Permanent Genetic Resources added to Molecular Ecology Resources Database 1 February 2013-31 March 2013

This article documents the addition of 142 microsatellite marker loci to the Molecular Ecology Resources database. Loci were developed for the following species: Agriophyllum squarrosum, Amazilia cyanocephala, Batillaria attramentaria, Fungal strain CTeY1 (Ascomycota), Gadopsis marmoratus, Juniperus phoenicea subsp. turbinata, Liriomyza sativae, Lupinus polyphyllus, Metschnikowia reukaufii, Puccinia striiformis and Xylocopa grisescens. These loci were cross-tested on the following species: Amazilia beryllina, Amazilia candida, Amazilia rutila, Amazilia tzacatl, Amazilia violiceps, Amazilia yucatanensis, Campylopterus curvipennis, Cynanthus sordidus, Hylocharis leucotis, Juniperus brevifolia, Juniperus cedrus, Juniperus osteosperma, Juniperus oxycedrus, Juniperus thurifera, Liriomyza bryoniae, Liriomyza chinensis, Liriomyza huidobrensis and Liriomyza trifolii. © 2013 John Wiley & Sons Ltd.Peer Reviewe

Comparison Of Three Methods For Enamel Protein Extraction In Different Developmental Phases Of Rat Lower Incisors

Protein extraction methods [urea, trichloroacetic acid (TCA), and acetic acid] were compared for protein recovery from rat incisor developing enamel in the S phase (intermediate/late secretion), M1 phase (early maturation), M2 phase (intermediate maturation), and M3 phase (final maturation). We compared the protein recoveries with the percentage of enamel matrix dry weight burnt off by incineration. Our results indicate that TCA and urea were equally efficient for the extraction of S-stage proteins (85% and 90% recovery, respectively), while urea was the best for M1-stage proteins (92% recovery), and TCA the best for M2-stage (99% recovery) and M3-stage (60% recovery) proteins. The other methods yielded less than 30% recovery in comparison to incineration for M2 and M3 stages. The fact that urea extraction works well in the S and M1 stages and not thereafter is probably related to the changes in the proteins during enamel development and the amount of mineral that needs to be dissolved. TCA is the single method that effectively recovered proteins from all developmental stages of the rat incisor enamel. © Eur J Oral Sci, 2006.114SUPPL. 1272275Glimcher M, J., Levine, P.T., Studies of the proteins, peptides and free amino acids of mature bovine enamel (1966) Biochem J, 98, pp. 742-753Robinson C, Briggs, H.D., Atkinson, P.J., Weatherell, J.A., Chemical composition of human deciduous enamel (1981) Arch Oral Biol, 26, pp. 1027-1033Simmer J, P., Jc-C, H., Expression, structure, and function of enamel proteinases (2002) Connect Tissue Res, 43, pp. 441-449Smith C, E., Pompura, J.R., Borenstein, S., Fazel, A., Nanci, A., Degradation and loss of matrix proteins from developing enamel (1989) Anat Rec, 224, pp. 292-316Brookes S, J., Robinson, C., Kirkham, J., Bonass, W.A., Biochemistry and molecular biology of amelogenin proteins of developing enamel (1995) Arch Oral Biol, 40, pp. 1-14Glimcher M, J., Brichley-Parsons, D., Levine, P.T., Studies of enamel proteins during maturation (1977) Calcif Tissue Res, 24, pp. 259-270Glimcher M, J., Friberg, U.A., Levine, P.T., The isolation and amino acid composition of the enamel proteins of erupted bovine teeth (1964) Biochem J, 93, pp. 202-210Termine J, D., Belcourt, A.B., Christner, P.J., Conn, K.N., Nylen, M.U., Properties of dissociatively extracted fetal tooth matrix proteins. I. Principal molecular species in developing bovine enamel (1980) J Biol Chem, 255, pp. 9760-9768Belcourt A, B., Fincham, A.G., Termine, J.D., Bovine high molecular weight amelogenin proteins (1983) Calcif Tissue Int, 32, pp. 111-114Fincham A, G., Belcourt, A.B., Lyaruu, D.M., Termine, J.D., Comparative protein biochemistry of developing dental enamel matrix from five mammalian species (1982) Calcif Tissue Int, 34, pp. 182-189Fukae M, Shimizu, M., Studies on the proteins developing bovine enamel (1974) Arch Oral Biol, 19, pp. 381-386Bensadoun A, Weinstein, D., Assay of proteins in the presence of interfering materials (1976) Anal Biochem, 70, pp. 241-150Bradford M, M., A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding (1976) Anal Biochem, 72, pp. 248-254Laemmli U, K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4 (1970) Nature, 227, pp. 680-685Rosenberg I, M., (1996) Protein Analysis and Purification: Benchtop Techniques, 1st Edn.Smith C, E., Cellular and chemical events during enamel maturation (1998) Crit Rev Oral Biol Med, 9, pp. 128-161Moradian-Oldak J, Tan, J., Fincham, A.G., Interaction of amelogenin with hydroxyapatite crystals: An adherence effect through amelogenin molecular self association (1998) Biopolymers, 46, pp. 225-238Seyer J, M., Glimcher, M.J., Evidence for the presence of numerous protein components in immature bovine dental enamel (1977) Calcif Tiss Res, 24, pp. 253-25

Recovery And Identification Of Mature Enamel Proteins In Ancient Teeth

Proteins in mineralized tissues provide a window to the past, and dental enamel is peculiar in being highly resistant to diagenesis and providing information on a very narrow window of time, such as the developing period; however, to date, complete proteins have not been extracted successfully from ancient teeth. In this work we tested the ability of a whole-crown micro-etch technique to obtain enamel protein samples from mature enamel of recently extracted (n=2) and ancient (n=2; ad 800 to 1100) third molars. Samples were analyzed using matrix-assisted laser desorption/ionization time-of-flight/time-of-flight (MALDI-TOF/TOF) mass spectrometry, and the resulting spectra were searched against the Swiss-Prot protein database using the Mascot software for protein identification. In our protocol, the separation of proteins in gel is not necessary. Successful identification of specific enamel proteins was obtained after whole-crown superficial enamel etching with 10% HCl. Most protein fragments recovered from dry teeth and mummy teeth contained amino-terminal amelogenin peptides. Only one peptide specific for the amelogenin X-isoform was identified. In conclusion, the reported techniques allowed the successful recovery of proteins specific to dental enamel from samples obtained in a very conservative manner, which may also be important in forensic and/or archeological science. © 2011 Eur J Oral Sci.119SUPPL.18387Smith, C.E., Cellular and chemical events during enamel maturation (1998) Crit Rev Oral Biol Med, 9, pp. 128-161Nanci, A., (2008) Ten Cate's oral histology: development, structure, and function, , Saint Louis: MosbyAlberts, B., Johnson, A., Lewis, J., Raff, M., Roberts, K., Walter, P., (2005) Molecular biology of the cell, , New York: Garland ScienceDean, M.C., Tooth microstructure tracks the pace of human life-history evolution (2006) Proc Biol Sci, 273, pp. 2799-2808Smith, T.M., Hublin, J.J., Dental tissue studies: 2D and 3D insights into human evolution (Preface) (2008) J Hum Evol, 54, pp. 169-172Smith, T.M., Incremental dental development: methods and applications in hominoid evolutionary studies (2008) J Hum Evol, 54, pp. 205-224Schweitzer, M.H., Zheng, W., Organ, C.L., Avci, R., Suo, Z., Freimark, L.M., Lebleu, V.S., Asara, J.M., Biomolecular characterization and protein sequences of the Campanian hadrosaur B. canadensis (2009) Science, 324, pp. 626-631Schweitzer, M.H., Wittmeyer, J.L., Horner, J.R., Soft tissue and cellular preservation in vertebrate skeletal elements from the Cretaceous to the present (2007) Proc Royal Soc B, 274, pp. 183-197Collins, M.J., Gernaey, A.M., Nielsen-Marsh, C.M., Vermeer, C., Westbroek, P., Slow rates of degradation of osteocalcin: green light for fossil bone protein? (2000) Geology, 28, pp. 1139-1142Nielsen-Marsh, C.M., Ostrom, P.H., Ghandi, H., Shapiro, B., Cooper, A., Hauschka, P.V., Collins, M.J., Sequence preservation of osteocalcin protein and mitochondrial DNA in bison bones older than 55 ka (2002) Geology, 30, pp. 1099-1102Nielsen-Marsh, C.M., Richards, M.P., Hauschka, P.V., Thomas-Oates, J.E., Trinkaus, E., Pettitt, P.B., Karavanic, I., Collins, M.J., Osteocalcin protein sequence of Neanderthals and modern primates (2005) Proc Natl Acad Sci U S A, 102, pp. 4409-4413Lee-Thorp, J.A., Van Der Merwe, N.J., Aspects of the chemistry of modern and fossil biological apatites (1991) J Arch Sci, 18, pp. 343-354Porto, I.M., Laurie, H.J., Sousa, F.B., Rosa, J.C., Gerlach, R.F., New techniques for the recovery of small amounts of mature enamel proteins (2011) J Arch Sci, 38, pp. 3596-3604Kosiba, S.B., Tykot, R.H., Carlsson, D., Stable isotopes as indicators of change in the food procurement and food preference of viking age and early Christian populations on Gotland (Sweden) (2007) J Anthropol Archaeol, 26, pp. 394-411Tykot, R.H., Isotope analyses and the histories of maize (2010) Histories of Maize in Mesoamerica, pp. 130-141. , STALLER JE, TYKOT RH, BENZ BF, eds. Multidisciplinary approaches. Amsterdam: Academy PressNielse-Marsh, C.M., Stegemann, C., Hoffmann, R., Smith, T., Feeney, R., Toussaint, M., Harvati, K., Richards, M.P., Extraction and sequencing of human and Neandethal mature enamel proteins using MALDI-TOF/TOF MS (2009) J Arch Sci, 36, pp. 1758-1763Porto, I.M., Merzel, J., De Sousa, F.B., Bachmann, L., Cury, J.A., Line, S.R., Gerlach, R.F., Enamel mineralization in the absence of maturation stage ameloblasts (2009) Arch Oral Biol, 54, pp. 313-321Fraser, R.A., Grün, R., Privat, K., Gagan, M.K., Stable-isotope microprofiling of wombat tooth enamel records seasonal changes in vegetation and environmental conditions in eastern Australia (2008) Palaeogeogr Palaeoclimatol Palaeoecol, 269, pp. 66-77Bartlett, J.D., Simmer, J.P., Proteinases in developing dental enamel (1999) Crit Rev Oral Biol Med, 10, pp. 425-441Aoba, T., Fukae, M., Tanabe, T., Shimizu, M., Moreno, E.C., Selective adsorption of porcine-amelogenins onto hydroxyapatite and their inhibitory activity on hydroxyapatite growth in supersaturated solutions (1987) Calcif Tissue Int, 41, pp. 281-289Sponheimer, M., Lee-Thorp, J.A., Isotopic evidence for the diet of an early hominid, Australopithecus africanus (1999) Science, 283, pp. 368-370Lee-Thorp, J.A., Sponheimer, M., Luyt, J., Tracking changing environments using stable carbon isotopes in fossil tooth enamel: an example from the South African hominin sites (2007) J Human Evol, 53, pp. 595-601Lee-Thorp, J.A., Sponheimer, M., Contributions of Biogeochemistry to understanding hominin dietary ecology (2006) Am J Phys Anthropol, 131, pp. 131-148Smith, C.C., Morgan, M.E., Pilbeam, D., Isotopic ecology and dietary profiles of Liberian chimpanzees (2010) J Human Evol, 58, pp. 43-55Wright, L.E., Schwarcz, H.P., Correspondence between stable carbon, oxygen and nitrogen isotopes in human tooth enamel and dentine: infant diets at Kaminaljuyú (1999) J Arch Sci, 26, pp. 1159-1170Steinlechner, M., Berger, B., Niederstätter, H., Parson, W., Rare failures in the amelogenin sex test (2002) Int J Legal Med, 116, pp. 117-120Tykot, R.H., Stable isotopes and diet: you are what you eat (2004) Physics methods in archaeometry, pp. 433-444. , Martini M, Milazzo M, Piacentini M, eds. Proceedings of the International School of Physics "Enrico Fermi". Amsterdam: IOS Pres

CYP3A4*22 genotype and systemic exposure affect paclitaxel-induced neurotoxicity

Purpose: Paclitaxel is used for the treatment of several solid tumors and displays a high interindividual variation in exposure and toxicity. Neurotoxicity is one of the most prominent side effects of paclitaxel. This study explores potential predictive pharmacokinetic and pharmacogenetic determinants for the onset and severity of neurotoxicity. Experimental Design: In an exploratory cohort of patients (n = 261) treated with paclitaxel, neurotoxicity incidence, and severity, pharmacokinetic parameters and pharmacogenetic variants were determined. Paclitaxel plasma concentrations were measured by high-performance liquid chromatography or liquid chromatography/tandem mass spectrometry, and individual pharmacokinetic parameters were estimated from previously developed population pharmacokinetic models by nonlinear mixed effects modeling. Genetic variants of paclitaxel pharmacokinetics tested were CYP3A4*22, CYP2C8*3, CYP2C8*4, and ABCB1 3435 C>T. The association between CYP3A4*22 and neurotoxicity observed in the exploratory cohort was validated in an independent patient cohort (n = 239). Results: Exposure to paclitaxel (logAUC) was correlated with severity of neurotoxicity (P 0.05) of paclitaxel in males or females. Other genetic variants displayed no association with neurotoxicity. In the subsequent independent validation cohort, CYP3A4*22 carriers were at risk of developing grade 3 neurotoxicity (OR = 19.1; P = 0.001). Conclusions: Paclitaxel exposure showed a relationship with the severity of paclitaxel-induced neurotoxicity. In this study, female CYP3A4*22 carriers had increased risk of developing severe neurotoxicity during paclitaxel therapy. These observations may guide future individualization of paclitaxel treatment

NR5A1 is a novel disease gene for 46,XX testicular and ovotesticular disorders of sex development

Purpose: We aimed to identify the genetic cause in a cohort of 11 unrelated cases and two sisters with 46,XX SRY-negative (ovo)testicular disorders of sex development (DSD). Methods: Whole-exome sequencing (n = 9), targeted resequencing (n = 4), and haplotyping were performed. Immunohistochemistry of sex-specific markers was performed on patients' gonads. The consequences o