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[PMID]: 28747404
[Au] Autor:Lim H; Yu CY; Jou TS
[Ad] Address:Graduate Institute of Molecular Medicine National Taiwan University, Taipei, Taiwan.
[Ti] Title:Galectin-8 regulates targeting of Gp135/podocalyxin and lumen formation at the apical surface of renal epithelial cells.
[So] Source:FASEB J;31(11):4917-4927, 2017 11.
[Is] ISSN:1530-6860
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Establishment of apical-basal polarity, through correct targeting of polarity determinants to distinct domains of the plasma membrane, is a fundamental process for the development of functioning epithelial tubules. Here we report that galectin (Gal)-8 regulates apical-basal polarity of Madin-Darby canine kidney (MDCK) cells apical targeting of 135-kDa glycoprotein (Gp135). Gal-8 interacts with newly synthesized Gp135 in a glycan-dependent manner. Gal-8 knockdown induces aberrant lumens at the lateral domain and mistargeting of Gp135 to this structure, thus disrupting the kidney epithelial polarity of MDCK cells, which organize lumens at the apical surface. The -glycosylation deletion mutant of Gp135 phenocopies the effect of Gal-8 knockdown, which suggests that Gal-8 is the decoding machinery for the apical sorting signals of Gp135 residing at its -glycosylation-rich region. Collectively, our results reveal a new role of Gal-8 in the development of luminal organs by regulating targeting of apical polarity protein Gp135.-Lim, H., Yu, C.-Y., Jou, T.-S. Galectin-8 regulates targeting of Gp135/podocalyxin and lumen formation at the apical surface of renal epithelial cells.
[Mh] MeSH terms primary: Cell Polarity/physiology
Epithelial Cells/metabolism
Galectins/metabolism
Kidney/metabolism
Sialoglycoproteins/metabolism
[Mh] MeSH terms secundary: Animals
Dogs
Epithelial Cells/cytology
Galectins/genetics
Kidney/cytology
Madin Darby Canine Kidney Cells
Sialoglycoproteins/genetics
[Pt] Publication type:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Name of substance:0 (Galectins); 0 (Sialoglycoproteins); 0 (podocalyxin)
[Em] Entry month:1711
[Cu] Class update date: 180306
[Lr] Last revision date:180306
[Js] Journal subset:IM
[Da] Date of entry for processing:170728
[St] Status:MEDLINE
[do] DOI:10.1096/fj.201601386R

  2 / 9902 MEDLINE  
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[PMID]: 29259037
[Au] Autor:Falch CM; Sundaram AYM; Øystese KA; Normann KR; Lekva T; Silamikelis I; Eieland AK; Andersen M; Bollerslev J; Olarescu NC
[Ad] Address:Section of Specialized EndocrinologyDepartment of Endocrinology cafal14@student.sdu.dk.
[Ti] Title:Gene expression profiling of fast- and slow-growing non-functioning gonadotroph pituitary adenomas.
[So] Source:Eur J Endocrinol;178(3):295-307, 2018 Mar.
[Is] ISSN:1479-683X
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:OBJECTIVE: Reliable biomarkers associated with aggressiveness of non-functioning gonadotroph adenomas (GAs) are lacking. As the growth of tumor remnants is highly variable, molecular markers for growth potential prediction are necessary. We hypothesized that fast- and slow-growing GAs present different gene expression profiles and reliable biomarkers for tumor growth potential could be identified, focusing on the specific role of epithelial-mesenchymal transition (EMT). DESIGN AND METHODS: Eight GAs selected for RNA sequencing were equally divided into fast- and slow-growing group by the tumor volume doubling time (TVDT) median (27.75 months). Data were analyzed by tophat2, cufflinks and cummeRbund pipeline. 40 genes were selected for RT-qPCR validation in 20 GAs based on significance, fold-change and pathway analyses. The effect of silencing (metadherin) and (endomucin) on migration of human adenoma cells was evaluated. RESULTS: 350 genes were significantly differentially expressed (282 genes upregulated and 68 downregulated in the fast group, -adjusted <0.05). Among 40 selected genes, 11 showed associations with TVDT (-0.669< <-0.46, < 0.05). These were and six EMT-related genes ( and ). , but not , demonstrated involvement in cell migration and association with EMT markers. CONCLUSIONS: Fast- and slow-growing GAs present different gene expression profiles, and genes related to EMT have higher expression in fast-growing tumors. In addition to , identified as an important contributor to aggressiveness, the other genes might represent markers for tumor growth potential and possible targets for drug therapy.
[Mh] MeSH terms primary: Adenoma/genetics
Epithelial-Mesenchymal Transition/genetics
Pituitary Neoplasms/genetics
RNA, Messenger/metabolism
[Mh] MeSH terms secundary: Adaptor Proteins, Signal Transducing/genetics
Adenoma/metabolism
Adult
Aged
Cadherins/genetics
Cell Adhesion Molecules/genetics
Cell Movement/genetics
Cyclic AMP-Dependent Protein Kinase Catalytic Subunits/genetics
Female
Follicle Stimulating Hormone/metabolism
Gene Expression Profiling
Gene Expression Regulation, Neoplastic
Gene Silencing
Humans
In Vitro Techniques
Intracellular Signaling Peptides and Proteins/genetics
Luteinizing Hormone/metabolism
Male
Membrane Glycoproteins/genetics
Microtubule-Associated Proteins/genetics
Middle Aged
Myosin Type I/genetics
Nerve Tissue Proteins/genetics
Pituitary Neoplasms/metabolism
Proto-Oncogene Proteins/genetics
Receptors, Cell Surface/genetics
Reverse Transcriptase Polymerase Chain Reaction
Ribonucleases/genetics
Sialoglycoproteins/genetics
Time Factors
[Pt] Publication type:JOURNAL ARTICLE
[Nm] Name of substance:0 (Adaptor Proteins, Signal Transducing); 0 (Cadherins); 0 (Cell Adhesion Molecules); 0 (EMCN protein, human); 0 (GPM6A protein, human); 0 (Intracellular Signaling Peptides and Proteins); 0 (MTDH protein, human); 0 (MYO1B protein, human); 0 (Membrane Glycoproteins); 0 (Microtubule-Associated Proteins); 0 (Nerve Tissue Proteins); 0 (PCDH18 protein, human); 0 (Proto-Oncogene Proteins); 0 (RNA, Messenger); 0 (Receptors, Cell Surface); 0 (SKIL protein, human); 0 (SPAG9 protein, human); 0 (Sialoglycoproteins); 0 (UNC5H4 protein, human); 0 (hook1 protein, human); 9002-67-9 (Luteinizing Hormone); 9002-68-0 (Follicle Stimulating Hormone); EC 2.7.11.11 (Cyclic AMP-Dependent Protein Kinase Catalytic Subunits); EC 2.7.11.11 (PRKACB protein, human); EC 3.1.- (CNOT6L protein, human); EC 3.1.- (Ribonucleases); EC 3.6.1.- (Myosin Type I)
[Em] Entry month:1802
[Cu] Class update date: 180220
[Lr] Last revision date:180220
[Js] Journal subset:IM
[Da] Date of entry for processing:171221
[St] Status:MEDLINE
[do] DOI:10.1530/EJE-17-0702

  3 / 9902 MEDLINE  
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[PMID]: 29223396
[Au] Autor:Matsuishi YI; Kato H; Masuda K; Yamaza H; Hirofuji Y; Sato H; Wada H; Kiyoshima T; Nonaka K
[Ad] Address:Section of Oral Medicine for Children, Division of Oral Health, Growth and Development, Faculty of Dental Science, Kyushu University, 3-1-1 Maidashi, Higashi-Ku, Fukuoka 812-8582, Japan.
[Ti] Title:Accelerated dentinogenesis by inhibiting the mitochondrial fission factor, dynamin related protein 1.
[So] Source:Biochem Biophys Res Commun;495(2):1655-1660, 2018 01 08.
[Is] ISSN:1090-2104
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Undifferentiated odontogenic epithelium and dental papilla cells differentiate into ameloblasts and odontoblasts, respectively, both of which are essential for tooth development. These differentiation processes involve dramatic functional and morphological changes of the cells. For these changes to occur, activation of mitochondrial functions, including ATP production, is extremely important. In addition, these changes are closely related to mitochondrial fission and fusion, known as mitochondrial dynamics. However, few studies have focused on the role of mitochondrial dynamics in tooth development. The purpose of this study was to clarify this role. We used mouse tooth germ organ cultures and a mouse dental papilla cell line with the ability to differentiate into odontoblasts, in combination with knockdown of the mitochondrial fission factor, dynamin related protein (DRP)1. In organ cultures of the mouse first molar, tooth germ developed to the early bell stage. The amount of dentin formed under DRP1 inhibition was significantly larger than that of the control. In experiments using a mouse dental papilla cell line, differentiation into odontoblasts was enhanced by inhibiting DRP1. This was associated with increased mitochondrial elongation and ATP production compared to the control. These results suggest that DRP1 inhibition accelerates dentin formation through mitochondrial elongation and activation. This raises the possibility that DRP1 might be a therapeutic target for developmental disorders of teeth.
[Mh] MeSH terms primary: Dentinogenesis/physiology
Dynamins/antagonists & inhibitors
[Mh] MeSH terms secundary: Adenosine Triphosphate/biosynthesis
Ameloblasts/cytology
Ameloblasts/physiology
Animals
Cell Differentiation/genetics
Cell Differentiation/physiology
Cell Line
Dynamins/genetics
Dynamins/physiology
Extracellular Matrix Proteins/biosynthesis
Female
Mice
Mice, Inbred C57BL
Mitochondrial Dynamics/physiology
Odontoblasts/cytology
Odontoblasts/physiology
Organ Culture Techniques
Phosphoproteins/biosynthesis
Pregnancy
RNA, Small Interfering/genetics
Sialoglycoproteins/biosynthesis
Tooth Germ/cytology
Tooth Germ/embryology
[Pt] Publication type:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Name of substance:0 (Extracellular Matrix Proteins); 0 (Phosphoproteins); 0 (RNA, Small Interfering); 0 (Sialoglycoproteins); 0 (dentin sialophosphoprotein); 8L70Q75FXE (Adenosine Triphosphate); EC 3.6.5.5 (Dnm1l protein, mouse); EC 3.6.5.5 (Dynamins)
[Em] Entry month:1802
[Cu] Class update date: 180220
[Lr] Last revision date:180220
[Js] Journal subset:IM
[Da] Date of entry for processing:171211
[St] Status:MEDLINE

  4 / 9902 MEDLINE  
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[PMID]: 29362874
[Au] Autor:Bigham AW; Magnaye K; Dunn DM; Weiss RB; Bamshad M
[Ad] Address:Department of Anthropology, The University of Michigan, 222C West Hall, 1085 S. University, Ann Arbor, MI, 48109-1107, USA. awbigham@umich.edu.
[Ti] Title:Complex signatures of natural selection at GYPA.
[So] Source:Hum Genet;137(2):151-160, 2018 Feb.
[Is] ISSN:1432-1203
[Cp] Country of publication:Germany
[La] Language:eng
[Ab] Abstract:The human MN blood group antigens are isoforms of glycophorin A (GPA) encoded by the gene, GYPA, and are the most abundant erythrocyte sialoglycoproteins. The distribution of MN antigens has been widely studied in human populations yet the evolutionary and/or demographic factors affecting population variation remain elusive. While the primary function of GPA is yet to be discovered, it serves as the major binding site for the 175-kD erythrocyte-binding antigen (EB-175) of the malarial parasite, Plasmodium falciparum, a major selective pressure in recent human history. More specifically, exon two of GYPA encodes the receptor-binding ligand to which P. falciparum binds. Accordingly, there has been keen interest in understanding what impact, if any, natural selection has had on the distribution of variation in GYPA and exon two in particular. To this end, we resequenced GYPA in individuals sampled from both P. falciparum endemic (sub-Saharan Africa and South India) and non-endemic (Europe and East Asia) regions of the world. Observed patterns of variation suggest that GYPA has been subject to balancing selection in populations living in malaria endemic areas and in Europeans, but no such evidence was found in samples from East Asia, Oceania, and the Americas. These results are consistent with malaria acting as a selective pressure on GYPA, but also suggest that another selective force has resulted in a similar pattern of variation in Europeans. Accordingly, GYPA has perhaps a more complex evolutionary history, wherein on a global scale, spatially varying selective pressures have governed its natural history.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1801
[Cu] Class update date: 180219
[Lr] Last revision date:180219
[St] Status:In-Data-Review
[do] DOI:10.1007/s00439-018-1866-3

  5 / 9902 MEDLINE  
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[PMID]: 28471445
[Au] Autor:Wang L; Zhou F; Zhang P; Wang H; Qu Z; Jia P; Yao Z; Shen G; Li G; Zhao G; Li J; Mao Y; Xie Z; Xu W; Xu Y; Xu Y
[Ad] Address:Department of Orthopaedics, the Second Affiliated Hospital of Soochow University, Suzhou 215004, China.
[Ti] Title:Human type H vessels are a sensitive biomarker of bone mass.
[So] Source:Cell Death Dis;8(5):e2760, 2017 May 04.
[Is] ISSN:2041-4889
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:Vascularization is fundamental for bone formation and bone tissue homeostasis. However, in human subjects, a direct molecular relationship has not been identified between angiogenesis and agents that promote bone disease or factors related to age. Osteopenia is a condition in which bone mineral density is lower than normal, and it represents a sign of normal aging. Here we tested whether the type H vessel, which was recently identified as strongly positive for CD31 and Endomucin (CD31 Emcn ) in mice, is an important indicator of aging and osteopenia in human subjects. We found that age-dependent losses of type H vessels in human bone sections conform to the observations in aged mice. The abundance of human type H vessels and osteoprogenitors may be relevant to changes in the skeletal microarchitecture and advanced osteopenia. Furthermore, ovariectomized mice, a widely used model for postmenopausal osteoporosis, exhibited significantly reduced type H vessels accompanied by reduced osteoprogenitors, which is consistent with impaired bone microarchitecture and osteoporosis, suggesting that this feature is an indicator of bone mass independent of aging. More importantly, administration of desferrioxamine led to significantly increased bone mass via enhanced angiogenesis and increased type H vessels in ovariectomized mice. Altogether, these data represent a novel finding that type H vessels are regulated in aged and osteopenia subjects. The abundance of human type H vessels is an early marker of bone loss and represents a potential target for improving bone quality via the induction of type H vessels.
[Mh] MeSH terms primary: Biomarkers/metabolism
Blood Vessels/metabolism
Bone Density/physiology
Bone and Bones/metabolism
[Mh] MeSH terms secundary: Adult
Aged
Aging
Animals
Blood Vessels/pathology
Bone Diseases, Metabolic/metabolism
Bone Diseases, Metabolic/pathology
Bone and Bones/diagnostic imaging
Bone and Bones/pathology
Disease Models, Animal
Femur/blood supply
Femur/metabolism
Femur/pathology
Humans
Mice
Mice, Inbred C57BL
Middle Aged
Osteoporosis/metabolism
Osteoporosis/pathology
Osteoporosis/veterinary
Sialoglycoproteins/metabolism
Stem Cells/metabolism
Stem Cells/pathology
Tibia/blood supply
Tibia/metabolism
Tibia/pathology
Young Adult
[Pt] Publication type:JOURNAL ARTICLE
[Nm] Name of substance:0 (Biomarkers); 0 (EMCN protein, human); 0 (Sialoglycoproteins)
[Em] Entry month:1801
[Cu] Class update date: 180129
[Lr] Last revision date:180129
[Js] Journal subset:IM
[Da] Date of entry for processing:170505
[St] Status:MEDLINE
[do] DOI:10.1038/cddis.2017.36

  6 / 9902 MEDLINE  
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[PMID]: 29269442
[Au] Autor:Wang Y; Gu Y; Gao H; Gao Y; Shao J; Pang W; Dong W
[Ad] Address:College of Animal Science and TechnologyNorthwest A&F University, Yangling, China.
[Ti] Title:Exploring boar sperm sialylation during capacitation using boronic acid-functionalized beads.
[So] Source:Reproduction;155(1):25-36, 2018 Jan.
[Is] ISSN:1741-7899
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:Sialic acid (SA), which usually occupies the terminal position of oligosaccharide chains in mammalian spermatozoa, has important functions in fertilization. Compared with other methods, such as lectin probing, boronic acid could recognize and bind SA with a higher affinity and specificity at pH 6.9. In this study, two boronic acid carriers, 3-aminophenylboronic acid-labeled fluorescent latex (CML-APBA) and magnetic beads (CMM-APBA were applied to explore surface sialylation profile and sialoglycoproteins of the boar sperm. There are three binding sections of CML-APBA on the head of ejaculated sperm: acrosomal region, equatorial segment and the head posterior, which are the major regions undergoing sialylation. After capacitation , two major binding patterns of CML-APBA exists on sperm head. On some spermatozoa, sialylation exists on the equatorial segment and the posterior head, whilst on other spermatozoa, sialylation occurs on the acrosomal region and equatorial segment. Flow cytometry analysis suggested that the level of sialylation on boar sperm membrane decreases after capacitation. Furthermore, using CMM-APBA, we pulled down sialylated proteins from spermatozoa. Among them, two decapacitation factors associating on sperm surface, AWN and PSP-1, were identified. The levels of the two proteins reduced during capacitation, which might contribute to the decrease of sialylation on boar sperm surface.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1712
[Cu] Class update date: 171222
[Lr] Last revision date:171222
[St] Status:In-Data-Review
[do] DOI:10.1530/REP-17-0369

  7 / 9902 MEDLINE  
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[PMID]: 28958711
[Au] Autor:Xu L; Zhang Z; Sun X; Wang J; Xu W; Shi L; Lu J; Tang J; Liu J; Su X
[Ad] Address:Department of Biochemistry and Molecular Biology, Soochow University Medical College, Suzhou 215123, China. Electronic address: xulan@suda.edu.cn.
[Ti] Title:Glycosylation status of bone sialoprotein and its role in mineralization.
[So] Source:Exp Cell Res;360(2):413-420, 2017 Nov 15.
[Is] ISSN:1090-2422
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:The highly glycosylated bone sialoprotein (BSP) is an abundant non-collagenous phosphoprotein in bone which enhances osteoblast differentiation and new bone deposition in vitro and in vivo. However, the structural details of its different glycosylation linkages have not been well studied and their functions in bone homeostasis are not clear. Previous studies suggested that the O-glycans, but not the N-glycans on BSP, are highly sialylated. Herein, we employed tandem mass spectrometry (MS/MS) to demonstrate that the N-glycanson the recombinant human integrin binding sialoprotein (rhiBSP) are also enriched in sialic acids (SAs) at their termini. We also identified multiple novel sites of N-glycan modification. Treatment of rhiBSP enhances osteoblast differentiation and mineralization of MC3T3-E1 cells and this effect could be partially reversed by efficient enzymatic removal of its N-glycans. Removal of all terminal SAs has a greater effect in reversing the effect of rhiBSP on osteogenesis, especially on mineralization, suggesting that sialylation at the termini of both N-glycans and O-glycans plays an important role in this regulation. Moreover, BSP-conjugated SAs may affect mineralization via ERK activation of VDR expression. Collectively, our results identified novel N-glycans enriched in SAs on the rhiBSP and demonstrated that SAs at both N- and O-glycans are important for BSP regulation of osteoblast differentiation and mineralization in vitro.
[Mh] MeSH terms primary: Bone and Bones/metabolism
Calcification, Physiologic
Osteoblasts/metabolism
Sialoglycoproteins/metabolism
[Mh] MeSH terms secundary: Animals
Carbohydrate Metabolism
Carbohydrate Sequence
Cell Line
Glycosylation
Mice
Polysaccharides/metabolism
Protein Processing, Post-Translational
[Pt] Publication type:JOURNAL ARTICLE
[Nm] Name of substance:0 (Polysaccharides); 0 (Sialoglycoproteins)
[Em] Entry month:1711
[Cu] Class update date: 171107
[Lr] Last revision date:171107
[Js] Journal subset:IM
[Da] Date of entry for processing:170930
[St] Status:MEDLINE

  8 / 9902 MEDLINE  
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[PMID]: 28842487
[Au] Autor:Song K; Fu J; Song J; Herzog BH; Bergstrom K; Kondo Y; McDaniel JM; McGee S; Silasi-Mansat R; Lupu F; Chen H; Bagavant H; Xia L
[Ad] Address:From the Cardiovascular Biology Research Program, Oklahoma Medical Research Foundation, Oklahoma City, Oklahoma 73104.
[Ti] Title:Loss of mucin-type -glycans impairs the integrity of the glomerular filtration barrier in the mouse kidney.
[So] Source:J Biol Chem;292(40):16491-16497, 2017 Oct 06.
[Is] ISSN:1083-351X
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:The kidney's filtration activity is essential for removing toxins and waste products from the body. The vascular endothelial cells of the glomerulus are fenestrated, flattened, and surrounded by podocytes, specialized cells that support glomerular endothelial cells. Mucin-type core 1-derived glycans ( -glycans) are highly expressed on both glomerular capillary endothelial cells and their supporting podocytes, but their biological role is unclear. Biosynthesis of core 1-derived -glycans is catalyzed by the glycosyltransferase core 1 ß1,3-galactosyltransferase (C1galt1). Here we report that neonatal or adult mice with inducible deletion of ( ) exhibit spontaneous proteinuria and rapidly progressing glomerulosclerosis. Ultrastructural analysis of the glomerular filtration barrier components revealed that loss of -glycans results in altered podocyte foot processes. Further analysis indicated that -glycan is essential for the normal signaling function of podocalyxin, a podocyte foot process-associated glycoprotein. Our results reveal a new function of -glycosylation in the integrity of the glomerular filtration barrier.
[Mh] MeSH terms primary: Galactosyltransferases/metabolism
Mucins
Podocytes/metabolism
Polysaccharides/metabolism
Sialoglycoproteins/metabolism
Signal Transduction/physiology
[Mh] MeSH terms secundary: Animals
Galactosyltransferases/genetics
Mice
Mice, Knockout
Polysaccharides/genetics
Sialoglycoproteins/genetics
[Pt] Publication type:JOURNAL ARTICLE
[Nm] Name of substance:0 (Mucins); 0 (Polysaccharides); 0 (Sialoglycoproteins); 0 (podocalyxin); EC 2.4.1.- (C1galt1 protein, mouse); EC 2.4.1.- (Galactosyltransferases)
[Em] Entry month:1710
[Cu] Class update date: 171012
[Lr] Last revision date:171012
[Js] Journal subset:IM
[Da] Date of entry for processing:170827
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.798512

  9 / 9902 MEDLINE  
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[PMID]: 28796952
[Au] Autor:Mangione F; EzEldeen M; Bardet C; Lesieur J; Bonneau M; Decup F; Salmon B; Jacobs R; Chaussain C; Opsahl-Vital S
[Ad] Address:1 EA 2496 Laboratory Orofacial Pathologies, Imagery and Biotherapies, Dental School and Life imaging Platform (PIV), University Paris Descartes Sorbonne Paris Cité, Montrouge, France.
[Ti] Title:Implanted Dental Pulp Cells Fail to Induce Regeneration in Partial Pulpotomies.
[So] Source:J Dent Res;96(12):1406-1413, 2017 Nov.
[Is] ISSN:1544-0591
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Cell-based partial pulp regeneration is one of the promising approaches to obtain newly formed functional dentin-pulp complex. It relies on the preservation of the healthy tissue while regenerating the damaged pulp. The aim of this study was to investigate whether this regenerative process could be achieved by implanting porcine dental pulp cells (pDPCs) in pulp defects in the minipig. By split-mouth model, self-assembling injectable nanopeptide hydrogel, with and without pDPCs, was implanted after cameral pulpotomy in premolars and molars. At day 21 after surgery, 3-dimensional morphometric characterization, Masson's trichrome staining, and immunolabeling for DSP and BSP (dentin sialoprotein and bone sialoprotein) were performed on treated teeth. This study demonstrated no pulp regeneration but systematic reparative dentinogenesis. In fact, regardless of the presence of pDPCs in the scaffold, an osteodentin bridge-the microarchitecture of which significantly differed from the native dentin-was systematically obtained. Furthermore, the presence of pDPCs significantly affected the microstructure of the dentin bridges. In the radicular area of each treated tooth, hyperemia in the remaining pulp and external root resorptions were observed. Under the conditions tested in this work, pulp regeneration was not achieved, which highlights the need of further investigations to develop favorable regenerative microenvironment.
[Mh] MeSH terms primary: Dental Pulp/cytology
Pulpotomy
Regeneration
Tissue Engineering/methods
[Mh] MeSH terms secundary: Animals
Cell Proliferation
Dentin, Secondary/physiology
Extracellular Matrix Proteins/analysis
Hydrogels
Integrin-Binding Sialoprotein/analysis
Phosphoproteins/analysis
Sialoglycoproteins/analysis
Staining and Labeling
Swine
Swine, Miniature
X-Ray Microtomography
[Pt] Publication type:JOURNAL ARTICLE
[Nm] Name of substance:0 (Extracellular Matrix Proteins); 0 (Hydrogels); 0 (Integrin-Binding Sialoprotein); 0 (Phosphoproteins); 0 (Sialoglycoproteins); 0 (dentin sialophosphoprotein)
[Em] Entry month:1711
[Cu] Class update date: 171101
[Lr] Last revision date:171101
[Js] Journal subset:D; IM
[Da] Date of entry for processing:170811
[St] Status:MEDLINE
[do] DOI:10.1177/0022034517725523

  10 / 9902 MEDLINE  
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[PMID]: 28760933
[Au] Autor:Dankwa S; Chaand M; Kanjee U; Jiang RHY; Nobre LV; Goldberg JM; Bei AK; Moechtar MA; Grüring C; Ahouidi AD; Ndiaye D; Dieye TN; Mboup S; Weekes MP; Duraisingh MT
[Ad] Address:Department of Immunology and Infectious Diseases, Harvard T.H. Chan School of Public Health, Boston, Massachusetts, USA.
[Ti] Title:Genetic Evidence for Erythrocyte Receptor Glycophorin B Expression Levels Defining a Dominant Plasmodium falciparum Invasion Pathway into Human Erythrocytes.
[So] Source:Infect Immun;85(10), 2017 Oct.
[Is] ISSN:1098-5522
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:, the parasite that causes the deadliest form of malaria, has evolved multiple proteins known as invasion ligands that bind to specific erythrocyte receptors to facilitate invasion of human erythrocytes. The EBA-175/glycophorin A (GPA) and Rh5/basigin ligand-receptor interactions, referred to as invasion pathways, have been the subject of intense study. In this study, we focused on the less-characterized sialic acid-containing receptors glycophorin B (GPB) and glycophorin C (GPC). Through bioinformatic analysis, we identified extensive variation in glycophorin B (GYPB) transcript levels in individuals from Benin, suggesting selection from malaria pressure. To elucidate the importance of the GPB and GPC receptors relative to the well-described EBA-175/GPA invasion pathway, we used an erythrocyte culture system to decrease expression of GPA, GPB, or GPC via lentiviral short hairpin RNA transduction of erythroid progenitor cells, with global surface proteomic profiling. We assessed the efficiency of parasite invasion into knockdown cells using a panel of wild-type laboratory strains and invasion ligand knockout lines, as well as Senegalese clinical isolates and a short-term-culture-adapted strain. For this, we optimized an invasion assay suitable for use with small numbers of erythrocytes. We found that all laboratory strains and the majority of field strains tested were dependent on GPB expression level for invasion. The collective data suggest that the GPA and GPB receptors are of greater importance than the GPC receptor, supporting a hierarchy of erythrocyte receptor usage in .
[Mh] MeSH terms primary: Erythrocytes/physiology
Erythrocytes/parasitology
Glycophorin/genetics
Plasmodium falciparum/pathogenicity
[Mh] MeSH terms secundary: Computational Biology
Glycophorin/metabolism
Humans
Ligands
Plasmodium falciparum/immunology
Plasmodium falciparum/physiology
Protein Binding
Proteomics
Receptors, Cell Surface/metabolism
[Pt] Publication type:JOURNAL ARTICLE
[Nm] Name of substance:0 (Glycophorin); 0 (Ligands); 0 (Receptors, Cell Surface); 0 (sialic acid receptor)
[Em] Entry month:1710
[Cu] Class update date: 171017
[Lr] Last revision date:171017
[Js] Journal subset:IM
[Da] Date of entry for processing:170802
[St] Status:MEDLINE


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