PGs and their constituent glycosaminoglycan (GAG) chains also bind to hydroxyapatite, which could also potentially protect these molecules from degradation.

Extracellular matrix (ECM) proteins bind very tightly to hydroxyapatite which protects these proteins from the destructive effects of temperature and chemical agents after death. The organic matrix is comprised mainly of collagen types I and III, non-collagenous proteins such as fibronectin, osteocalcin, osteopontin, osteonectin and bone sialoprotein II, and proteoglycans (PGs) such as decorin and biglycan. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.Ĭompeting interests: The authors have declared that no competing interests exist.īone tissue is mineralized dense connective tissue that consists mainly of a mineral component (hydroxyapatite) and an organic matrix. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are creditedĭata Availability: All relevant data are within the paper.įunding: This research was made possible by support from CAPES (Coordenação de Aperfeiçoamento de Pessoal de Nível Superior), CNPq (Conselho Nacional de Desenvolvimento Científico e Tecnológico) and FAPESP (Fundação de Amparo a Pesquisa do Estado de São Paulo). Received: OctoAccepted: Published: June 24, 2015Ĭopyright: © 2015 Coulson-Thomas et al. (2015) The Identification of Proteoglycans and Glycosaminoglycans in Archaeological Human Bones and Teeth. The finding that significant quantities of PGs and GAGs persist in archaeological bones and teeth opens novel venues for the field of Paleontology.Ĭitation: Coulson-Thomas YM, Coulson-Thomas VJ, Norton AL, Gesteira TF, Cavalheiro RP, Meneghetti MCZ, et al. Staining patterns were different for juvenile and adult bones, whilst adolescent bones had a similar staining pattern to adult bones. The localization of CS, HA, three small leucine rich PGs (biglycan, decorin and fibromodulin) and glypican was analyzed in archaeological human bone slices. The GAG populations isolated were chondroitin sulfate (CS) and hyaluronic acid (HA). PGs and GAGs were successfully extracted from both archaeological human bones and teeth, and characterized by their electrophoretic mobility in agarose gel, degradation by specific enzymes and HPLC. We therefore optimized methods for the extraction of both PGs and GAGs from archaeological human skeletons. The ability to isolate and characterize PG and GAG content from archaeological skeletons would unveil valuable paleontological information. PGs and GAGs play a major role in bone morphogenesis, homeostasis and degenerative bone disease.

DNA and proteins have been successfully extracted from archaeological skeletons from which valuable information has been obtained however, to date neither PGs nor glycosaminoglycan (GAG) chains have been studied in archaeological skeletons. Extracellular matrix proteins and PGs bind tightly to hydroxyapatite which would protect these molecules from the destructive effects of temperature and chemical agents after death. Bone tissue is mineralized dense connective tissue consisting mainly of a mineral component (hydroxyapatite) and an organic matrix comprised of collagens, non-collagenous proteins and proteoglycans (PGs).

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