Localization of blood coagulation factors in the germinal centers of human Peyer's patches.

The immunohistochemical distribution of 15 blood coagulation factors in the germinal centers (GCs) of human Peyer's patches (PPs) was studied. Although factor VIII, active alpha-thrombin, and fibrinogen were hardly evident in the GCs, the majority of coagulation factors, such as kallikrein, high-molecular-weight kininogen, factors XII, X, IX, VII, V, XIIIa and XIIIb, prothrombin, anti-thrombin III and inactive alpha-thrombin were found, showing a lace-like staining pattern similar to that obtained with a monoclonal antibody, R4/23, specific for follicular dendritic cells (FDCs) in the GCs. By immunoelectron microscopy, positive reactions for factor X and XIIIa were found on the surfaces of FDCs, GC cells, and/or in the intercellular spaces of GCs, being especially marked on the surface of the labyrinth-like structure of FDCs. It is concluded that a majority of coagulation factors are localized in the GCs of human PPs. Furthermore, it is suggested that some of these coagulation factors have a close topographical relationship with FDCs.     

The cDNA Sequence of NS3-Glycoprotein from Brassica campestris and its Homology to Related Proteins

A cDNA clone encoding NS₃-glycoprotein was isolated from stigmasof Brassica campestris. NS-glycoproteins correspond to the SLRI-glycoproteinsof B. oleracea and are highly conserved within the species.These data suggest that the NS-glycoproteins may play a rolein discrimination between species in the fertilization systemof Brassica. (Received September 4, 1992; Accepted November 9, 1992)     

Primary cilia-dependent lipid raft/caveolin dynamics regulate adipogenesis

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Establishment of consomic strains derived from A/J and SM/J mice for genetic analysis of complex traits

Consomic strains, in which one chromosome is derived from a donor strain and the other chromosomes are derived from the recipient strain, provide a powerful tool for the dissection of complex genetic traits. In this study we established ten consomic strains (A-2^SM, A-6^SM, A-11^SM, A-12^SM, A-13^SM, A-15^SM, A-17^SM, A-18^SM, A-19^SM, A-Y^SM) using the SM/J strain as the donor and the A/J strain as the recipient; these are the parental strains of a set of SMXA recombinant inbred (RI) strains that we had developed previously. We analyzed body weights and blood lipid levels in the consomic and parental strains. The mean values for each trait showed a continuous range of variation in the consomic strains suggesting that they are controlled by multiple genes. We previously identified suggestive QTLs for body weight on chromosome 6 in SMXA RI strains and (SM/J × A/J)F₂ mice. The observation that the A-6^SM consomic strain had a significantly lower mean body weight than the A/J strain supports the presence of this QTL on chromosome 6. Similarly, the higher blood triglyceride level in the A-11^SM strain shows the existence of a previously mapped QTL on chromosome 11, and the A-12^SM strain provides evidence of a QTL for blood total cholesterol level on chromosome 12. These consomic strains, along with the previously developed set of SMXA RI strains from A/J and SM/J mice, offer an invaluable and powerful resource for the analysis of complex genetic traits in mice.

     

Vitelline-coat lysin: Comparison of lysins among three species in the genus Tegula

Vitelline-coat lysins from two species of marine mollusc of the genus Tegula, Tegula lischkei and Tegula sp., were purified and their properties compared with those of Tegula pfeifferi. Cross-reaction tests among these three species proved that the lysin action on the vitelline coat was species specific. Each of the lysins from these three species is a single, basic polypeptide with a molecular weight of 16000-17000 and an isoelectric point of pH 10.5. All of them share a common antibody recognition site(s) for the anti-T. pfeifferi lysin antibody. Their amino acid sequences were analyzed using intact lysins and peptides separated by reverse phase high-performance liquid chromatography after V8 proteinase digestion. The amino acid sequences of the N-terminus (Nos 1-66) from the three species showed 98% homology, and those of the C-terminus (Nos 91-118) showed 89% homology. It was concluded that the species specificity of the vitelline coat lysin appears to be determined by a sequence of 24 residues (Nos 67-90) in the middle region of the molecule.     

A Study on Spin-Labelled Oligonucleotide Synthesis and its Electron Spin Resonance Behavior in Solution

An oligonucleotide spin-labelled with 4-amino-2,2,6,6-tetramethylpiperidine-N-oxyl (4-amino-TEMPO) at the internucleotide bond (d-Tp(L)TpTpTpT) prepared by oxidation of the pentanucleotide containing the H-phosphonate diester (d-Tp(H)TpTpTpT) in the presence of 4-amino-TEMPO, was separated and identified by high-performance, reverse-phase liquid chromatography combined with detection by electron spin resonance spectroscopy. This spin-labelled oligonucleotide produced a triplet with the slightly broadened M₁ = — I ESR component, while a triplet with almost equal intensities was obtained from the spin-label. The M₁ = —1 component from the labelled oligonucleotide was further broadened in the presence of poly(A) which forms a complementary double strand with this molecule.     

Isolation of pertussis toxin subunit proteins by reverse-phase high-performance liquid chromatography and reconstitution of the holotoxin molecule

Reverse-phase high-performance liquid chromatography on a column of trimethylsilylated silica gel (TSK-TMS 250) was utilized for the isolation of the subunit proteins of pertussis toxin (PT). Recovery up to 95% was obtained for each of the five distinct subunits with a high degree of homogeneity as revealed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. None of the individual subunit proteins exhibited PT-related leukocytosis-promoting activity or the ability to bind haptoglobin; however, these activities were partially restored when an equimolar mixture of the isolated subunit in 6 M guanidine-HCl was diluted from this chaotropic agent. The complex macromolecule subsequently isolated from the mixture displayed subunit composition and biological activities indistinguishable from those of native PT, indicating that the toxin molecule had been reassembled.