Disease relevance of Amelx

• In the present study, we investigated the localization of amelogenin in odontogenic tumors, using an anti-amelogenin polyclonal antibody [1].

High impact information on Amelx

• Two specific cDNAs comprised from amelogenin gene exons 2,3,4,5,6d,7 and 2,3,5,6d, 7 were identified [2].
• Low molecular mass amelogenin-related polypeptides extracted from mineralized dentin have the ability to affect the differentiation pathway of embryonic muscle fibroblasts in culture and lead to the formation of mineralized matrix in in vivo implants [2].
• Low amounts of amelogenin RNA persisted after the differentiation of ameloblasts into the maturative stage [3].
• The expression of amelogenin mRNA in growing rat molars was studied [3].
• The early amelogenin RNA expression occurred adjacent to the initial deposition of the dentin matrix [3].

Biological context of Amelx

• Alternative splicing of amelogenin mRNA from rat incisor ameloblasts [4].
• Amelogenin and type I collagen gene expression increases during dentin mineralization [5].
• The expression patterns of cytokeratin 14, nerve growth factor receptor p75, amelogenin, Notch2, and alkaline phosphatase were examined by immunohistochemistry in both lower and higher cell densities [6].
• The unique hereditary enamel defect clearly related to the disturbance of one enamel matrix protein is X-linked amelogenesis imperfecta (AI), in which several mutations of amelogenin gene have been identified [7].
• Immunocytochemical study of amelogenin deposition during the early odontogenesis of molars in alendronate-treated newborn rats [8].

Anatomical context of Amelx

• This alternatively spliced product is almost identical to products previously identified in both cow and mouse enamel organs: the leucine-rich amelogenin peptide (LRAP) [9].
• Identification of the chondrogenic-inducing activity from bovine dentin (bCIA) as a low-molecular-mass amelogenin polypeptide [10].
• Interestingly amelogenin, ameloblastin and enamelin were also expressed in the odontoblasts during dentin formation [11].
• Our results confirm the presence of MMP-20 protein in ameloblasts and odontoblasts of rat incisor and show it to be localized in the same sites of the forming enamel as amelogenin [12].
• Internalization of amelogenin by dendritic cells of the papillary layer during transition and early maturation stages [13].

Associations of Amelx with chemical compounds

• During maturation, most of these components are selectively lost, more or less completely, from the enamel. 'Amelogenin' components rich in proline and histidine are removed first and 'tuft protein', characterized by high serine and glycine, is often partially retained in mature enamel [14].
• The rats were perfused with aldehyde and the mandibular incisors were processed for histochemical and ultrastructural analyses and for postembedding colloidal gold immunolabeling with antibodies to amelogenin, ameloblastin, and albumin [15].
• Administration of brefeldin A and cycloheximide to stop protein secretion revealed that the immunoblotting pattern of amelogenin was relatively stable, whereas ameloblastin broke down rapidly into lower molecular weight fragments [16].
• The effect of amelogenin was inhibited by the tyrosine kinase inhibitor herbimycin A [17].
• The cells also appear to release at least one phosphoprotein with molecular weight near 27 kDa, which may be an amelogenin, and up to five cysteine-containing proteins with molecular weights near 94, 90, 72, 55, and 27 kDa [18].

Physical interactions of Amelx

• The distance from the cell surface at which immunolabeling for amelogenin stabilized generally corresponded to the point at which that for ameloblastin started to show a net reduction [16].

Other interactions of Amelx

• In the culture system, c-Met appeared in all cells, whereas K14 and amelogenin appeared mainly in clustered cells that were considered to be in the post-proliferating stage [19].
• Twenty-six percent of the clones strongly matched genes and proteins in the data bases, including amelogenin, alpha 1(I) and alpha 2(I) collagen chains, osteonectin, and decorin [20].
• Sections of incisor, molars, and alveolar bone were processed for postembedding colloidal gold immunolabeling using antibodies against ameloblastin, amelogenin, bone sialoprotein, or osteopontin [21].
• Amelogenin was abundant between differentiating ameloblasts and labeling for osteopontin appeared over the Golgi apparatus of odontoblasts after initiation of dentine mineralization [21].
• At the same time, amelogenin protein was detected in the extracellular matrix between dentin and differentiating ameloblasts and in some EFA cells of the second cusp [22].

Analytical, diagnostic and therapeutic context of Amelx

• In these studies, we have used anchored PCR to identify alternatively spliced amelogenin cDNA sequences in the rat [4].
• Northern blot experiments showed that most amelogenin RNA in rat teeth was represented by two bands of 1.1 and 0.8 kb [3].
• In this paper, we studied the pattern of expression of four mineralizing protein genes (type I collagen, amelogenin, DSPP and osteocalcin) during the development of rat teeth by in situ hybridization on serial sections [5].
• The aim of the present study was to use a combination of atomic and chemical force microscopy to characterize developing enamel crystal surfaces and to determine their relationship with endogenous enamel matrix protein (amelogenin) [23].
• First, Western blot analysis of microdissected enamel matrix (secretion and maturation stages) showed no clear evidence of dysregulation of amelogenin protein processing in -D rats as compared with the controls [7].

References