A review of migration and fertility theory through the lens of African immigrant fertility in France

This paper evaluates fertility and migration theory in order to further understand the impact of migration on fertility. I first analyze the fertility and migration literature separately and then look at the burgeoning literature on the impact of migration on fertility. As a result, I propose an integrated framework for analyzing the migration-fertility nexus. Within the fertility context, I use Bongaarts and Watkins concept of social interaction, whereas within the migration context, I draw on Massey’s capitalist transition theory, and Pessar and Mahler’s ‘gendered geometries of power’. This integrated framework considers three major factors: the sending country, the global context of migration systems, and the receiving country. Gender is the key to understanding fertility decisions within all three levels. Migration from Africa to France is considered in order to exemplify these processes. Bozon’s typology of African demographic patterns shows how and why the sending country matters for future childbearing decisions post-migration. To further explore this facet, four countries are used to evaluate the impact of migrating from specific types of countries on fertility post-migration: Senegal, Mali, Cameroon, and Rwanda. The global context of migration is constantly changing, both encouraging and restraining men and women in particular ways, which also affects fertility choices. Finally, the receiving country interacts with migrants in various ways—immigration policies, the economy, and social institutions—playing important roles in fertility outcomes.Africa, France, fertility, migration

Substrate-induced inactivation of the Escherichia coli AmiD N-acetylmuramoyl-L-alanine amidase highlights a new strategy to inhibit this class of enzyme.

In the eubacterial cell, the peptidoglycan is perpetually hydrolyzed throughout the cell cycle by different enzymes such as lytic transglycosylases, endopeptidases, and amidases. In Escherichia coli, four N-acetylmuramoyl-l-alanine amidases, AmiA, -B, -C, and -D, are present in the periplasm. AmiA, -B, and -C are soluble enzymes, whereas AmiD is a lipoprotein anchored in the outer membrane. To determine more precisely the specificity and the kinetic parameters of AmiD, we overproduced and purified the native His-tagged AmiD in the presence of detergent and a soluble truncated form of this enzyme by removing its signal peptide and the cysteine residue responsible for its lipidic anchorage. AmiD is a zinc metalloenzyme and is inactivated by a metal chelator such as EDTA. Native His-tagged and truncated AmiD hydrolyzes peptidoglycan fragments that have at least three amino acids in their peptide chains, and the presence of an anhydro function on the N-acetylmuramic acid is not essential for its activity. The soluble truncated AmiD exhibits a biphasic kinetic time course that can be explained by the inactivation of the enzyme by the substrate. This behavior highlights a new strategy to inhibit this class of enzymes

Thrombocytopenia associated with dengue hemorrhagic fever responds to intravenous administration of anti-D (RH0-D) immune globulin

Severe thrombocytopenia and increased vascular permeability are two major characteristics of dengue hemorrhagic fever (DHF). An immune mechanism of thrombocytopenia due to increased platelet destruction appears to be operative in patients with DHF (see Saito et al., 2004, Clin Exp Immunol 138: 299-303; Mitrakul, 1979, Am J Trop Med Hyg 26: 975-984; and Boonpucknavig, 1979, Am J Trop Med Hyg 28: 881-884). The interim data of two randomized placebo controlled trials in patients (N = 47) meeting WHO criteria for dengue hemorrhagic fever (DHF) with severe thrombocytopenia (platelets ≤ 50,000/mm3) reveal that the increase in platelet count with anti-D immune globulin (WinRho® SDF), 50 μg/kg (250 IU/kg) intravenously is more brisk than the placebo group. The mean maximum platelet count of the anti-D-treated group at 48 hours was 91,500/mm3 compared with 69,333/mm3 in the placebo group. 75% of the anti-D-treated group demonstrated an increase of platelet counts ≥ 20,000 compared with only 58% in the placebo group. These data suggest that treatment of severe thrombocytopenia accompanying DHF with anti-D may be a useful and safe therapeutic option. Copyright © 2007 by The American Society of Tropical Medicine and Hygiene

XBP1s activation can globally remodel N-glycan structure distribution patterns.

Classically, the unfolded protein response (UPR) safeguards secretory pathway proteostasis. The most ancient arm of the UPR, the IRE1-activated spliced X-box binding protein 1 (XBP1s)-mediated response, has roles in secretory pathway maturation beyond resolving proteostatic stress. Understanding the consequences of XBP1s activation for cellular processes is critical for elucidating mechanistic connections between XBP1s and development, immunity, and disease. Here, we show that a key functional output of XBP1s activation is a cell type-dependent shift in the distribution of N-glycan structures on endogenous membrane and secreted proteomes. For example, XBP1s activity decreased levels of sialylation and bisecting GlcNAc in the HEK293 membrane proteome and secretome, while substantially increasing the population of oligomannose N-glycans only in the secretome. In HeLa cell membranes, stress-independent XBP1s activation increased the population of high-mannose and tetraantennary N-glycans, and also enhanced core fucosylation. mRNA profiling experiments suggest that XBP1s-mediated remodeling of the N-glycome is, at least in part, a consequence of coordinated transcriptional resculpting of N-glycan maturation pathways by XBP1s. The discovery of XBP1s-induced N-glycan structural remodeling on a glycome-wide scale suggests that XBP1s can act as a master regulator of N-glycan maturation. Moreover, because the sugars on cell-surface proteins or on proteins secreted from an XBP1s-activated cell can be molecularly distinct from those of an unactivated cell, these findings reveal a potential new mechanism for translating intracellular stress signaling into altered interactions with the extracellular environment