Towards a new osteometric method for sexing ancient cremated human remains. Analysis of Late Bronze Age and Iron Age samples from Italy with gendered grave goods

Sex estimation of human remains is one of the most important research steps for physical anthropologists and archaeologists dealing with funerary contexts and trying to reconstruct the demographic structure of ancient societies. However, it is well known that in the case of cremations sex assessment might be complicated by the destructive/transformative effect of the fire on bones. Osteometric standards built on unburned human remains and contemporary cremated series are often inadequate for the analysis of ancient cremations, and frequently result in a significant number of misclassifications. This work is an attempt to overcome the scarcity of methods that could be applied to pre-proto-historic Italy and serve as methodological comparison for other European contexts. A set of 24 anatomical traits were measured on 124 Bronze Age and Iron Age cremated individuals with clearly engendered grave goods. Assuming gender largely correlated to sex, male and female distributions of each individual trait measured were compared to evaluate sexual dimorphism through inferential statistics and Chaktaborty and Majumder\u2019s index. The discriminatory power of each variable was evaluated by cross-validation tests. Eight variables yielded an accuracy equal to or greater than 80%. Four of these variables also show a similar degree of precision for both sexes. The most diagnostic measurements are from radius, patella, mandible, talus, femur, first metatarsal, lunate and humerus. Overall, the degree of sexual dimorphism and the reliability of estimates obtained from our series are similar to those of a modern cremated sample recorded by Gon\ue7alves and collaborators. Nevertheless, mean values of the male and female distributions in our case study are lower, and the application of the cut-off point calculated from the modern sample to our ancient individuals produces a considerable number of misclassifications. This result confirms the need to build population-specific methods for sexing the cremated remains of ancient individuals

Latherin: A Surfactant Protein of Horse Sweat and Saliva

Horses are unusual in producing protein-rich sweat for thermoregulation, a major component of which is latherin, a highly surface-active, non-glycosylated protein. The amino acid sequence of latherin, determined from cDNA analysis, is highly conserved across four geographically dispersed equid species (horse, zebra, onager, ass), and is similar to a family of proteins only found previously in the oral cavity and associated tissues of mammals. Latherin produces a significant reduction in water surface tension at low concentrations (≤1 mg ml−1), and therefore probably acts as a wetting agent to facilitate evaporative cooling through a waterproofed pelt. Neutron reflection experiments indicate that this detergent-like activity is associated with the formation of a dense protein layer, about 10 Å thick, at the air-water interface. However, biophysical characterization (circular dichroism, differential scanning calorimetry) in solution shows that latherin behaves like a typical globular protein, although with unusual intrinsic fluorescence characteristics, suggesting that significant conformational change or unfolding of the protein is required for assembly of the air-water interfacial layer. RT-PCR screening revealed latherin transcripts in horse skin and salivary gland but in no other tissues. Recombinant latherin produced in bacteria was also found to be the target of IgE antibody from horse-allergic subjects. Equids therefore may have adapted an oral/salivary mucosal protein for two purposes peculiar to their lifestyle, namely their need for rapid and efficient heat dissipation and their specialisation for masticating and processing large quantities of dry food material

Secretory proteins as potential semiochemical carriers in the horse

Two soluble proteins were isolated as major secretory products of horse sweat and of the parotid gland and characterized for structural and functional properties. The first protein, lipocalin allergen EquC1, was characterized for its glycosylation sites and bound glycosidic moieties. Only one (Asn53) of the two putative glycosylation sites within the sequence was post-translationally modified; a different glycosylation pattern was determined with respect to data previously reported. When purified from horse sweat, this protein contained oleamide and other organic molecules as natural ligands. Ligand binding experiments indicated good protein selectivity toward volatile compounds having a straight chain structure of 9-11 carbon atoms, suggesting a role of this lipocalin in chemical communication. The second protein, here reported for the first time in the horse, belongs to the group of parotid secretory proteins, part of a large superfamily of binding proteins whose function in most cases is still unclear. This protein was sequenced and characterized for its post-translational modifications. Of the three cysteine residues present, two were involved in a disulfide bridge (Cys155-Cys198). A model, built up on the basis of similar proteins, indicated a general fold characterized by the presence of a long hydrophobic barrel. Binding experiments performed with a number of different organic compounds failed to identify ligands for this protein with a well-defined physiological role