bluuebunny/crossref_metadata_2025_split huggingface dataset:
Evaluation of phosphorus management practices in East Mediterranean altered wetland soils
Authors: Barnea I. , Litaor M. I. , Shenker M. 
Published: January 2012

AbstractIn this study, we re‐examined the common practice of intensive P fertilization in altered wetland soils even when soil test (Olsen‐P) indicates sufficient P levels (>10 mg/kg). We tested the effects of P fertilization on crop performance and P leaching in 36 lysimeters (1.5 m3) filled with peat, marl or alluvial materials and compared a new bone‐char‐based fertilizer to the common superphosphate. The lysimeter experiment consisted of the two fertilizer types, two application rates and a typical crop rotation of setaria (Setaria italica), pea (Pisum sativum) and tomatoes (Lycopersicon esculentum). By the end of each crop rotation, the yield was evaluated relative to P‐fertilization rates and soil‐test P. P fertilization resulted in increased Olsen‐P, soil‐solution P and P loss through leachates and a slight quality yield advantage in pea and tomato with no increase in yield of any crop. P budget calculations showed that plant uptake was not affected by the amount or type of applied P. We concluded that P fertilizer application should be significantly reduced because of limited crop response and increased P concentrations in leachates that may increase P loss to waterways especially in the marl soils. The ABC Protector exhibited slow P release, but its environmental implications should be further studied.
Calcified neurocysticercosis lesions and hippocampal sclerosis: Potential dual pathology?
Authors: Rathore Chaturbhuj , Thomas Bejoy , Kesavadas Chandrasekharan , Radhakrishnan Kurupath 
Published: January 2012

SummaryIn areas where cysticercosis is endemic, calcified neurocysticercosis lesion(s) (CNL) and hippocampal sclerosis (HS) commonly coexist in patients with localization‐related epilepsies. To understand the pathogenesis of HS associated with CNL, we compared the characteristics of three groups of patients with antiepileptic drug–resistant epilepsies: CNL with HS, CNL without HS (CNL alone), and HS without CNL (HS alone). In comparison to patients with CNL alone, those with CNL with HS had CNL more frequently located in the ipsilateral temporal lobe. Those with CNL with HS had a lower incidence of febrile seizures, older age at initial precipitating injury and at onset of habitual complex partial seizures, and more frequent clustering of seizures and extratemporal/bitemporal interictal epileptiform discharges as compared to patients with HS alone. Our study illustrates that HS associated with CNL might have a different pathophysiologic basis as compared to classical HS.
3T Magnetic Resonance Neurography of Tibial Nerve Pathologies
Authors: Chalian Majid , Soldatos Theodoros , Faridian‐Aragh Neda , Williams Eric H. , Rosson Gedge D. , Eng John , Carrino John A. , Chhabra Avneesh 
Published: January 2012

ABSTRACTDiagnosis of tibial neuropathy has been traditionally based on clinical examination and electrodiagnostic studies; however, cross‐sectional imaging modalities have been used to increase the diagnostic accuracy and provide anatomic mapping of the abnormalities. In this context, magnetic resonance neurography (MRN) offers high‐resolution imaging of the tibial nerve (TN), its branches and the adjacent soft tissues, and provides an objective assessment of the neuromuscular anatomy, abnormality, and the surrounding pathology. This review describes the pathologies affecting the TN and illustrates their respective 3 Tesla (T) MRN appearances with relevant case examples.
Characterization of kallikrein‐related peptidase 4 glycosylations
Authors: Yamakoshi Yasuo , Yamakoshi Fumiko , Hu Jan C‐C. , Simmer James P. 
Published: January 2012

Yamakoshi Y, Yamakoshi F, Hu JC‐C, Simmer JP. Characterization of kallikrein‐related peptidase 4 glycosylations.

Eur J Oral Sci 2011; 119 (Suppl. 1): 234–240. © 2011 Eur J Oral SciKallikrein‐related peptidase 4 (KLK4) is a glycosylated serine protease that functions in the maturation (hardening) of dental enamel. Pig and mouse KLK4 contain three potential N‐glycosylation sites. We isolated KLK4 from developing pig and mouse molars and characterized their N‐glycosylations. N‐glycans were enzymatically released by digestion with N‐glycosidase F and fluorescently labeled with 2‐aminobenzoic acid. Normal‐phase high‐performance liquid chromatography (NP‐HPLC) revealed N‐glycans with no, or with one, two, or three sialic acid attachments in pig KLK4 and with no, or with one or two sialic acid attachments in mouse KLK4. The labeled N‐glycans were digested with sialidase to generate the asialo N‐glycan cores that were fractionated by reverse‐phase HPLC, and their retention times were compared with similarly labeled glycan standards. The purified cores were characterized by mass spectrometric and monosaccharide composition analyses. We determined that pig and mouse KLK4 have NA2 and NA2F biantennary N‐glycan cores. The pig triantennary core is NA3. The mouse triantennary core is NA3 with a fucose connected by an α1‐6 linkage, indicating that it is attached to the first N‐acetyglucosamine (NA3F). We conclude that pig KLK4 has NA2, NA2F, and NA3 N‐glycan cores with no, or with one, two, or three sialic acids. Mouse KLK4 has NA2, NA2F, and NA3F N‐glycan cores with no, or with one or two sialic acids.
Identification of Amelotin‐ and ODAM‐interacting enamel matrix proteins using the yeast two‐hybrid system
Authors: Holcroft James , Ganss Bernhard 
Published: January 2012

Holcroft J, Ganss B. Identification of Amelotin‐ and ODAM‐interacting enamel matrix proteins using the yeast two‐hybrid system.  Eur J Oral Sci 2011; 119 (Suppl. 1): 301–306. © 2011 Eur J Oral SciThe formation of dental enamel is a prototype of functional tissue development through biomineralization. Amelotin (AMTN) is a recently discovered secreted enamel protein predominantly expressed during the maturation stage of enamel formation. It accumulates in a basal lamina‐like structure at the interface between ameloblasts and enamel mineral and it co‐localizes with another recently described enamel protein, odontogenic ameloblast‐associated protein (ODAM). The purpose of this study was to determine whether AMTN and ODAM bind to each other and/or to other well‐established enamel matrix proteins. The coding sequences of all enamel proteins were cloned into appropriate vectors of the GAL4‐based Matchmaker Gold Yeast Two‐Hybrid System. The growth of yeast cells on selective media and color induction were used as indicators for reporter gene expression through protein–protein interactions in combinations of prey and bait constructs. We found that AMTN interacts with itself and with ODAM, but not with amelogenin (AMEL), ameloblastin (AMBN), or enamelin (ENAM). Using ODAM as bait, the interaction with AMTN was confirmed. Furthermore, ODAM was found to bind to itself and to AMBN, as well as weakly to AMEL but not to ENAM. We propose a model where the distinct expression of AMTN and ODAM and their interaction are involved in defining the enamel microstructure at the enamel surface.
Wnt‐RhoA signaling is involved in dental enamel development
Authors: Peng Li , Li Yong , Shusterman Kate , Kuehl Melissa , Gibson Carolyn W. 
Published: January 2012

Peng L, Li Y, Shusterman K, Kuehl M, Gibson CW. Wnt‐RhoA signaling is involved in dental enamel development.

Eur J Oral Sci 2011; 119 (Suppl. 1): 41–49. © 2011 Eur J Oral SciTransgenic mice that express dominant‐negative RhoA (RhoADN) in ameloblasts have hypoplastic enamel with defects in molar cusps. β‐catenin and Wnt5a were up‐regulated in enamel organs of RhoADN transgenic mice, which indicated that both canonical and non‐canonical Wnt pathways are implicated in the process of enamel defect formation. It was hypothesized that expression of RhoADN in ameloblasts interfered with normal enamel development through the pathways that were induced by fluoride. The Wnt and RhoA pathways were further investigated in an ameloblast‐lineage cell line (ALC) by treatment with sodium fluoride (NaF). The activities of RhoA and Rho‐associated protein kinase (ROCK) II decreased significantly by 8–12 hours, similar to decreased activity in RhoADN transgenic mice. Both canonical and non‐canonical Wnt pathways were activated by treatment with NaF, which was verified by western blotting and the β‐catenin‐TCF/LEF (T cell factor lymphanoid/enhancer factor) reporter gene (TOPflash) assay. β‐catenin localization to both cytoplasm and nucleus was up‐regulated in NaF‐treated ALC, while Gsk‐3β, the negative regulator of the Wnt pathway, showed a decreased pattern of expression. The current results indicate that both Wnt and RhoA pathways are implicated in fluoride‐induced signaling transductions in the ALC as well as in the development of enamel defects in RhoADN transgenic mice.
The role of amelogenin during enamel‐crystallite growth and organization in vivo
Authors: Wright J. Tim , Li Yong , Suggs Cynthia , Kuehl Melissa A. , Kulkarni Ashok B. , Gibson Carolyn W. 
Published: January 2012

Wright JT, Li Y, Suggs C, Kuehl MA, Kulkarni AB, Gibson CW. The role of amelogenin during enamel‐crystallite growth and organization in vivo.  Eur J Oral Sci 2011; 119 (Suppl. 1): 65–69. © 2011 Eur J Oral SciAmelogenin is critical for enamel formation, and human amelogenin gene (AMELX) mutations cause hypoplastic and/or hypomaturation enamel phenotypes. The Amelx null (AKO) mouse has a severe hypoplastic phenotype. This study evaluated the effect of amelogenin loss on enamel formation and crystallite morphology. Enamel from AKO and wild‐type (WT) mice was used. The AKO mice were mated with transgenic mice expressing the most abundant known amelogenin isoform, TgM180‐87, to rescue (KOM180‐87) the enamel crystallite phenotype. Molar enamel was embedded, sectioned with a diamond microtome, and images were obtained by transmission electron microscopy. The crystallite sizes from multiple sections were measured using Image J. The mean thicknesses (WT = 26 nm, AKO = 16 nm, and KOM180‐87 = 25 nm) and the mean widths (WT = 96 nm, AKO = 59 nm, KOM180‐87 = 85 nm) of crystallites were measured. Despite a complete loss of amelogenin in AKO mice, a mineralized enamel layer with well‐defined and organized crystallites is formed. In the absence of amelogenin, enamel crystallites were reduced in thickness and width. For the first time we show that introduction of the m180 amelogenin isoform into the AKO mouse through cross‐breeding rescues the crystallite phenotype. We conclude that amelogenin is essential for the development of normal crystallite size.
Ameloblastin regulates cell attachment and proliferation through RhoA and p27
Authors: Zhang Youbin , Zhang Xu , Lu Xuanyu , Atsawasuwan Phimon , Luan Xianghong 
Published: January 2012

Zhang Y, Zhang X, Lu X, Atsawasuwan P, Luan X. Ameloblastin regulates cell attachment and proliferation through RhoA and p27.

Eur J Oral Sci 2011; 119 (Suppl. 1): 280–285. © 2011 Eur J Oral SciThe matrix adhesion protein ameloblastin (AMBN) is one of the unique components of the mineralizing matrix of bones and teeth. Here we focused on two types of cells expressing AMBN – mouse dental follicle cells (mDF) and mouse periodontal ligament cells (mPDL) – to decipher AMBN function in developing dental, periodontal, and bone tissues. To test AMBN function, cell culture dishes of mDF and mPDL were exposed to either full‐length or C‐terminal (amino acids 137–407) recombinant Ambn protein. Alternatively, cells were subjected to transient transfection using an Ambn– small hairpin (sh) RNA vector. Our cell culture studies documented that dishes coated with full‐length AMBN promoted the attachment of mPDL and mDF cells as early as 1 h after seeding. In order to identify potential intermediaries that might aid the effect of AMBN on adhesion, RhoA expression levels in AMBN‐coated and uncoated control dishes were assessed. These studies indicated that AMBN induced RhoA expression 4 h after seeding, especially in mPDL cells. After 4 h of culture, the cell cycle inhibitor p27 was also up‐regulated. In addition, exogenous AMBN and its C‐terminal fragment reduced the proliferation of mDF and mPDL. Finally, transient transfection of mDF and mPDL cells with the Ambn–shRNA vector resulted in the down‐regulation of p27 in mPDL cells. Together, these data indicate that AMBN affects cell adhesion via RhoA and cell cycle progression through p27.
Exclusion of all three calbindins from a calcium‐ferry role in rat enamel cells
Authors: Hubbard Michael J. , McHugh Nicola J. , Mangum Jonathan E. 
Published: January 2012

Hubbard MJ, McHugh NJ, Mangum JE. Exclusion of all three calbindins from a calcium‐ferry role in rat enamel cells.  Eur J Oral Sci 2011; 119 (Suppl. 1): 112–119. © 2011 Eur J Oral SciIt is widely accepted that healthy enamel formation depends on a steady supply of calcium, yet only fragmentary understanding exists about the mechanisms underlying transepithelial calcium transport. Several lines of evidence indicate that calcium principally follows a transcellular route, which classically is thought to be facilitated by cytosolic calcium‐binding proteins termed calbindins. In enamel cells, however, this ‘calcium‐ferry’ dogma appears to fail as we previously found that the major calbindin in murine enamel cells (calbindin‐28 kDa) was down‐regulated during the peak period of calcium transport and enamel was formed normally in mice lacking calbindin‐28 kDa. It remains to be clarified whether the two other known calbindins could function as calcium ferries instead. This study used biochemical and proteomic approaches to obtain definitive identification and quantification of the 30‐kDa calbindin (calretinin) and calbindin‐9 kDa (S100‐G) in enamel epithelium from rat. By establishing that both of these calbindins contribute insufficient calcium capacities in molars and incisors, our results render the calcium‐ferry dogma untenable. Of significance to enamel defects and dental bioengineering, these findings support other evidence for an alternative organelle‐based mode of calcium transport (calcium transcytosis) and also implicate S100‐G/calbindin‐9 kDa, but not calretinin, in a calcium‐signaling role during enamel maturation.
Molecular evolution of matrix metalloproteinase 20
Authors: Kawasaki Kazuhiko , Suzuki Tohru 
Published: January 2012

Kawasaki K, Suzuki T. Molecular evolution of matrix metalloproteinase 20. Eur J Oral Sci 2011; 119 (Suppl. 1): 247–253. © 2011 Eur J Oral SciDental enamel is a hypermineralized tissue, containing only trace amounts of organic components. During enamel formation, matrix metalloproteinase 20 (MMP20) processes proteins comprising enamel matrix and facilitates hypermineralization. In the human genome, 24 distinct MMP genes have been identified. Among these genes,MMP20is clustered with eight other genes, includingMMP13, and all these clustered genes show phylogenetically close relationships. In this study, we investigatedMMP20and closely related MMP genes in various tetrapods and in a teleost fish, fugu. In the genome of the chicken, a toothless tetrapod, we identified degraded exons ofMMP20, which supports the previous proposition thatMMP20is important specifically for enamel formation. Nevertheless, for unknown reasons, we failed to identifyMMP20in the platypus genome. In the opossum, lizard, and frog genomes,MMP20was found clustered withMMP13. Furthermore, in the fugu genome, we identified anMMP20‐like gene located adjacent toMMP13, suggesting thatMMP20arose before the divergence of ray‐finned fish and lobe‐finned fish. The teleost tooth surface is covered with enameloid, a hypermineralized tissue different from enamel. Thus, we hypothesize thatMMP20could have been used in an ancient hypermineralized tissue, which evolved into enameloid in teleosts and into enamel in tetrapods.
Enamel matrix derivative stimulates expression and secretion of resistin in mesenchymal cells
Authors: Obregon‐Whittle Maria V. , Stunes Astrid K. , Almqvist Sofia , Brookes Steven J. , Lee James D. , Syversen Unni , Lyngstadaas Staale P. , Reseland Janne E. 
Published: January 2012

Obregon‐Whittle MV, Stunes AK, Almqvist S, Brookes SJ, Lee JD, Syversen U, Lyngstadaas SP, Reseland JE. Enamel matrix derivative stimulates expression and secretion of resistin in mesenchymal cells.  Eur J Oral Sci 2011; 119 (Suppl. 1): 366–372. © 2011 Eur J Oral SciIn this study we wanted to identify the effect of enamel matrix derivative (EMD) on adipocytokines, so‐called adipokines. Primary human cells of mesenchymal origin (osteoblasts, periodontal ligament cells, mesenchymal stem cells, and pulp cells) and hematopoietic origin (monocytes) were incubated with EMD. The levels of adipokines in cell culture medium were quantified using the Lincoplex human adipocyte panel (Luminex) and by real‐time PCR of mRNA isolated from cell lysates. Rats were injected with 2 mg of EMD or saline intramuscularly every third day for 14 d. Blood samples were taken before and after injections, and the level of resistin in rat plasma was measured by ELISA. We found a dramatic increase in the secretion of resistin from mesenchymal stem cells, and verified this result in all the cells of mesenchymal origin tested. However, we observed no significant changes in the amount of resistin secreted from monocytes exposed to EMD compared with the control. Injections of EMD significantly enhanced the circulating levels of resistin in rats, and EMD also significantly enhanced the activity of the resistin promoter in transfected mesenchymal stem cells, indicating a direct effect on resistin expression. Our results indicate that resistin may play a role in mediating the biological effect of EMD in mesenchymal tissues.
Epithelial‐specific knockout of the Rac1 gene leads to enamel defects
Authors: Huang Zhan , Kim Jieun , Lacruz Rodrigo S. , Bringas Jr Pablo , Glogauer Michael , Bromage Timothy G. , Kaartinen Vesa M. , Snead Malcolm L. 
Published: January 2012

Huang Z, Kim J, Lacruz RS, Bringas P Jr, Glogauer M, Bromage TG, Kaartinen VM, Snead ML. Epithelial‐specific knockout of the Rac1 gene leads to enamel defects.  Eur J Oral Sci 2011; 119 (Suppl. 1): 168–176. © 2011 Eur J Oral SciThe Ras‐related C3 botulinum toxin substrate 1 (Rac1) gene encodes a 21‐kDa GTP‐binding protein belonging to the RAS superfamily. RAS members play important roles in controlling focal adhesion complex formation and cytoskeleton contraction, activities with consequences for cell growth, adhesion, migration, and differentiation. To examine the role(s) played by RAC1 protein in cell–matrix interactions and enamel matrix biomineralization, we used the Cre/loxP binary recombination system to characterize the expression of enamel matrix proteins and enamel formation in Rac1 knockout mice (Rac1−/−). Mating between mice bearing the floxed Rac1 allele and mice bearing a cytokeratin 14‐Cre transgene generated mice in which Rac1 was absent from epithelial organs. Enamel of the Rac1 conditional knockout mouse was characterized by light microscopy, backscattered electron imaging in the scanning electron microscope, microcomputed tomography, and histochemistry. Enamel matrix protein expression was analyzed by western blotting. Major findings showed that the Tomes’ processes of Rac1−/− ameloblasts lose contact with the forming enamel matrix in unerupted teeth, the amounts of amelogenin and ameloblastin are reduced in Rac1−/− ameloblasts, and after eruption, the enamel from Rac1−/− mice displays severe structural defects with a complete loss of enamel. These results support an essential role for RAC1 in the dental epithelium involving cell–matrix interactions and matrix biomineralization.
Ameloblastin‐rich enamel matrix favors short and randomly oriented apatite crystals
Authors: Lu Xuanyu , Ito Yoshihiro , Kulkarni Ashok , Gibson Carolyn , Luan Xianghong , Diekwisch Thomas G. H. 
Published: January 2012

Lu X, Ito Y, Kulkarni A, Gibson C, Luan X, Diekwisch TGH. Ameloblastin‐rich enamel matrix favors short and randomly oriented apatite crystals.

Eur J Oral Sci 2011; 119 (Suppl. 1): 254–260. © 2011 Eur J Oral SciMolecular evolution studies suggest that amelogenin (AMELX), the principal component of the mammalian enamel matrix, emerged considerably later than ameloblastin (AMBN), and enamelin. Here, we created a transgenic mouse model to ask the question how a conceivable basal enamel lacking AMELX and enriched in the more basal AMBN might compare with recent mouse enamel. To answer this question we overexpressed AMBN using a keratin 14 (K14) promoter and removed AMELX from the genetic background by crossbreeding with amelx−/− mice. Enamel coverings of amelx−/− mice and of the squamate Iguana iguana were used for comparison. Scanning electron microscopic analysis documented that AMBN transgenic (TG) × amelx−/− mouse molars were covered by a 5 μm thin ‘enameloid’ layer resembling the thin enamel of the Iguana squamate. Transmission electron microscopy revealed that the enamel of developing AMBN TG × amelx−/− mouse molars contained short (approximately 70 nm) and randomly oriented crystals, while WT controls, AMBN overexpressors, and AMELX−/− mice all featured elongated and parallel oriented crystals measuring between 300 and 600 nm in average length. Together, these studies illustrate that AMBN promotes the growth of a crystalline enamel layer with short and randomly oriented crystals, but lacks the ability to facilitate the formation of long and parallel oriented apatite crystals.
Enamel alterations in serotonin 2B receptor knockout mice
Authors: Harichane Yassine , Dimitrova‐Nakov Sasha , Marchadier Arnaud , Collet Corinne , Baudry Anne , Vidal Catherine , Kamoun‐Goldrat Agnès , Kellermann Odile , Goldberg Michel 
Published: January 2012

Harichane Y, Dimitrova‐Nakov S, Marchadier A, Collet C, Baudry A, Vidal C, Kamoun‐Goldrat A, Kellermann O, Goldberg M. Enamel alterations in serotonin 2B receptor knockout mice.

Eur J Oral Sci 2011; 119 (Suppl. 1): 177–184. © 2011 Eur J Oral SciThe role of the serotonin 2B receptor (5‐HT2BR) in enamel formation and mineralization was explored in adult 5HT2BR knockout (KO) mice compared with wild‐type (WT) mice. In the molar, quantitative data obtained by micro‐computed tomography imaging showed that the overall volume of the enamel layer was firmly reduced in KO mice. Defective mineralization was ascertained by energy‐dispersive X‐ray microanalysis. We also observed, using scanning electron microscopy, that parazones in the KO mice included two or three helicoidally twisted rods within Hunter–Schreger bands, instead of a single rod, as found in the WT mice. Minor disturbances were also detected in the incisors of KO mice. Structural modifications, thinner enamel crystallites, and porosities observed in KO mice indicate that the 5‐HT2BR‐mediated signaling pathways as part of the enamel formation process. These data provide a basis for evaluating the role of 5‐HT2BR in ameloblast functions. Defects observed in the mineralization and structure of enamel in KO mice highlight that the 5‐HT2BR interferes with the mechanisms directing amelogenesis.