Bovine intestinal calcium-binding proteins

Genetic Susceptibility to Lead Poisoning

“…(61)(62)(63). In addition, calbindin-D binds lead with high affinity and may be implicated in its transport (64). These data suggest that calcium and lead are cotransported through the gut into the blood, and from there the two metals may be codistributed to calcium-rich tissues such as the bone (65).…”

Characterizing Golden Eagle Risk to Lead and Anticoagulant Rodenticide Exposure: A Review

“…Lead inhibits uptake of calcium into isolated renal mitochondria and may enter mitochondria as a substrate for a calcium transporter (Kapoor et al 1985). This would be consistent with evidence that lead can interact with calcium binding proteins and thereby affect calciummediated or regulated events in a variety of tissues (Fullmer et al 1985;Goldstein 1993;Goldstein and Ar 1983;Habermann et al 1983;Platt and Busselberg 1994;Pounds 1984;Richardt et al 1986;Rosen and Pounds 1989;Simons and Pocock 1987;Sun and Suszkiw 1995;Tomsig and Suszkiw 1995;Watts et al 1995). Impairments of oxidative metabolism could conceivably contribute to transport deficits and cellular degeneration; however, the exact role this plays in lead-induced nephrotoxicity has not been elucidated.…”

Pb(II) Disruption of Synaptic Activity Through Ca(II)- and Zn(II)-binding Proteins

“…As a borderline Lewis Acid ( Figure 3A), Pb 2+ can display properties of either hard or soft acids, which would allow it to replace a variety of different metal ions in proteins. Indeed, studies have demonstrated that Pb 2+ can displace Mg 2+ in pyrimidine 5'-nucleotidase type 1 [71] , Fe 2+ in divalent cation transporter-1 [2] , Zn 2+ in 5-aminolevulinic acid dehydratase (ALAD) [72,73] , and Ca 2+ in a variety of Ca 2+ -binding proteins (CaBPs) [74][75][76][77][78] including PKC [79,80] , synaptotagmin [81] , and CaM [78,82] ; all proteins involved in neural pathways that represent targets for Pb 2+ -induced neurotoxicity. A comprehensive statistical analysis of Pb 2+ -bound structures in the Protein DataBank (PDB), revealed that Pb 2+ is remarkably adept at occupying the binding sites of physiologically relevant metal ions, despite differences in coordination numbers, coordination geometries, and ligand type [60] .…”