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Acta biomaterialia2014; 10(9); 3969-3977; doi: 10.1016/j.actbio.2014.05.027

Bovine and equine peritubular and intertubular dentin.

Abstract: Dentin contains 1-2μm diameter tubules extending from the pulp cavity to near the junction with enamel. Peritubular dentin (PTD) borders the tubule lumens and is surrounded by intertubular dentin (ITD). Differences in PTD and ITD composition and microstructure remain poorly understood. Here, a (∼200nm)(2), 10.1keV synchrotron X-ray beam maps X-ray fluorescence and X-ray diffraction simultaneously around tubules in 15-30μm thick bovine and equine specimens. Increased Ca fluorescence surrounding tubule lumens confirms that PTD is present, and the relative intensities in PTD and ITD correspond to carbonated apatite (cAp) volume fraction of ∼0.8 in PTD vs. 0.65 assumed for ITD. In the PTD near the lumen edges, Zn intensity is strongly peaked, corresponding to a Zn content of ∼0.9mgg(-1) for an assumed concentration of ∼0.4mgg(-1) for ITD. In the equine specimen, the Zn K-edge position indicates that Zn(2+) is present, similar to bovine dentin (Deymier-Black et al., 2013), and the above edge structure is consistent with spectra from macromolecules related to biomineralization. Transmission X-ray diffraction shows only cAp, and the 00.2 diffraction peak (Miller-Bravais indices) width is constant from ITD to the lumen edge. The cAp 00.2 average preferred orientation is axisymmetric (about the tubule axis) in both bovine and equine dentin, and the axisymmetric preferred orientation continues from ITD through the PTD to the tubule lumen. These data indicate that cAp structure does not vary from PTD to ITD.
Publication Date: 2014-06-06 PubMed ID: 24911530PubMed Central: PMC4123743DOI: 10.1016/j.actbio.2014.05.027Google Scholar: Lookup
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  • Journal Article
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Summary

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This research article examines and compares the compositions and structures of peritubular and intertubular dentin in bovine and equine specimens. The study uses advanced X-ray technologies to confirm the presence of key substances and structures, with findings indicating that the structure of carbonated apatite, a significant mineral component, does not vary between peritubular and intertubular dentin.

Dentin and the Study Focus

  • Dentin is a crucial component of teeth, containing microscopic tubules that extend from the center of the tooth towards the enamel junction.
  • There are two types of dentin: Peritubular Dentin (PTD), which envelops the tubule lumens, and Intertubular Dentin (ITD) that surrounds the PTD. However, differences in their microstructure and composition are not fully understood, prompting the need for this study.
  • The research aims to gain insights into these differences by analyzing bovine and equine dentin specimens using synchrotron X-ray beams.

Research Method and Findings

  • The high-energy X-ray beams mapped X-ray fluorescence and diffraction simultaneously, providing detailed insights into the structure and composition of the specimens.
  • Increased Calcium (Ca) fluorescence around the tubule lumen confirms the presence of PTD. Relative intensities suggest a carbonated apatite (cAp) volume fraction of approximately 0.8 in PTD versus 0.65 in ITD. cAp is a crucial mineral constituent of dentin.
  • Single-crystal Zn, with an intensity peak near the lumen edges in PTD, corresponds to a Zinc (Zn) content of about 0.9mgg(-1) assuming a concentration of 0.4mgg(-1) in ITD.

Results on Equine Specimen and Final Conclusions

  • In the equine specimen, Zn(2+) is present, and its edge structure aligns with spectra from biomolecules related to biomineralization.
  • Transmission X-ray diffraction shows only cAp and the cAp 00.2 average preferred orientation is the same in bovine and equine dentin and doesn’t change from ITD through the PTD to the tubule lumen.
  • These findings suggest that the cAp structure, a significant mineral element of dentin, remains constant from PTD to ITD.

Cite This Article

APA
Stock SR, Deymier-Black AC, Veis A, Telser A, Lux E, Cai Z. (2014). Bovine and equine peritubular and intertubular dentin. Acta Biomater, 10(9), 3969-3977. https://doi.org/10.1016/j.actbio.2014.05.027

Publication

ISSN: 1878-7568
NlmUniqueID: 101233144
Country: England
Language: English
Volume: 10
Issue: 9
Pages: 3969-3977
PII: S1742-7061(14)00239-6

Researcher Affiliations

Stock, S R
  • Department of Molecular Pharmacology and Biological Chemistry, Northwestern University, 303 E. Chicago Ave, Chicago, IL 60611-3008, USA. Electronic address: s-stock@northwestern.edu.
Deymier-Black, A C
  • Department of Cell and Molecular Biology, Northwestern University, 303 E. Chicago Ave, Chicago, IL 60611-3008, USA.
Veis, A
  • Department of Cell and Molecular Biology, Northwestern University, 303 E. Chicago Ave, Chicago, IL 60611-3008, USA.
Telser, A
  • Department of Cell and Molecular Biology, Northwestern University, 303 E. Chicago Ave, Chicago, IL 60611-3008, USA.
Lux, E
  • Department of Cell and Molecular Biology, Northwestern University, 303 E. Chicago Ave, Chicago, IL 60611-3008, USA.
Cai, Z
  • Advanced Photon Source, Argonne National Laboratory, 9700 S. Cass Ave, Argonne, IL 60439, USA.

MeSH Terms

  • Animals
  • Calcium / analysis
  • Cattle
  • Crystallography, X-Ray
  • Dentin / chemistry
  • Dentin / diagnostic imaging
  • Fluorescence
  • Horses
  • Radiography
  • X-Ray Absorption Spectroscopy
  • Zinc / analysis

Grant Funding

  • R01 DE001374 / NIDCR NIH HHS
  • DE001374 / NIDCR NIH HHS

Conflict of Interest Statement

. The authors have no conflict of interest to report.

References

This article includes 34 references
  1. Stock SR, Veis A, Telser A, Cai Z. Near tubule and intertubular bovine dentin mapped at the 250 nm level.. J Struct Biol 2011 Nov;176(2):203-11.
    pmc: PMC3199959pubmed: 21821132doi: 10.1016/j.jsb.2011.07.014google scholar: lookup
  2. Deymier-Black AC, Veis A, Cai Z, Stock SR. Crystallographic texture and elemental composition mapped in bovine root dentin at the 200 nm level.. Scanning 2014 Mar-Apr;36(2):231-40.
    doi: 10.1002/sca.21093pmc: PMC4727833pubmed: 23630059google scholar: lookup
  3. Takuma S, Eda S. Structure and Development of the Peritubular Matrix in Dentin. J Dent Res 1966;45:683–692.
  4. Weber DF. The distribution of peritubular matrix in human coronal dentin.. J Morphol 1968 Dec;126(4):435-45.
    pubmed: 5716436doi: 10.1002/jmor.1051260405google scholar: lookup
  5. Jones SJ, Boyde A. Ultrastructure of dentin and dentinogenesis. .
  6. Libera J, Cai Z, Lai B, Xu S. Integration of a hard x-ray microprobe with a diffractometer for microdiffraction. Rev Sci Instrum 2002;73:1506–1508.
  7. Hammersley AP. FIT2D V9.129 reference manual V3.1. ESRF Internal Report 1998.
  8. Deymier-Black AC, Almer JD, Stock SR, Haeffner DR, Dunand DC. Synchrotron X-ray diffraction study of load partitioning during elastic deformation of bovine dentin.. Acta Biomater 2010 Jun;6(6):2172-80.
    pubmed: 19925891doi: 10.1016/j.actbio.2009.11.017google scholar: lookup
  9. Deymier-Black AC, Almer JD, Stock SR, Dunand DC. Variability in the elastic properties of bovine dentin at multiple length scales.. J Mech Behav Biomed Mater 2012 Jan;5(1):71-81.
    pubmed: 22100081doi: 10.1016/j.jmbbm.2011.08.005google scholar: lookup
  10. Schilke R, Lisson JA, Bauss O, Geurtsen W. Comparison of the number and diameter of dentinal tubules in human and bovine dentine by scanning electron microscopic investigation.. Arch Oral Biol 2000 May;45(5):355-61.
    pubmed: 10739856doi: 10.1016/s0003-9969(00)00006-6google scholar: lookup
  11. Muylle S, Simoens P, Lauwers H. Tubular contents of equine dentin: a scanning electron microscopic study.. J Vet Med A Physiol Pathol Clin Med 2000 Aug;47(6):321-30.
  12. BOYDE A, SWITSUR VR, FEARNHEAD RW. Application of the scanning electron-probe x-ray microanalyser to dental tissues.. J Ultrastruct Res 1961 Jun;5:201-7.
    pubmed: 13872172doi: 10.1016/s0022-5320(61)90015-6google scholar: lookup
  13. Höhling HJ, Steffens H, Heuck F. [Density of mineralization in hard tissues containing protein-polysaccharides or collagen as main constituents of the matrix. Electron microscopy and electron-ray microanalysis of dentin and osteopetrotic bones].. Z Zellforsch Mikrosk Anat 1972;134(2):283-96.
    pubmed: 4119479
  14. Miller WA, Eick JD, Neiders ME. Inorganic components of the peritubular dentin in young human permanent teeth.. Caries Res 1971;5(3):264-78.
    pubmed: 5284352doi: 10.1159/000259752google scholar: lookup
  15. BRUDEVOLD F, STEADMAN LT, SPINELLI MA, AMDUR BH, GRON P. A study of zinc in human teeth.. Arch Oral Biol 1963 Mar-Apr;8:135-44.
    pubmed: 14016161doi: 10.1016/0003-9969(63)90051-7google scholar: lookup
  16. Kumagai A, Fujita Y, Endo S, Itai K. Concentrations of trace element in human dentin by sex and age.. Forensic Sci Int 2012 Jun 10;219(1-3):29-32.
  17. Goldberg M, Kulkarni AB, Young M, Boskey A. Dentin: structure, composition and mineralization.. Front Biosci (Elite Ed) 2011 Jan 1;3(2):711-35.
    pmc: PMC3360947pubmed: 21196346doi: 10.2741/e281google scholar: lookup
  18. Cullity BD, Stock SR. Elements of X-ray Diffraction. Upper Saddle River, NJ: Prentice Hall; 2001.
  19. Bobyr E, Lassila JK, Wiersma-Koch HI, Fenn TD, Lee JJ, Nikolic-Hughes I, Hodgson KO, Rees DC, Hedman B, Herschlag D. High-resolution analysis of Zn(2+) coordination in the alkaline phosphatase superfamily by EXAFS and x-ray crystallography.. J Mol Biol 2012 Jan 6;415(1):102-17.
    pmc: PMC3249517pubmed: 22056344doi: 10.1016/j.jmb.2011.10.040google scholar: lookup
  20. Matsunaga K, Murata H, Mizoguchi T, Nakahira A. Mechanism of incorporation of zinc into hydroxyapatite.. Acta Biomater 2010 Jun;6(6):2289-93.
    pubmed: 19944784doi: 10.1016/j.actbio.2009.11.029google scholar: lookup
  21. Weiner S, Veis A, Beniash E, Arad T, Dillon JW, Sabsay B, Siddiqui F. Peritubular dentin formation: crystal organization and the macromolecular constituents in human teeth.. J Struct Biol 1999 Jun 1;126(1):27-41.
    pubmed: 10329486doi: 10.1006/jsbi.1999.4096google scholar: lookup
  22. Gotliv BA, Robach JS, Veis A. The composition and structure of bovine peritubular dentin: mapping by time of flight secondary ion mass spectroscopy.. J Struct Biol 2006 Nov;156(2):320-33.
    pubmed: 16600633doi: 10.1016/j.jsb.2006.02.005google scholar: lookup
  23. Gotliv BA, Veis A. Peritubular dentin, a vertebrate apatitic mineralized tissue without collagen: role of a phospholipid-proteolipid complex.. Calcif Tissue Int 2007 Sep;81(3):191-205.
    pubmed: 17674072doi: 10.1007/s00223-007-9053-xgoogle scholar: lookup
  24. Bertassoni LE, Stankoska K, Swain MV. Insights into the structure and composition of the peritubular dentin organic matrix and the lamina limitans.. Micron 2012 Feb;43(2-3):229-36.
    pubmed: 21890367doi: 10.1016/j.micron.2011.08.003google scholar: lookup
  25. Weiner S, Wagner HD. The material bone: Structure-mechanical function relations. Annu Rev Mater Sci 1998;28:271–298.
  26. Ten Cate AR. Oral histology: Development, structure and function. St Louis: Mosby; 1980.
  27. Yamakoshi Y, Hu JC, Iwata T, Kobayashi K, Fukae M, Simmer JP. Dentin sialophosphoprotein is processed by MMP-2 and MMP-20 in vitro and in vivo.. J Biol Chem 2006 Dec 15;281(50):38235-43.
    pubmed: 17046814doi: 10.1074/jbc.m607767200google scholar: lookup
  28. Sulkala M, Tervahartiala T, Sorsa T, Larmas M, Salo T, Tjäderhane L. Matrix metalloproteinase-8 (MMP-8) is the major collagenase in human dentin.. Arch Oral Biol 2007 Feb;52(2):121-7.
  29. Mazzoni A, Pashley DH, Tay FR, Gobbi P, Orsini G, Ruggeri A Jr, Carrilho M, Tjäderhane L, Di Lenarda R, Breschi L. Immunohistochemical identification of MMP-2 and MMP-9 in human dentin: correlative FEI-SEM/TEM analysis.. J Biomed Mater Res A 2009 Mar 1;88(3):697-703.
    pubmed: 18335530doi: 10.1002/jbm.a.31920google scholar: lookup
  30. Sulkala M, Pääkkönen V, Larmas M, Salo T, Tjäderhane L. Matrix metalloproteinase-13 (MMP-13, collagenase-3) is highly expressed in human tooth pulp.. Connect Tissue Res 2004;45(4-5):231-7.
    pubmed: 15763932doi: 10.1080/03008200490885788google scholar: lookup
  31. Hirata A, Sugahara T, Nakamura H. Localization of runx2, osterix, and osteopontin in tooth root formation in rat molars.. J Histochem Cytochem 2009 Apr;57(4):397-403.
    pmc: PMC2664981pubmed: 19124839doi: 10.1369/jhc.2008.952192google scholar: lookup
  32. Chen S, Gluhak-Heinrich J, Wang YH, Wu YM, Chuang HH, Chen L, Yuan GH, Dong J, Gay I, MacDougall M. Runx2, osx, and dspp in tooth development.. J Dent Res 2009 Oct;88(10):904-9.
    pmc: PMC3045537pubmed: 19783797doi: 10.1177/0022034509342873google scholar: lookup
  33. Falla-Sotelo FO, Rizzutto MA, Tabacniks MH, Added N, Barbosa MDL, Markarian RA, Quinelato A, Mori M, Youssef M. Analysis and discussion of trace elements in teeth of different animal species. Braz J Phys 2005;35:761–762.
  34. Zoeger N, Streli C, Wobrauschek P. Determination of the elemental distribution in human joint bones by SR micro XRF. X-Ray Spectrom 2008;37:3–11.

Citations

This article has been cited 7 times.
  1. Besnard C, Marie A, Sasidharan S, Harper RA, Shelton RM, Landini G, Korsunsky AM. Synchrotron X-ray Studies of the Structural and Functional Hierarchies in Mineralised Human Dental Enamel: A State-of-the-Art Review.. Dent J (Basel) 2023 Apr 7;11(4).
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  2. Stock SR. On `Flexible design in the stomatopod dactyl club'.. IUCrJ 2023 May 1;10(Pt 3):251-252.
    doi: 10.1107/S2052252523003408pubmed: 37079401google scholar: lookup
  3. Brozou A, Mannino MA, Van Malderen SJM, Garrevoet J, Pubert E, Fuller BT, Dean MC, Colard T, Santos F, Lynnerup N, Boldsen JL, Jørkov ML, Soficaru AD, Vincze L, Le Cabec A. Using SXRF and LA-ICP-TOFMS to Explore Evidence of Treatment and Physiological Responses to Leprosy in Medieval Denmark.. Biology (Basel) 2023 Jan 25;12(2).
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  4. Sui T, Dluhoš J, Li T, Zeng K, Cernescu A, Landini G, Korsunsky AM. Structure-Function Correlative Microscopy of Peritubular and Intertubular Dentine.. Materials (Basel) 2018 Aug 21;11(9).
    doi: 10.3390/ma11091493pubmed: 30134596google scholar: lookup
  5. Dean C, Le Cabec A, Spiers K, Zhang Y, Garrevoet J. Incremental distribution of strontium and zinc in great ape and fossil hominin cementum using synchrotron X-ray fluorescence mapping.. J R Soc Interface 2018 Jan;15(138).
    doi: 10.1098/rsif.2017.0626pubmed: 29321271google scholar: lookup
  6. Stock SR, Seto J, Deymier AC, Rack A, Veis A. Growth of second stage mineral in Lytechinus variegatus.. Connect Tissue Res 2018 Jul;59(4):345-355.
    doi: 10.1080/03008207.2017.1391233pubmed: 29083939google scholar: lookup
  7. Stock SR. The Mineral-Collagen Interface in Bone.. Calcif Tissue Int 2015 Sep;97(3):262-80.
    doi: 10.1007/s00223-015-9984-6pubmed: 25824581google scholar: lookup