with the same retention time as the major peak from thePachnoda-species; however, this peak material does not elicit biological activity in the assays used here. After fractionation by RP-HPLC the main biologically active compounds were subjected to amino acid analyses. All factors are peptidic and contain 8 amino acid residues. The peptides from the tenebrionid species have the amino acid residues Asx₍₂₎, Glx₍₁₎, Ser₍₁₎, Pro₍₁₎, Leu₍₁₎, Phe₍₁₎ and Trp_(i), whereas the main peptide from corpora cardiaca ofP. marginata contains the residues Asx₍₂₎, Glx₍₁₎, Ser₍₁₎, Pro₍₁₎, Tyr₍₁₎, Leu₍₁₎ and Trp₍₁₎. Amino acid composition analyses of the two active fractions fromL. decemlineata reveal the residues Asx₍₂₎, Glx₍₁₎, Ser₍₁₎, Pro₍₁₎, Val₍₁₎, Phe₍₁₎ and Trp₍₁₎ for compound I and Asx₍₁₎, Glx₍₁₎, Thr₍₂₎, Pro₍₁₎, Leu₍₁₎, Phe₍₁₎ and Trp₍₁₎ for compound II.     

The Drosophila PROS-28.1 gene is a member of the proteasome gene family

In the present communication, we report the identification of a new gene family which encodes the protein subunits of the proteasome. The proteasome is a high-M_r complex possessing proteolytic activity. Screening a Drosophila λgt11 cDNA expression library with the proteasome-specific antibody N19-28 we isolated a clone encoding the 28-kDa No. 1 proteasome protein subunit. In accordance with the nomenclature of proteasome subunits in Drosophila, the corresponding gene is designated PROS-28.1, and it encodes an mRNA of 1.1 kb with an open reading frame of 249 amino acids (aa). Genomic Southern-blot hybridization shows PROS-28.1 to be a member of a family of related genes. Analysis of the predicted aa sequence reveals a potential nuclear targeting signal, a potential site for tyrosine kinase and a potential cAMP/cGMP-dependent phosphorylation site. The aa sequence comparison of the products of PROS-28.1 and PROS-35 with the C2 proteasome subunit of rat shows a strong sequence similarity between the different proteasome subunits. The data suggest that at least a subset of the proteasome-encoding genes belongs to a family of related genes (PROS gene family) which may have evolved from a common ancestral PROS gene.     

Genetics of the quantitative Lp(a) lipoprotein trait

The Lp(a) lipoprotein is a complex particle composed of a low density lipoprotein (LDL)-like lipoprotein and the disulfide bonded Lp(a) glycoprotein. The complex represents a quantitative genetic trait. SDS gel electrophoresis under reducing conditions of sera followed by immunoblotting with affinity-purified polyclonal anti-Lp(a) demonstrated inter- and intra-individual size heterogeneity of the glycoprotein with apparent Mr in the range 400-700kDa. According to their relative mobilities compared to apo B-100 the Lp(a) patterns were categorized into phenotypes F, B, S1, S2, S3 und S4 and into the respective double-band phenotypes. This size heterogeneity seems to be controlled by multiple alleles designated LpF, LpB, LpS1, LpS2, LpS3, LpS4 and a null allele (LpO) at a single locus. Phenotype frequencies observed in 441 unrelated subjects were in good agreement with those expected from the genetic hypothesis. Comparison of Lp(a) lipoprotein concentrations in the different phenotypes revealed a highly significant association of phenotypes B, S1 and S2 with high, and phenotypes S3 und S4 with intermediate Lp(a) concentrations. A third mode is represented by the null phenotype were no Lp(a) band is detected upon immunoblotting and Lp(a) lipoprotein is low or absent. We conclude that the same gene locus is involved in determining Lp(a) glycoprotein phenotype and Lp(a) lipoprotein concentrations in plasma. This major gene seems to be the Lp(a) glycoprotein structural gene locus.     

Genetics of the quantitative Lp(a) lipoprotein trait

Summary Lp(a) glycoprotein exhibits an apparent size polymorphism that is associated with genetically controlled Lp(a) lipoprotein concentrations in plasma (Utermann et al. 1988). We have tested the hypothesis that this polymorphism is genetically controlled by studying 15 matings with a total of 44 offspring. This confirmed our conclusion that Lp(a) types are controlled by a series of codominant alleles Lp^F, Lp^B, Lp^S1, Lp^S2, Lp^S3 and Lp^S4 and by a null allele Lp^o. Together with the data from the accompanying paper this indicates that the structural gene for the Lp(a) protein is the major gene locus determining Lp(a) lipoprotein concentrations in plasma.