Immunohistochemical Study of Amelogenin Binding Proteins in an Amelogenin Point Mutation Mouse

SUMMARY: Amelogenin is one of the enamel matrices secreted by ameloblasts. A mutation of the amelogenin gene can cause hereditary dental enamel defects known as amelogenesis imperfecta (AI). Since lysosome-associated membrane protein-1 (LAMP-1), -3 (LAMP-3), and 78kDa glucose-related protein (Grp78)...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Otawa-Kamogashira,Naoko, Matsuda,Yuko, Takezaki,Masaaki, Hatakeyama,Yuji, Tamaoki,Sachio, Ishikawa,Hiroyuki
Lenguaje:	English
Publicado:	Sociedad Chilena de Anatomía 2019
Materias:	Amelogenin Amelogenesis imperfecta 78kDa glucose-related protein (Grp78) Lysosome-associated membrane proteins (LAMPs)
Acceso en línea:	http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-95022019000200522
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:scielo:S0717-95022019000200522
record_format	dspace
spelling	oai:scielo:S0717-950220190002005222019-09-11Immunohistochemical Study of Amelogenin Binding Proteins in an Amelogenin Point Mutation MouseOtawa-Kamogashira,NaokoMatsuda,YukoTakezaki,MasaakiHatakeyama,YujiTamaoki,SachioIshikawa,Hiroyuki Amelogenin Amelogenesis imperfecta 78kDa glucose-related protein (Grp78) Lysosome-associated membrane proteins (LAMPs) SUMMARY: Amelogenin is one of the enamel matrices secreted by ameloblasts. A mutation of the amelogenin gene can cause hereditary dental enamel defects known as amelogenesis imperfecta (AI). Since lysosome-associated membrane protein-1 (LAMP-1), -3 (LAMP-3), and 78kDa glucose-related protein (Grp78) were identified as binding proteins of amelogenin, several studies have suggested the involvement of these binding proteins with the cell kinetics of ameloblasts in normal or abnormal conditions. The purpose of this study is to investigate the distribution of these amelogenin binding proteins in the ameloblast cell differentiation of mice with a point mutation of the amelogenin gene (Amelx). The incisors of Amelx mice had a white opaque color and the tooth surface was observed to be rough under a scanning electron microscope. Among the sequential ameloblast cell differentiation in the Amelx* mice, the shape of ameloblasts at the transition stage was irregular in comparison to those in wild-type (WT) mice. Immunostaining of Grp78 revealed that the whole cytoplasm of the transition stage ameloblasts was immunopositive for Grp78 antibody, while only the distal part of cell was positive in the WT mice. Furthermore, in the Amelx* mice, the cytoplasm of the transition stage ameloblasts was immunopositive for LAMP-1 and LAMP-3. These results suggest that Amelx* may cause the abnormal distribution of amelogenin binding proteins in the cytoplasm of ameloblasts.info:eu-repo/semantics/openAccessSociedad Chilena de AnatomíaInternational Journal of Morphology v.37 n.2 20192019-06-01text/htmlhttp://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-95022019000200522en10.4067/S0717-95022019000200522
institution	Scielo Chile
collection	Scielo Chile
language	English
topic	Amelogenin Amelogenesis imperfecta 78kDa glucose-related protein (Grp78) Lysosome-associated membrane proteins (LAMPs)
spellingShingle	Amelogenin Amelogenesis imperfecta 78kDa glucose-related protein (Grp78) Lysosome-associated membrane proteins (LAMPs) Otawa-Kamogashira,Naoko Matsuda,Yuko Takezaki,Masaaki Hatakeyama,Yuji Tamaoki,Sachio Ishikawa,Hiroyuki Immunohistochemical Study of Amelogenin Binding Proteins in an Amelogenin Point Mutation Mouse
description	SUMMARY: Amelogenin is one of the enamel matrices secreted by ameloblasts. A mutation of the amelogenin gene can cause hereditary dental enamel defects known as amelogenesis imperfecta (AI). Since lysosome-associated membrane protein-1 (LAMP-1), -3 (LAMP-3), and 78kDa glucose-related protein (Grp78) were identified as binding proteins of amelogenin, several studies have suggested the involvement of these binding proteins with the cell kinetics of ameloblasts in normal or abnormal conditions. The purpose of this study is to investigate the distribution of these amelogenin binding proteins in the ameloblast cell differentiation of mice with a point mutation of the amelogenin gene (Amelx). The incisors of Amelx mice had a white opaque color and the tooth surface was observed to be rough under a scanning electron microscope. Among the sequential ameloblast cell differentiation in the Amelx* mice, the shape of ameloblasts at the transition stage was irregular in comparison to those in wild-type (WT) mice. Immunostaining of Grp78 revealed that the whole cytoplasm of the transition stage ameloblasts was immunopositive for Grp78 antibody, while only the distal part of cell was positive in the WT mice. Furthermore, in the Amelx* mice, the cytoplasm of the transition stage ameloblasts was immunopositive for LAMP-1 and LAMP-3. These results suggest that Amelx* may cause the abnormal distribution of amelogenin binding proteins in the cytoplasm of ameloblasts.
author	Otawa-Kamogashira,Naoko Matsuda,Yuko Takezaki,Masaaki Hatakeyama,Yuji Tamaoki,Sachio Ishikawa,Hiroyuki
author_facet	Otawa-Kamogashira,Naoko Matsuda,Yuko Takezaki,Masaaki Hatakeyama,Yuji Tamaoki,Sachio Ishikawa,Hiroyuki
author_sort	Otawa-Kamogashira,Naoko
title	Immunohistochemical Study of Amelogenin Binding Proteins in an Amelogenin Point Mutation Mouse
title_short	Immunohistochemical Study of Amelogenin Binding Proteins in an Amelogenin Point Mutation Mouse
title_full	Immunohistochemical Study of Amelogenin Binding Proteins in an Amelogenin Point Mutation Mouse
title_fullStr	Immunohistochemical Study of Amelogenin Binding Proteins in an Amelogenin Point Mutation Mouse
title_full_unstemmed	Immunohistochemical Study of Amelogenin Binding Proteins in an Amelogenin Point Mutation Mouse
title_sort	immunohistochemical study of amelogenin binding proteins in an amelogenin point mutation mouse
publisher	Sociedad Chilena de Anatomía
publishDate	2019
url	http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-95022019000200522
work_keys_str_mv	AT otawakamogashiranaoko immunohistochemicalstudyofamelogeninbindingproteinsinanamelogeninpointmutationmouse AT matsudayuko immunohistochemicalstudyofamelogeninbindingproteinsinanamelogeninpointmutationmouse AT takezakimasaaki immunohistochemicalstudyofamelogeninbindingproteinsinanamelogeninpointmutationmouse AT hatakeyamayuji immunohistochemicalstudyofamelogeninbindingproteinsinanamelogeninpointmutationmouse AT tamaokisachio immunohistochemicalstudyofamelogeninbindingproteinsinanamelogeninpointmutationmouse AT ishikawahiroyuki immunohistochemicalstudyofamelogeninbindingproteinsinanamelogeninpointmutationmouse
_version_	1718445097857581056

Immunohistochemical Study of Amelogenin Binding Proteins in an Amelogenin Point Mutation Mouse

Ejemplares similares