A sea change in our view of overturning in the subpolar North Atlantic.

To provide an observational basis for the Intergovernmental Panel on Climate Change projections of a slowing Atlantic meridional overturning circulation (MOC) in the 21st century, the Overturning in the Subpolar North Atlantic Program (OSNAP) observing system was launched in the summer of 2014. The first 21-month record reveals a highly variable overturning circulation responsible for the majority of the heat and freshwater transport across the OSNAP line. In a departure from the prevailing view that changes in deep water formation in the Labrador Sea dominate MOC variability, these results suggest that the conversion of warm, salty, shallow Atlantic waters into colder, fresher, deep waters that move southward in the Irminger and Iceland basins is largely responsible for overturning and its variability in the subpolar basin.

Lactic acid buffering by bone and shell in anoxic softshell and painted turtles.

We tested two hypotheses: first, that the inferior anoxia tolerance of the softshell turtle, Apalone spinifera, compared to the western painted turtle, Chrysemys picta bellii, is related to its less mineralized shell, and second, that turtle bone, like its shell, stores lactate during prolonged anoxia. Lactate concentrations of blood, hindlimb bone, and shell were measured on normoxic Apalone and Chrysemys and after anoxic submergence at 10 degrees C for 2 and 9 d, respectively. Blood and shell concentrations of Ca(2+), Mg(2+), Na(+), K(+), and inorganic phosphate (P(i); for shell only) were also measured. Because a preliminary study indicated lactate distribution in Chrysemys throughout its skeleton during anoxia at 20 degrees C, we used hindlimb bones as representative skeletal samples. Apalone shell, though a similar percentage of body mass as Chrysemys shell, had higher water content (76.9% vs. 27.9%) and only 20%-25% as much Ca(2+), Mg(2+), CO(2), and P(i). When incubated at constant pH of 6.0 or 6.5, Apalone shell powder released only 25% as much buffer per gram wet weight as Chrysemys shell. In addition, plasma [Ca(2+)] and [Mg(2+)] increased less in Apalone during anoxia at an equivalent plasma lactate concentration. Lactate concentrations increased in the shell and skeletal bone in both species. Despite less mineralization, Apalone shell took up lactate comparably to Chrysemys. In conclusion, a weaker compensatory response to lactic acidosis in Apalone correlates with lower shell mineralization and buffer release and may partially account for the poorer anoxia tolerance of this species.

The human H1 histone gene FNC16 is functionally expressed in proliferating HeLa S3 cells and is down-regulated during terminal differentiation in HL60 cells.

The human H1 histone gene FNC16 resides in a 2.7-kb EcoRI fragment present in a histone gene cluster that also contains one copy of each of the core (H2A, H2B, H3, and H4) histone genes. The cap site for FNC16 H1 mRNA is located 58 nucleotides upstream of the ATG translational start codon, and S1 nuclease protection analysis clearly distinguishes between correctly initiated FNC16 transcripts and transcripts from other nonidentical H1 histone genes. We have observed, using S1 analysis, that the FNC16 H1 histone gene is expressed in a replication-dependent manner in HeLa cells and is expressed in proliferating, but down-regulated in differentiated, HL60 cells. Similar results were found in HeLa S3 and HL60 cells for the cell cycle-dependent human H4 histone gene FO108. Nuclear extracts derived from HeLa S3 cells are capable of directing FNC16 H1 histone gene transcription in vitro. This finding is consistent with previous work that established at least two sites for protein-DNA interaction in vitro in the proximal promoter region of this gene. We have observed a difference in the extent to which the FNC16 H1 histone gene is expressed in HeLa S3 and proliferating HL60 cells, which suggests that this H1 gene is differentially regulated in various cell types. Although results reported for a potentially identical human H1 histone gene designated Hh8C (LaBella, F., Zhong, R., and Heintz, N. (1988) J. Biol. Chem. 263, 2115-2118) support differential regulation of human H1 genes in various cell types, their observations that the Hh8C gene is not expressed in HeLa cells and that the restriction patterns differ indicate that FNC16 and Hh8C are different H1 genes.

Genetic engineering of an H-2Dd/Q10b chimeric histocompatibility antigen: purification of soluble protein from transformant cell supernatants.

We have constructed a recombinant class I gene in which 5' sequences of H-2Dd are linked to the 3' half of a Qa subregion gene, Q10b. This hybrid gene would be expected to direct the synthesis of a protein containing the N and C1 domains of H-2Dd covalently linked to the C2 domain of the secreted, nonpolymorphic, Q10b antigen. Following DNA-mediated gene transfer into mouse L cells, transformants were analyzed by radiolabeling and immunoprecipitation. These cells secreted a molecule reactive with anti-H-2Dd monoclonal antibodies that identify epitopes on the N and C1 domains as well as with an anti-Q10 carboxyl-terminal peptide antiserum. The H-2Dd-derived antigen is associated with beta 2-microglobulin and is readily purified in milligram amounts from culture supernatants by immunoaffinity chromatography.