This includes individual efforts such as removing lead-containing items from the home, workplace efforts such as improved ventilation and monitoring, state laws that ban the use of and national policies such as laws that ban lead in products such as paint, gasoline, ammunition, wheel weights, and fishing weights reduce allowable levels in water or soil, and provide for cleanup of contaminated soil. Workers education could be helpful as well. The major treatments are removal of the source of lead and the use of medications that bind lead so it can be eliminated from the body, known as chelation therapy. Chelation therapy in children is recommended when blood levels are greater than 40–45 µg/dl. Medications used include dimercaprol, edetate calcium disodium, and succimer.In 2016, lead is believed to have resulted in 540,000 deaths worldwide. It occurs most commonly in the developing world. There also are numerous cases in the developed world, with there being thousands of American communities with higher lead burdens than seen during the peak of the Flint water crisis. Those who are poor are at greater risk. Lead is believed to result in 0.6% of the worlds disease burden. According to a study, half of the US population has been exposed to substantially detrimental lead levels in early childhood – mainly from car exhaust whose lead pollution peaked in the 1970s and caused widespread loss in cognitive ability.People have been mining and using lead for thousands of years.
A vast amount of carbohydrate binding molecules (lectins) depend on correct glycosylation for appropriate binding; the selectins, involved in leukocyte extravasation, is a prime example. Their binding depends on a correct fucosylation of cell surface glycoproteins. Lack thereof leads to leukocytosis and increase sensitivity to infections as seen in SLC35C1-CDG(CDG-IIc); caused by a GDP-fucose (Fuc) transporter deficiency.All N-linked oligosaccharides originate from a common lipid-linked oligosaccharide (LLO) precursor, synthesized in the ER on a dolichol-phosphate (Dol-P) anchor. The mature LLO is transferred co-translationally to consensus sequence Asn residues in the nascent protein, and is further modified by trimming and re-building in the Golgi. Deficiencies in the genes involved in N-linked glycosylation constitute the molecular background to most of the CDGs. Type I defects involve the synthesis and transfer of the LLO
Type II defects impair the modification process of protein-bound oligosaccharides. Type I
Type II
The mature LLO chain is next transferred to the growing protein chain, a process catalysed by the oligosaccharyl transferase (OST) complex. Once transferred to the protein chain, the oligosaccharide is trimmed by specific glycosidases. This process is vital since the lectin chaperones calnexin and calreticulin, involved in protein quality, bind to the Glc1Man9GlcNAc-structure and assure proper folding. Lack of the first glycosidase (GCS1) causes CDG-IIb. Removal of the Glc residues and the first Man residue occurs in the ER. The glycoprotein then travels to the Golgi, where a multitude of different structures with different biological activities are formed.