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Cellular uptake of amelogenin, and its localization to CD63, and Lamp1-positive vesicles.

Cellular uptake of amelogenin, and its localization to CD63, and Lamp1-positive vesicles. Research Abstract Details 

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  • Cellular uptake of amelogenin, and its localization to CD63, and Lamp1-positive vesicles. Abstract Text:

    j l shapiroJ L Shapiro,x wenX Wen,c t okamotoC T Okamoto,h j wangH J Wang,s p lyngstadaasS P Lyngstadaas,m goldbergM Goldberg,m l sneadM L Snead,m l paineM L Paine,

    Proteins of the developing enamel matrix include amelogenin, ameloblastin and enamelin. Of these three proteins amelogenin predominates. Protein-protein interactions are likely to occur at the ameloblast Tomes' processes between membrane-bound proteins and secreted enamel matrix proteins. Such protein-protein interactions could be associated with cell signaling or endocytosis. CD63 and Lamp1 are ubiquitously expressed, are lysosomal integral membrane proteins, and localize to the plasma membrane. CD63 and Lamp1 interact with amelogenin in vitro. In this study our objective was to study the molecular events of intercellular trafficking of an exogenous source of amelogenin, and related this movement to the spatiotemporal expression of CD63 and Lamp1 using various cell lineages. Exogenously added amelogenin moves rapidly into the cell into established Lamp1-positive vesicles that subsequently localize to the perinuclear region. These data indicate a possible mechanism by which amelogenin, or degraded amelogenin peptides, are removed from the extracellular matrix during enamel formation and maturation.

    Cellular uptake of amelogenin, and its localization to CD63, and Lamp1-positive vesicles. Publishing Authors By Initials

    jl shapiroJL Shapiro,x wenX Wen,ct okamotoCT Okamoto,hj wangHJ Wang,sp lyngstadaasSP Lyngstadaas,m goldbergM Goldberg,ml sneadML Snead,ml paineML Paine,

    For similar cells: cellular structures: intracellular space: cytoplasm: cytoplasmic structures: organelles: cytoplasmic vesicles: transport vesicles research abstracts see: cells: cellular structures: intracellular space: cytoplasm: cytoplasmic structures: organelles: cytoplasmic vesicles: transport vesicles research

    PUBMED ID PMID:

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    Cellular uptake of amelogenin, and its localization to CD63, and Lamp1-positive vesicles. Journal Published:

    PUBLICATION TYPE: Research Support, N.I.H., Extr

    Journal: Cellular and molecular life sciences : CMLS

    VOLUME: 64

    Page Numbers: 244-56

    Journal Abbreviation: Cell. Mol. Life Sci.

    ISSN: 1420-682X

    DAY: 3

    MONTH: Jan

    YEAR: 2007

    Cellular uptake of amelogenin, and its localization to CD63, and Lamp1-positive vesicles. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 9705402

    Cellular uptake of amelogenin, and its localization to CD63, and Lamp1-positive vesicles. Keywords Mesh Terms:

    KEYWORDS: Transport Vesicles

    MESH TERMS: metabolism

    Chemical & Substance for Abstract: Cellular uptake of amelogenin, and its localization to CD63, and Lamp1-positive vesicles. Information

    Substance Name: Green Fluorescent Proteins

    Registry Number: 147336-22-9

    Grant and Affiliation Information for Cellular uptake of amelogenin, and its localization to CD63, and Lamp1-positive vesicles.

    AFFILIATION: Center for Craniofacial Molecular Biology, University of Southern California School of Dentistry, Los Angeles, CA 90033-1004, USA.

    Country: Switzerland

    Switzerland Research PublicationSwitzerland Research Publication

    AGENCY: United States NIDCR

    GRANT: DE014867

    ACRONYM: DE

    MEDLINETA: Cell Mol Life Sci

    REFSOURCE:

    DATABASENAME:

    ACCESSION NUMBER:

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