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Article: An immunocytochemical study of the routes of secretion of collagen and phosphophoryn from odontoblasts into dentin

TitleAn immunocytochemical study of the routes of secretion of collagen and phosphophoryn from odontoblasts into dentin
Authors
KeywordsRat incisor dentin
Mineralization front
Proteins
Phosphoprotein
Calcification
Issue Date1995
Citation
International Journal of Connective Tissues, 1995, v. 31, p. 197-209 How to Cite?
AbstractPolyclonal antibodies to rat incisor phosphophoryns and to the amino-telopeptide of the al(I)-chain of type I collagen were used to follow the pathways of movement of collagen I (COLI) and phosphophoryns (PP) from synthesis in the odontoblast to secretion into the mineralized dentin. The antibodies were detected at the transmission electron microscopic level by their reaction with Protein A-colloidal gold conjugates. Special care was given in specimen preparation to retention of maximal antigenicity during fixation while maintaining cellular and extracellular ultrastructure at the mineralization front (MF) in nondemineralized sections. Intracellularly, COLI and PP were detected within the endoplasmic reticulum (ER), the Golgi (G) and secretory granules (SG). However, as determined by double-immunolabeling with different size gold particles the COLI and PP were not found together within the same ER, G or SG compartments. PP was localized within the tubular ER, round-shaped transitional vesicles, the Golgi and in narrow asymmetric SG. These asymmetric SG were found in abundance in the odontoblastic process. PP secretion from these vesicles was near the MF at the predentin-dentin boundary. COLI was localized within rosette form ER compartments, the Golgi and in large, distinctive SG. COLI was deposited at the cell-predentin boundary. No COLI SG were seen within the odontoblastic process near the MF. In the region of the MF, prior to mineralization, the PP was localized along the surfaces of the COLI fibrils of the predentin. The mineral phase etched surfaces revealed both COLI- and abundant mineral-associated PP. These data support the hypotheses that, in dentin, the interaction between COLI and PP may initiate crystal nucleation and that additional interactions between PP and the growing crystals may modulate the crystal growth pattern and crystal size.
Persistent Identifierhttp://hdl.handle.net/10722/88182
ISSN
2015 Impact Factor: 1.411
2015 SCImago Journal Rankings: 0.622
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorRabie, ABMen_HK
dc.contributor.authorVeis, Aen_HK
dc.date.accessioned2010-09-06T09:39:54Z-
dc.date.available2010-09-06T09:39:54Z-
dc.date.issued1995en_HK
dc.identifier.citationInternational Journal of Connective Tissues, 1995, v. 31, p. 197-209en_HK
dc.identifier.issn0300-8207-
dc.identifier.urihttp://hdl.handle.net/10722/88182-
dc.description.abstractPolyclonal antibodies to rat incisor phosphophoryns and to the amino-telopeptide of the al(I)-chain of type I collagen were used to follow the pathways of movement of collagen I (COLI) and phosphophoryns (PP) from synthesis in the odontoblast to secretion into the mineralized dentin. The antibodies were detected at the transmission electron microscopic level by their reaction with Protein A-colloidal gold conjugates. Special care was given in specimen preparation to retention of maximal antigenicity during fixation while maintaining cellular and extracellular ultrastructure at the mineralization front (MF) in nondemineralized sections. Intracellularly, COLI and PP were detected within the endoplasmic reticulum (ER), the Golgi (G) and secretory granules (SG). However, as determined by double-immunolabeling with different size gold particles the COLI and PP were not found together within the same ER, G or SG compartments. PP was localized within the tubular ER, round-shaped transitional vesicles, the Golgi and in narrow asymmetric SG. These asymmetric SG were found in abundance in the odontoblastic process. PP secretion from these vesicles was near the MF at the predentin-dentin boundary. COLI was localized within rosette form ER compartments, the Golgi and in large, distinctive SG. COLI was deposited at the cell-predentin boundary. No COLI SG were seen within the odontoblastic process near the MF. In the region of the MF, prior to mineralization, the PP was localized along the surfaces of the COLI fibrils of the predentin. The mineral phase etched surfaces revealed both COLI- and abundant mineral-associated PP. These data support the hypotheses that, in dentin, the interaction between COLI and PP may initiate crystal nucleation and that additional interactions between PP and the growing crystals may modulate the crystal growth pattern and crystal size.-
dc.languageengen_HK
dc.relation.ispartofInternational Journal of Connective Tissuesen_HK
dc.subjectRat incisor dentin-
dc.subjectMineralization front-
dc.subjectProteins-
dc.subjectPhosphoprotein-
dc.subjectCalcification-
dc.titleAn immunocytochemical study of the routes of secretion of collagen and phosphophoryn from odontoblasts into dentinen_HK
dc.typeArticleen_HK
dc.identifier.emailRabie, ABM: rabie@hkusua.hku.hken_HK
dc.identifier.authorityRabie, ABM=rp00029en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.3109/03008209509010811-
dc.identifier.pmid15609627-
dc.identifier.scopuseid_2-s2.0-0029186899-
dc.identifier.hkuros9588en_HK
dc.identifier.isiWOS:A1995TM96600003-

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