Studies on the primary sequence requirements for PKC-alpha, -beta 1 and -gamma peptide substrates.

The substrate specificity of purified PKC-alpha, -beta and -gamma has been investigated. A series of synthetic peptides based upon the sequence surrounding serine-7 in glycogen synthase were generated and used to determine the basic residue requirements of these PKC isotypes. While PKC-alpha and -beta are indistinguishable in their phosphorylation of these peptides, PKC-gamma shows a distinct specificity profile for these synthetic substrates.     

Interaction between corticosteroid binding globulin and activated leukocytes in vitro

The interaction between human corticosteroid binding globulin and activated leukocytes is restricted to the granulocyte population, and is characterized by specific proteolytic cleavage of corticosteroid binding globulin which markedly reduces its steroid binding activity. A direct interaction between corticosteroid binding globulin and the activated cells appears to enhance this event, and does not involve cellular internalization of corticosteroid binding globulin or its proteolytic degradation products, which resemble those obtained after incubation of corticosteroid binding globulin with neutrophil elastase. These data suggest that corticosteroid binding globulin interacts with elastase on the surface of activated neutrophils, and may promote glucocorticoid delivery to these cells during inflammation.     

Solitary angiomyolipoma of the liver. Report of a case initially examined by fine needle aspiration biopsy

Transabdominal fine needle aspiration biopsy of a solitary space-occupying lesion in the liver produced smears containing irregular bundles of smooth muscle cells with granular or fibrillary cytoplasm and slightly pleomorphic nuclei. In a few bundles, aggregates of mature fat cells were present, which is characteristic for an angiomyolipoma. Histologic examination of the resected mass showed it to be a solitary angiomyolipoma of the liver. The diagnosis was further confirmed by immunohistochemical and electron microscopic studies.     

Regional localization of the genes for human HEXB. PGK, GALA. HPRT, G6PD by somatic cell hybridization

Twenty independent man-mouse (Cl1D,LA/TK-, HPRT-) and man-hamster (CH,HPRT-) hybrids using female human cells with balanced reciprocal translocation XX,t(X;5)(q21;q11) were analyzed for human genes localized on chromosome 5 (HEXB), on chromosome X (PGK, GALA, HPRT, G6PD) and for the different chromosomes in relation with the balanced reciprocal translocation (chr.5, chr.5q-, chr.Xq+, chr.X). The different results obtained indicate that the genes for human markers HEXB, PGK are on Xq+, and that the genes for human markers GALA, G6PD are on 5q-. These data implicate finally the following localizations: HEXB on 5q11 leads to 5qter; PGK on Xq21 leads to Xpter; GALA, HPRT, G6PD on Xq21 leads to Xqter.     

Comparative ultrastructure of Mycobacterium leprae and Mycobacterium lepraemurium cell envelopes.

The structural properties of the cell envelopes of Mycobacterium leprae and Mycobacterium lepraemurium were investigated by freeze-fracture, freeze-etching, and negative-staining techniques. Freeze-fracture split the cell wall and exposed the internal features of the peptidoglycolipid mycosidic filamentous network. The cell membrane was also split into two asymmetric faces. The external fracture face was characterized by linear arrays of intramembranous particles, whereas the protoplasmic fracture face showed randomly distributed clusters of particulate entities. Comparative analysis of the ultrastructural features observed in M. leprae and M. lepraemurium indicated that the organization of the cell envelope in these two species differed particularly with respect to the amount and complexity of the superficial peptidoglycolipid and mycosidic integument, which is poorly developed in the mycobacterium responsible for human disease.     

Etude comparee des proprietes physico-chimiques des mannanes de neuf levures

In order to correlate and compare the antigenic relationships observed between nine yeast strains, we have studied their major antigenic determinant represented by the mannans. This material is a constituent of their cell.The compounds that we have isolated are, in reality, glycopeptides. All their polysaccharide fractions consist of mannose only — except for those of the compounds that we have isolated of R. glutinis and C. lipolytica. All these polysaccharides have very close ramified structures; the only one that seems to be very different is that of R. glutinis, and this is in agreement with the antigenic properties of that yeast.The peptidic fractions of these glycopeptides are rich in threonine, serine and aspartic acid and it is very likely that these amino acids make the link with the polysaccharide fraction. The quantity of these amino acids seem to be affected by the conditions of culture of the yeasts, but not their presence or absence.     

A three-step method for isolating a few to several hundred milligrams of protein

An operationally simple general protein isolation method was devised from three previously available separation tools, and was tested by application to two demanding fractionation problems and for yield. One test system was the isolation by gel electrofocusing of two model proteins with pI values of 4.6 and 4.8, bovine serum albumin and ovalbumin, with a load of 220 mg each. The other test was the isolation of 10 mg of human growth hormone isohormone B from a mixture of closely migrating other isohormones. The three-step procedure comprises of: (1) separation into zones of homogeneous protein by gel electrofocusing; (2) excision of the zones of homogeneous protein from the gel followed by concentration of the protein to a small volume of solution by means of Steady-State Stacking; (3) purification from polyacrylamide-like contaminants and non-volatile buffers by gel filtration followed by lyophilization. The average overall recovery was 70--80%.     

Les corps myéloïdes de l'épithelium pigmentaire rétinien

Résumé La morphologie (forme, taille, structure) des corps myéloïdes de l'épithelium pigmentaire rétinien est décrite, ainsi que leur répartition chez les différentes classes de vertébrés. On définit les critères d'identification de ces corps: Ils ne sont jamais limités par une membrane, sont en continuité avec le reticulum endoplasmique lisse, sont formés de saccules aplatis, liés deux à deux par des complexes de jonction. Ils établissent des relations de continuité avec la membrane nucléaire. Les confusions entre corps myéloïdes et diverses autres structures (phagosomes en particulier) sont discutées. Il n'existe pas de corps myéloïdes dans la rétine des Mammifères.

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Myeloid bodies of the retinal pigment epitheliumI. Distribution, morphology and connections with cytoplasmic organels

Summary The morphology (shape, dimensions, structure) of the myeloid bodies of the retinal pigment epithelium and their distribution through several classes of vertebrates is described. The criteria of identity of these bodies are defined: They are never membrane-bounded, they are in direct continuity with the smooth endoplasmic reticulum, they are made of flattened discs linked two and two by junction complexes. They are in direct relation with the nuclear membrane. The confusion between myeloïd bodies and other structures, like phagosomes, is discussed. The retina of Mammals does not contain myeloïd bodies.

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