The Macromolecular Organization of Dentine Matrix Collagen. I. Characterization of Dentine Collagen<sup>*</sup>

Veis, Arthur; Schlueter, Robert J.

doi:10.1021/bi00899a009

Cited by 137 publications

(42 citation statements)

References 24 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Although these agents are commonly used in commercial dentin etchants, it is well known that they are not good solvents for dentin collagen. 24 Previous authors have speculated that most smear layers are created under conditions that generate either high temperatures or high shear forces, which may lead to denaturation of surface collagen. 2,22 The Raman results shown in Figure 3 indicate that the mineral within the smear debris was accessible to EDTA but not readily accessible to the acid.…”

Section: Discussionmentioning

confidence: 99%

Analysis of acid‐treated dentin smear debris and smear layers using confocal Raman microspectroscopy

Wang

Spencer

2002

J. Biomed. Mater. Res.

View full text Add to dashboard Cite

Smear layers are generally present on any dentin surface prepared with cutting instruments and are often the only available substrate for bonding. It is commonly reported that acid removes these layers, but to date there has been no chemical evidence to support this observation. Confocal Raman microspectroscopy was used to investigate changes in the composition and molecular structure of acid-treated smear debris and in situ dentin smear layers. The exposed dentin in human molars was abraded with 600-grit silicon carbide sandpaper. Raman spectra were acquired on the smear debris and collected from the sandpaper before and after treatment with 10% citric acid, 35% H3PO4, or 0.5M ethylenediaminetetraacetic acid (EDTA). The resultant smeared dentin samples were treated with one of the aforementioned reagents, and spectra were acquired at 1.0-microm intervals across the interfaces of the smear layers/demineralized dentin/mineralized dentin. Corresponding specimens were morphologically analyzed with scanning electron microscopy (SEM). The results showed that the composition of the smear debris and the in situ smear layers was a mixture of disorganized collagen and mineral. Spectral changes in the smear debris suggested that the disorganized collagen was denatured by acid treatment. The denatured collagen formed a gelatinous matrix around the mineral in the smear layer, thereby shielding it from the acid. The smear layers were not apparent in the SEM micrographs of acid-etched dentin prepared and processed with conventional techniques. The micro-Raman spectroscopic results presented in this study provide the first direct evidence that partially denatured collagen within smear layers is not removed and that the mineral is only partially removed with acids that represent conventional dentin adhesive etchants.

show abstract

Section: Discussionmentioning

confidence: 99%

Analysis of acid‐treated dentin smear debris and smear layers using confocal Raman microspectroscopy

Wang

Spencer

2002

J. Biomed. Mater. Res.

View full text Add to dashboard Cite

show abstract

“…Although much of the early work attempted to show that the collagen fibrils were responsible for the placement and induction of mineral deposition, this proposition was never verified. Instead, attention began to focus on the non-collagenous protein components of the matrix (Herring and Kent, 1963;Schlueter and Veis, 1964;Veis and Schlueter, 1964;Spector and Glimcher, 1972;Veis et al, 1972;Glimcher, 1976), especially since it was recognized that, as a class, the non-collagenous extracellular proteins (NCP) shared a common char360Crit Rev Oral Biol Med 8(4) …”

mentioning

confidence: 99%

Phosphorylation of the Proteins of the Extracellular Matrix of Mineralized Tissues By Casein Kinase-Like Activity

Veis

Sfeir

1997

Critical Reviews in Oral Biology & Medicine

Self Cite

View full text Add to dashboard Cite

The extracellular matrix of the connective tissue contains non-collagenous proteins (NCP) which are acidic in character. The NCP of mineralizing systems (bone, dentin) differ from those of the non-mineralizing systems (skin, tendon) in that the mineralized tissue NCP are frequently phosphorylated. The phosphorylated proteins have been implicated in various aspects of the mineralization process. Thus, it is of interest to consider the mechanism and regulation of phosphorylation of the major matrix NCP. The majority of the phosphorylation takes place at Ser or Thr residues embedded within acidic sequences, and therefore are targets for casein kinase I (CKI ) or casein kinase 11 (CK2)-like kinases. CKI and CK2 are distantly related members of the protein kinase family. They are ubiquitous, constitutively active, second-messenger-independent kinases. CKI is found in a variety of isoforms, all homologous to the cx-subunit of the protein kinase family. It acts as a monomer. The active form of CK2 is a tetrameric holoenzyme, with 2 cx catalytic subunits and 2 ( regulatory subunits. The CK2 ac has activity alone, but the holoenzyme is four-to five-fold that activity. CK2 can use either ATP or GTP as the phosphate donor, but CK 1 can use only ATP. The CK2 activity which phosphorylates the mineralized tissue NCP appears to be localized to membraneassociated cell fractions, and is present in the endoplasmic reticulum and Golgi compartments in osteoblasts, where phosphorylation of the secreted proteins appears to take place as co-and post-translational processes. Data Bone and dentin are tissues in which mineral deposits of carbonate apatite form in an orderly fashion within a pre-formed collagen fibril matrix. Structural studies clearly show that the majority of the mineral phase is composed of carbonate-apatite crystals, whose crystal c-axes are aligned with the fibril axes of the collagen fibrils (FittonJackson, 1957;Glimcher and Krane, 1968;Glimcher, 1976;Weiner and Traub, 1986;Arsenault, 1988;Arsenault et al, 1991;Landis et al., 1992). Although much of the early work attempted to show that the collagen fibrils were responsible for the placement and induction of mineral deposition, this proposition was never verified. Instead, attention began to focus on the non-collagenous protein components of the matrix (Herring and Kent, 1963;Schlueter and Veis, 1964;Veis and Schlueter, 1964;Spector and Glimcher, 1972;Veis et al., 1972;Glimcher, 1976), especially since it was recognized that, as a class, the non-collagenous extracellular proteins (NCP) shared a common char360Crit Rev Oral Biol Med 8(4)

show abstract

“…Levels of inorganic components have been reported to be reduced, and organic components such as collagen become exposed in demineralized dentin. [11][12][13][14] Gwinett reported that the volume of dentin collagen demineralized by acids depended on its moisture content, and that dentin collagen showed shrinkage under dry conditions. 13 Veis and Schlueter reported that collagen in demineralized dentin was different from, and more swollen than, skin collagen.…”

Section: Figmentioning

confidence: 99%

“…13 Veis and Schlueter reported that collagen in demineralized dentin was different from, and more swollen than, skin collagen. 14 In other words, demineralized dentin represents dentin with no inorganic components, and its exposure to acid degenerated the collagen. 11 It has been suggested that such an exposed collagen network contains a large amount of moisture originating from saliva.…”

Section: Figmentioning

confidence: 99%

Effect of Dentin Hardness on Ablation Rate with Er:YAG Laser

Osuka

Amagai²,

Kukidome³

et al. 2009

Photomedicine and Laser Surgery

View full text Add to dashboard Cite

Objective: This study used artificially demineralized bovine dentin to ascertain the effect of hardness of demineralized dentin on ablation rate with the Er:YAG laser. Background Data: Before restoration of carious teeth, it is necessary to ablate any infected dentin that cannot be remineralized due to softening by the invading caries. A correlation has been suggested between the ablation efficiency of the Er:YAG laser and the progression of caries in dentin. To the best of our knowledge, no studies have investigated the relationship between degree of demineralization by dentinal caries and ablation rate with the Er:YAG laser. Materials and Methods: Bovine mandibular anterior tooth roots were used as dentin samples. Each sample was soaked in a demineralizing solution (2 M lactic acid, pH 4.0) for 3 d to obtain demineralized dentin (DD) samples. Another group of samples were prepared without demineralization as a sound dentin (SD) group for comparison. After determining the Knoop hardness number (KHN) of each sample, the dentin surface was ablated with an Er:YAG laser. Tip output and pulse rate were set at 50 mJ and 20 pulses per second (pps), respectively, and the water spray was set at 3.5 mL/min. Ablation width, depth, and volume were measured following irradiation. Results: In the DD group, dentin hardness was 10.4 Ϯ 1.6 KHN at 100 m from the surface. In the sound dentin group, Knoop hardness was 51.0 Ϯ 1.6 KHN cross-sectionally throughout. No differences were observed from the surface to a depth of 2000 m. In the DD group, dentin ablation volume at the superficial demineralized layer was 2888 Ϯ 272 ϫ 10 4 m. In the SD group, dentin ablation volume was 1298 Ϯ 219 m 3 . The relationship between ablation volume and Knoop hardness was defined as Yϭ -40.699x ϩ 3350, revealing a marked negative correlation. Conclusion:The results demonstrate that the ablation volume for demineralized dentin was greater than that for sound dentin. The results suggest that the Er:YAG laser is capable of ablating infected dentin without damaging sound dentin by adjustment of tip output and pulse rate. 395

show abstract

The Macromolecular Organization of Dentine Matrix Collagen. I. Characterization of Dentine Collagen^*

Cited by 137 publications

References 24 publications

Analysis of acid‐treated dentin smear debris and smear layers using confocal Raman microspectroscopy

Analysis of acid‐treated dentin smear debris and smear layers using confocal Raman microspectroscopy

Phosphorylation of the Proteins of the Extracellular Matrix of Mineralized Tissues By Casein Kinase-Like Activity

Effect of Dentin Hardness on Ablation Rate with Er:YAG Laser

Contact Info

Product

Resources

About

The Macromolecular Organization of Dentine Matrix Collagen. I. Characterization of Dentine Collagen*

Cited by 137 publications

References 24 publications

Analysis of acid‐treated dentin smear debris and smear layers using confocal Raman microspectroscopy

Analysis of acid‐treated dentin smear debris and smear layers using confocal Raman microspectroscopy

Phosphorylation of the Proteins of the Extracellular Matrix of Mineralized Tissues By Casein Kinase-Like Activity

Effect of Dentin Hardness on Ablation Rate with Er:YAG Laser

Contact Info

Product

Resources

About

The Macromolecular Organization of Dentine Matrix Collagen. I. Characterization of Dentine Collagen^*