The Politics of News Media

Michael Parenti, author of fourteen books and many essays for a variety of newspapers and magazines, is considered one of the nation\u27s leading progressive speakers. This talk was delivered at the Sixth Annual Media Studies Symposium at Sacred Heart University on March 26, 2000

The corporate university: An e-interview with Dave Hill, Alpesh Maisuria, Anthony Nocella, and Michael Parenti

Since the neo-liberal turn, corporate investment in universities has accelerated as the withdrawal of government funding, among other factors, has further exposed universities to market forces. While this process offers numerous benefits for corporations and wealthy individuals, it has been mostly detrimental for students, educators, and the public at large. In this interview, international scholars Dave Hill, Alpesh Maisuria, Anthony Nocella, and Michael Parenti broadly explain why corporations have been aggressively investing in universities. They address the numerous ways that corporate involvement in university activity negatively impacts academic freedom, research outcomes, and the practice of democracy. The interview ends on a hopeful note by presenting examples of resistance against corporate influence. Their analyses focus primarily on the United States, United Kingdom, and Canada

Bacillus thuringiensis toxin inhibits K+-gradient-dependent amino acid transport across the brush border membrane of Pieris brassicae midgut cells

AbstractThe luminal membrane of larval midgut cells is the site of action of insecticidal delta-endotoxin from Bacillus thuringiensis. At concentrations that correspond to normal effective doses in vivo, the toxin inhibits the uptake of amino acids by brush border membrane vesicles prepared from midguts of Pieris brassicae larvae. The toxin does not interact with the K+-amino acid symport but rather increases the K+ permeability of the membrane. The toxin does not increase the permeability of lepidopteran midgut brush border membrane to either Na+ or H+ nor does it increase the K+ permeability of brush border membrane vesicles prepared from mammalian small intestine

The Corporate University: An E-interview with Dave Hill, Alpesh Maisuria, Anthony Nocella, and Michael Parenti

Since the neo-liberal turn, corporate investment in universities has accelerated as the withdrawal of government funding, among other factors, has further exposed universities to market forces. While this process offers numerous benefits for corporations and wealthy individuals, it has been mostly detrimental for students, educators, and the public at large. In this interview, international scholars Dave Hill, Alpesh Maisuria, Anthony Nocella, and Michael Parenti broadly explain why corporations have been aggressively investing in universities. They address the numerous ways that corporate involvement in university activity negatively impacts academic freedom, research outcomes, and the practice of democracy. The interview ends on a hopeful note by presenting examples of resistance against corporate influence. Their analyses focus primarily on the United States, United Kingdom, and Canada

The Dually Acylated NH2-terminal Domain of Gi1α Is Sufficient to Target a Green Fluorescent Protein Reporter to Caveolin-enriched Plasma Membrane Domains: PALMITOYLATION OF CAVEOLIN-1 IS REQUIRED FOR THE RECOGNITION OF DUALLY ACYLATED G-PROTEIN α SUBUNITS IN VIVO

Here we investigate the molecular mechanisms that govern the targeting of G-protein α subunits to the plasma membrane. For this purpose, we used Gi1α as a model dually acylated G-protein. We fused full-length Gi1α or its extreme NH2-terminal domain (residues 1–32 or 1–122) to green fluorescent protein (GFP) and analyzed the subcellular localization of these fusion proteins. We show that the first 32 amino acids of Gi1α are sufficient to target GFP to caveolin-enriched domains of the plasma membrane in vivo, as demonstrated by co-fractionation and co-immunoprecipitation with caveolin-1. Interestingly, when dual acylation of this 32-amino acid domain was blocked by specific point mutations (G2A or C3S), the resulting GFP fusion proteins were localized to the cytoplasm and excluded from caveolin-rich regions. The myristoylated but nonpalmitoylated (C3S) chimera only partially partitioned into caveolin-containing fractions. However, both nonacylated GFP fusions (G2A and C3S) no longer co-immunoprecipitated with caveolin-1. Taken together, these results indicate that lipid modification of the NH2-terminal of Gi1α is essential for targeting to its correct destination and interaction with caveolin-1. Also, a caveolin-1 mutant lacking all three palmitoylation sites (C133S, C143S, and C156S) was unable to co-immunoprecipitate these dually acylated GFP-G-protein fusions. Thus, dual acylation of the NH2-terminal domain of Gi1α and palmitoylation of caveolin-1 are both required to stabilize and perhaps regulate this reciprocal interaction at the plasma membrane in vivo. Our results provide the first demonstration of a functional role for caveolin-1 palmitoylation in its interaction with signaling molecules

Simultaneous ectopic adrenocorticotropic hormone syndrome and adrenal metastasis of a medullary thyroid carcinoma causing paraneoplastic Cushing's syndrome

Medullary thyroid carcinomas (MTC) constitute about 5 to 7 % of thyroid neoplasms. They originate from parafollicular C-cells which can secrete adrenocorticotropic hormone (ACTH) and/or corticotropin-releasing factor (CRF) in abnormally high concentrations, potentially causing paraneoplastic Cushing's Syndrome (CS)