Landfast sea-ice and platelet-layer thickness and conductivity of Atka Bay, Antarctica, December 2012

Ice shelves strongly impact coastal Antarctic sea-ice and the associated ecosystem through the formation of a sub-sea-ice platelet layer. Although progress has been made in determining and understanding its spatio-temporal variability based on point measurements, an investigation of this phenomenon on a larger scale remains a challenge due to logistical constraints and a lack of suitable methodology. In this study, we applied a laterally-constrained Marquardt-Levenberg inversion to a unique multi-frequency electromagnetic (EM) induction sounding dataset obtained on the landfast sea ice of Atka Bay, eastern Weddell Sea, in 2012. In addition to consistent fast-ice thickness and -conductivities along > 100 km transects; we present the first comprehensive, high resolution platelet-layer thickness and -conductivity dataset recorded on Antarctic sea ice. The reliability of the algorithm was confirmed by using synthetic data, and the inverted platelet-layer thicknesses agreed within the data uncertainty to drill-hole measurements. Ice-volume fractions were calculated from platelet-layer conductivities, revealing that an older and thicker platelet layer is denser and more compacted than a loosely attached, young platelet layer. The overall platelet-layer volume below Atka Bay fast ice suggests that the contribution of ocean/ice-shelf interaction to sea-ice volume in this region is even higher than previously thought. This study also implies that multi-frequency EM induction sounding is an effective approach in determining platelet layer volume on a larger scale than previously feasible. When applied to airborne multi-frequency EM, this method could provide a step towards an Antarctic-wide quantification of ocean/ice-shelf interaction.

Field measurements of the atmosphere, ocean, sea ice and sub-ice platelet layer at Atka Bay in 2013

Ice shelves strongly interact with coastal Antarctic sea ice and the associated ecosystem by creating conditions favourable to the formation of a sub-ice platelet layer. The close investigation of this phenomenon and its seasonal evolution remain a challenge due to logistical constraints and a lack of suitable methodology. In this study, we characterize the seasonal cycle of Antarctic fast ice adjacent to the Ekström Ice Shelf in the eastern Weddell Sea. We used a thermistor chain with the additional ability to record the temperature response induced by cyclic heating of resistors embedded in the chain. Vertical sea-ice temperature and heating profiles obtained daily between November 2012 and February 2014 were analyzed to determine sea-ice and snow evolution, and to calculate the basal energy budget. The residual heat flux translated into an ice-volume fraction in the platelet layer of 0.18 ± 0.09, which we reproduced by a independent model simulation and agrees with earlier results. Manual drillings revealed an average annual platelet-layer thickness increase of at least 4m, and an annual maximum thickness of 10m beneath second-year sea ice. The oceanic contribution dominated the total sea-ice production during the study, effectively accounting for up to 70% of second-year sea-ice growth. In summer, an oceanic heat flux of 21 W/m**2 led to a partial thinning of the platelet layer. Our results further show that the active heating method, in contrast to the acoustic sounding approach, is well suited to derive the fast-ice mass balance in regions influenced by ocean/ice-shelf interaction, as it allows sub-diurnal monitoring of the platelet-layer thickness.

The inositol polyphosphate 4-phosphatase forms a complex with phosphatidylinositol 3-kinase in human platelet cytosol

Inositol polyphosphate 4-phosphatase (4-phosphatase) is an enzyme that catalyses the hydrolysis of the 4-position phosphate from phosphatidylinositol 3,4-bisphosphate [PtdIns(3,4)P2]. In human platelets the formation of this phosphatidylinositol, by the actions of phosphatidylinositol 3-kinase (PI 3-kinase), correlates with irreversible platelet aggregation. We have shown previously that a phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase forms a complex with the p85 subunit of PI 3-kinase. In this study we investigated whether PI 3-kinase also forms a complex with the 4-phosphatase in human platelets. Immunoprecipitates of the p85 subunit of PI 3-kinase from human platelet cytosol contained 4-phosphatase enzyme activity and a 104-kDa polypeptide recognized by specific 4-phosphatase antibodies. Similarly, immunoprecipitates made using 4-phosphatase-specific antibodies contained PI 3-kinase enzyme activity and an 85-kDa polypeptide recognized by antibodies to the p85 adapter subunit of PI 3-kinase. After thrombin activation, the 4-phosphatase translocated to the actin cytoskeleton along with PI 3-kinase in an integrin- and aggregation-dependent manner. The majority of the PI 3-kinase/4-phosphatase complex (75%) remained in the cytosolic fraction. We propose that the complex formed between the two enzymes serves to localize the 4-phosphatase to sites of PtdIns(3,4)P2 production.

Platelet signal transduction defect with Gα subunit dysfunction and diminished Gαq in a patient with abnormal platelet responses

G proteins play a major role in signal transduction upon platelet activation. We have previously reported a patient with impaired agonist-induced aggregation, secretion, arachidonate release, and Ca2+ mobilization. Present studies demonstrated that platelet phospholipase A2 (cytosolic and membrane) activity in the patient was normal. Receptor-mediated activation of glycoprotein (GP) IIb-IIIa complex measured by flow cytometry using antibody PAC-1 was diminished despite normal amounts of GPIIb-IIIa on platelets. Ca2+ release induced by guanosine 5′-[γ-thio]triphosphate (GTP[γS]) was diminished in the patient’s platelets, suggesting a defect distal to agonist receptors. GTPase activity (a function of α-subunit) in platelet membranes was normal in resting state but was diminished compared with normal subjects on stimulation with thrombin, platelet-activating factor, or the thromboxane A2 analog U46619. Binding of 35S-labeled GTP[γS] to platelet membranes was decreased under both basal and thrombin-stimulated states. Iloprost (a stable prostaglandin I2 analog) -induced rise in cAMP (mediated by Gαs) and its inhibition (mediated by Gαi) by thrombin in the patient’s platelet membranes were normal. Immunoblot analysis of Gα subunits in the patient’s platelet membranes showed a decrease in Gαq (<50%) but not Gαi, Gαz, Gα12, and Gα13. These studies provide evidence for a hitherto undescribed defect in human platelet G-protein α-subunit function leading to impaired platelet responses, and they provide further evidence for a major role of Gαq in thrombin-induced responses.