Digging Deep for the Heritage Fund: Why the Right Fund for Alberta Pays Dividends Long After Oil Is Gone

Albertans have long been aware that while their provincial government has shown a lack of consistent discipline in investing oil royalty revenues in the Alberta Heritage Savings Trust Fund, the Norwegians have been showing oil-rich jurisdictions just how effectively saving can be done. While Alberta’s fund was established in the mid-1970s, more than a decade before Norway began its national savings program, the Norwegian fund was worth more than $900 billion as of the beginning of 2014; Alberta’s is worth roughly$15 billion today, revealing the province’s inability to stick with firm, routine contribution commitments, and its occasional habit of using the fund’s earnings to cover spending priorities. But while many economists, politicians and pundits from both the left and right have long pointed to Norway as the model for Alberta to follow, it would in fact be wrong for Alberta to mimic Norway’s strategy. Indeed, the right plan for Alberta can set the province up in better shape for the future than even Norway will be. The Norway approach will inevitably prove unsustainable. As it is, Norway deposits all resource revenue into its fund, which then distributes a dividend to the government every year worth four per cent of the fund’s wealth. As the fund grows, so to does the size of the dividend. Yet, as wealth is converted from belowground assets (oil) to aboveground assets (cash and investments), the belowground wealth becomes gradually but inevitably depleted. At some point, all of Norway’s oil wealth will have been converted into aboveground assets, and the dividend will eventually have to be adjusted downward. A more sustainable approach, and one that Alberta should pursue, is one where the dividend is a falling proportion of fund assets. In other words, the province will want to calculate an appropriate dividend that is a fraction not just of the size of the financial fund (aboveground), but a constant fraction of total wealth — the value of the belowground assets and the aboveground asset portfolio. This ensures that the dividend grows in line with GDP. What is feasible for Alberta is an ongoing resource dividend equivalent to 30 per cent of government revenue. In order to achieve that goal, the province will have to build the fund such that it is worth the equivalent of 40 per cent of provincial GDP by 2030, 100 per cent of GDP by 2050, and 165 per cent of GDP in the year 2100. This means that within just the next 16 years, the Heritage Fund will need to be worth $200 billion in order to achieve its first benchmark — more than thirteen times its current size. Note the differences here with the recommendations made by the Alberta Financial Investment and Planning Advisory Commission (the Mintz commission), which advocated saving a fixed percentage of Alberta’s resource revenue each year, and set a 2030 target at just half that size.But what this plan does have in common with the Mintz commission’s recommendations is that it requires the Alberta government to finally become serious about preparing itself to preserve wealth for future generations through the use of disciplined and meaningful investment in the resource fund. A serious investment approach also must mean that the fund should not be used as a source of capital investment to favour businesses in the province; Albertans have perfectly good access to capital markets, and worthwhile investments can and should compete for capital funds on their merits, not their location. Quite the contrary, a properly diversified Heritage Fund should be investing largely, if not entirely, outside the province. Most importantly, of course, is that Albertans need to insist that their government commit to a strategic plan for investing its oil revenue. Alberta can create a better fund strategy than Norway’s for ensuring economic sustainability through future generations, but first it must finally get serious about doing it

In Vivo Models for the Evaluation of Antisense Oligonucleotides in Skin

Here, we describe an in vivo model in which antisense oligonucleotides were preclinically evaluated in reconstituted patient and healthy control skin. The aim was to investigate the effect of antisense oligonucleotides upon local or systemic administration. This allows for clinically relevant evaluation of antisense oligonucleotides in an in vivo setting. In this model, primary human keratinocytes and fibroblasts were placed into silicone grafting chambers, implanted onto the back of athymic nude mice. After sufficient cells were expanded, within a few weeks, human skin grafts were generated with a high success rate. These mice bearing grafts were subsequently treated with antisense oligonucleotides targeting exon 105 of the COL7A1 gene which encodes type VII collagen. Patients completely lacking expression of type VII collagen develop severe blistering of skin and mucosa, i.e., recessive dystrophic epidermolysis bullosa. In this chapter, we describe the in vivo model used for the preclinical evaluation of antisense oligonucleotides as therapeutic approach for recessive dystrophic epidermolysis bullosa

In Vitro Models for the Evaluation of Antisense Oligonucleotides in Skin

The genodermatosis dystrophic epidermolysis bullosa (DEB) is caused by mutations in the COL7A1 gene which encodes type VII collagen (C7). In the cutaneous basement membrane zone, C7 secures attachment of the epidermal basal keratinocyte to the papillary dermis by means of anchoring fibril formation. The complete absence of these anchoring fibrils leads to severe blistering of skin and mucosa upon the slightest friction and early mortality. To date, although preclinical advances toward therapy are promising, treatment for the disease is merely symptomatic. Therefore, research into novel therapeutics is warranted.Antisense oligonucleotide (ASO)-mediated exon skipping is such a therapy . Clinical examination of naturally occurring exon skipping suggested that this mechanism could most likely benefit the most severely affected patients. The severe form of DEB is caused by biallelic null mutations. Exon skipping aims to bind an ASO to the mutated exon of the pre-mRNA in the cell nucleus. Thereby, the ASO inhibits the recognition of the mutated exon by the splicing machinery, and as a result, the mutated exon is spliced out from the mRNA with its surrounding introns, i.e., it is skipped. Here, we describe in vitro methods to evaluate ASO-mediated exon skipping in a preclinical setting

Unsteady Ekman--Stokes dynamics: implications for surface-wave induced drift of floating marine litter

We examine Stokes drift and wave‐induced transport of floating marine litter on the surface of a rotating ocean with a turbulent mixed layer. Due to Coriolis‐Stokes forcing and surface wave stress, a second‐order Eulerian‐mean flow forms, which must be added to the Stokes drift to obtain the correct wave‐induced Lagrangian velocity. We show that this wave‐driven Eulerian‐mean flow can be expressed as a convolution between the unsteady Stokes drift and an “Ekman‐Stokes kernel.” Using this convolution, we calculate the unsteady wave‐driven contribution to particle transport. We report significant differences in both direction and magnitude of transport when the Eulerian‐mean Ekman‐Stokes velocity is included

Experimental Observation of Modulational Instability in Crossing Surface Gravity Wavetrains

The coupled nonlinear Schrödinger equation (CNLSE) is a wave envelope evolution equation applicable to two crossing, narrow-banded wave systems. Modulational instability (MI), a feature of the nonlinear Schrödinger wave equation, is characterized (to first order) by an exponential growth of sideband components and the formation of distinct wave pulses, often containing extreme waves. Linear stability analysis of the CNLSE shows the effect of crossing angle, θ, on MI, and reveals instabilities between 0◦ < θ < 35◦, 46◦ < θ < 143◦, and 145◦ < θ < 180◦. Herein, the modulational stability of crossing wavetrains seeded with symmetrical sidebands is determined experimentally from tests in a circular wave basin. Experiments were carried out at 12 crossing angles between 0◦ ≤ θ ≤ 88◦, and strong unidirectional sideband growth was observed. This growth reduced significantly at angles beyond θ ≈ 20◦, reaching complete stability at θ = 30–40◦. We find satisfactory agreement between numerical predictions (using a time-marching CNLSE solver) and experimental measurements for all crossing angles

Probing metal ion binding and conformational properties of the colicin E9 endonuclease by electrospray ionization time-of-flight mass spectrometry

Nano-electrospray ionization time-of-flight mass spectrometry (ESI-MS) was used to study the conformational consequences of metal ion binding to the colicin E9 endonuclease (E9 DNase) by taking advantage of the unique capability of ESI-MS to allow simultaneous assessment of conformational heterogeneity and metal ion binding. Alterations of charge state distributions on metal ion binding/release were correlated with spectral changes observed in far- and near-UV circular dichroism (CD) and intrinsic tryptophan fluorescence. In addition, hydrogen/deuterium (H/D) exchange experiments were used to probe structural integrity. The present study shows that ESI-MS is sensitive to changes of the thermodynamic stability of E9 DNase as a result of metal ion binding/release in a manner consistent with that deduced from proteolysis and calorimetric experiments. Interestingly, acid-induced release of the metal ion from the E9 DNase causes dramatic conformational instability associated with a loss of fixed tertiary structure, but secondary structure is retained. Furthermore, ESI-MS enabled the direct observation of the noncovalent protein complex of E9 DNase bound to its cognate immunity protein Im9 in the presence and absence of Zn2+. Gas-phase dissociation experiments of the deuterium-labeled binary and ternary complexes revealed that metal ion binding, not Im9, results in a dramatic exchange protection of E9 DNase in the complex. In addition, our metal ion binding studies and gas-phase dissociation experiments of the ternary E9 DNase-Zn2+-Im9 complex have provided further evidence that electrostatic interactions govern the gas phase ion stability

Structure-function relationships of E-type endonuclease colicins

Colicin cytotoxicity can take various guises, the most remarkable being degradation of bacterial DNA, requiring the 60 kDa toxin to translocate its C-terminal, 15 kDa enzymatic domain across two membrane boundaries in order to reach the cytoplasm. Current theories concerning colicin translocation envisage that conformational changes, and partly unfolding, are required before the toxin can enter the cell. To date, four colicin DNases have been identified, i.e. E2, E7, E8 and E9, which share high sequence homology. In our study nano-ESI-MS was used to gain insights into metal binding and conformational properties of these metalloproteins. Thermostability and intrinsic trypthophan accessibility measurements were performed and correlated with our ESI-MS data. ESI-MS analysis of each DNase revealed substantial different folding properties even though they are highly homologous. In the absence of zinc ions, which bind with nM affinity to the enzyme, the E7 DNase mass spectra were dominated by a loosely packed ('unfolded') population of protein conformers, while mass spectra for apo-E8 DNase represented mostly 'folded' conformers. The presence of zinc ions resulted in increased conformational stability for all proteins thereby adopting states that are more folded and uniform. Taken together, the present study demonstrates that ESI-MS is sensitive to changes in the conformational stability in the four DNases in a manner consistent with experimental data deduced from calorimetry and intrinsic Trp fluorescence quenching