Hemispheric asymmetry in ocean change and the productivity of ecosystem sentinels.

Climate change and other human activities are causing profound effects on marine ecosystem productivity. We show that the breeding success of seabirds is tracking hemispheric differences in ocean warming and human impacts, with the strongest effects on fish-eating, surface-foraging species in the north. Hemispheric asymmetry suggests the need for ocean management at hemispheric scales. For the north, tactical, climate-based recovery plans for forage fish resources are needed to recover seabird breeding productivity. In the south, lower-magnitude change in seabird productivity presents opportunities for strategic management approaches such as large marine protected areas to sustain food webs and maintain predator productivity. Global monitoring of seabird productivity enables the detection of ecosystem change in remote regions and contributes to our understanding of marine climate impacts on ecosystems.

Characterization of the processed form of a ubiquitous protein displaying a variable membrane organization in erythroid cells.

We recently identified a group of proteins that are present in all hematopoietic cells but are organized in the cell membrane of erythrocytes in a lineage-specific fashion (Blood 61:803, 1983). One of these polypeptides has a mol wt of approximately 37,000 (p37T) when translated in vitro from messenger RNA (mRNA) extracted from the erythroleukemic K562 cell line. The membrane-associated form of the p37 translation product has been analyzed in detail here. When detergent lysates prepared from biosynthetically labeled K562 cells were reacted with an antiserum containing anti-p37T antibodies, one of the proteins immunoprecipitated had a nominal mol wt of 36,000 to 37,000 (p37M). Several results suggest that this protein is homologous to the p37 translation product: (1) the protein, like the mRNA coding for the p37 translation product, was expressed in cell lines with diverse differentiated phenotypes; (2) the antigenic determinant(s) on p37M and p37T are oriented to the inner surface of the erythrocyte membrane while being oriented to the outer surface of erythroleukemic cells; and (3) one-dimensional peptide maps show homology between p37M and p37T. P37M does not appear to possess an N-terminal leader sequence that is proteolytically cleaved as the molecule is inserted into the membrane. In addition, p37M is not glycosylated.

Reorientation of membrane polypeptides during erythrocyte maturation.

Messenger RNA extracted from the erythroleukemic cell line K562 was translated in vitro and the translation products reacted with an antiserum raised against human erythrocyte ghosts. Polypeptides immunoprecipitated by the antiserum were characterized by SDS-polyacrylamide gel electrophoresis and fluorography. The antiserum immunoprecipitated polypeptides with nominal molecular weights of 37,000 (p37), 20,000 (p20), 19,000 (p19), 18,000 (p18), 14,000 (p14), 13,000 (p13), and 11,000 (p11) daltons. Since the antiserum was raised against antigenic determinants present on both the inner and outer surface of the red cell membrane, differential absorption of antiserum with intact red cells, or ghosts, was used to localize the translation products to the inner or outer membrane surface. Absorption was also used to determine if any of the immunoprecipitated translation products represented membrane markers for the erythroid lineage. Absorption of the antiserum with red cell ghosts removed all antibodies reacting with in vitro translation products. Absorption with intact cells from various lineages removed anti-p20 antibodies and did not absorb anti-p19 or anti-p18 antibodies. Absorption with intact cells from all lineages except mature erythrocytes absorbed anti-p37, anti-p14, and anti-p13 antibodies, suggesting that these antigens are expressed on the outer membrane surface. Mature erythrocytes were incapable of absorbing these antibody populations, suggesting a lineage-specific reorientation of these antigens in the membrane during erythropoiesis.