Early Evidence for Northern Salmonid Fisheries Discovered using Novel Mineral Proxies.

Salmonid resources currently foster socioeconomic prosperity in several nations, yet their importance to many ancient circumpolar societies is poorly understood due to insufficient fish bone preservation at archaeological sites. As a result, there are serious gaps in our knowledge concerning the antiquity of northern salmonid fisheries and their impacts on shaping biodiversity, hunter-gatherer adaptations, and human-ecological networks. The interdisciplinary study presented here demonstrates that calcium-magnesium phosphate minerals formed in burned salmonid bones can preserve at ancient northern sites, thus informing on the early utilization of these resources despite the absence of morphologically classifiable bones. The minerals whitlockite and beta magnesium tricalcium phosphate were identified in rare morphologically classifiable Atlantic salmonid bones from three Mid-Holocene sites in Finland. Large amounts of beta magnesium tricalcium phosphate were also experimentally formed by burning modern Atlantic salmonid and brown trout bones. Our results demonstrate the value of these minerals as proxies for ancient northern salmonid fishing. Specifically, the whitlockite mineral was discovered in hearth sediments from the 5,600 year old Yli-Ii Kierikinkangas site on the Iijoki River in northern Finland. Our fine sieving and mineralogical analyses of these sediments, along with zooarchaeological identification of recovered bone fragments, have confirmed for the first time that the people living at this village did incorporate salmonids into their economies, thus providing new evidence for early estuary/riverine fisheries in northern Finland.

Effects of antibody binding on structural transitions of the nicotinic acetylcholine receptor.

Patch-clamping and photoaffinity-labeling techniques were used to study the effects of binding of monoclonal antibodies (mAbs) on the function of Torpedo californica nicotinic acetylcholine receptor (nAChR). The rat anti-Torpedo nAChR mAbs examined here are known to inhibit ligand binding to either the high-affinity (mAb 247) or both the high- and low-affinity binding sites (mAb 370 and mAb 387) [Mihovilovic, M. & Richman, D. P. (1984) J. Biol. Chem. 259, 15051-15059; Mihovilovic, M., & Richman, D. P. (1987) J. Biol. Chem. 262, 4978-4986]. Single-channel analysis shows that mAb 247 and the Fab fragment of mAb 247 inhibit the opening of the nAChR ion channel, although they have no effects on the structural transition from the resting to desensitized state as monitored by the extent of decreased labeling by the photoreactive probe 3-(trifluoromethyl)-3-(m- [125I]iodophenyl)diazirine ([125I]-TID). In the presence of mAb 387, the nAChR single-channel amplitude was decreased by 20%, whereas Fab 387 completely inhibited channel opening. [125I-TID]-labeling studies suggest that the mAb 387-nAChR and Fab 387-nAChR complexes are able to undergo the transition between resting and desensitized states. This result confirms that the nAChR can assume a desensitized state without prior channel opening. In addition, mAb 35 and mAb 132, which recognize the main immunogenic region (MIR) of the nAChR, and mAb 370 do not alter either single-channel behavior or labeling patterns. Combining the results from characterization with respect to their epitopes and their effects on agonist (carbamylcholine) and antagonist [alpha-bungarotoxin (alpha-BTX) and curare] binding, these results indicate that mAbs could be used to map functional and structural domains.