Growth Differentiation Factors

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Morgan Sheng - One of the best experts on this subject based on the ideXlab platform.

  • direct interaction of cask lin 2 and syndecan heparan sulfate proteoglycan and their overlapping distribution in neuronal synapses
    Journal of Cell Biology, 1998
    Co-Authors: Yiping Hsueh, Fu Chia Yang, Viktor Kharazia, Scott Naisbitt, Alexandra R Cohen, Richard J Weinberg, Morgan Sheng
    Abstract:

    CASK, the rat homolog of a gene (LIN-2) required for vulval Differentiation in Caenorhabditis elegans, is expressed in mammalian brain, but its function in neurons is unknown. CASK is distributed in a punctate somatodendritic pattern in neurons. By immunogold EM, CASK protein is concentrated in synapses, but is also present at nonsynaptic membranes and in intracellular compartments. This immunolocalization is consistent with biochemical studies showing the presence of CASK in soluble and synaptosomal membrane fractions and its enrichment in postsynaptic density fractions of rat brain. By yeast two-hybrid screening, a specific interaction was identified between the PDZ domain of CASK and the COOH terminal tail of syndecan-2, a cell surface heparan sulfate proteoglycan (HSPG). The interaction was confirmed by coimmunoprecipitation from heterologous cells. In brain, syndecan-2 localizes specifically at synaptic junctions where it shows overlapping distribution with CASK, consistent with an interaction between these proteins in synapses. Cell surface HSPGs can bind to extracellular matrix proteins, and are required for the action of various heparin-binding polypeptide Growth/Differentiation Factors. The synaptic localization of CASK and syndecan suggests a potential role for these proteins in adhesion and signaling at neuronal synapses.

  • direct interaction of cask lin 2 and syndecan heparan sulfate proteoglycan and their overlapping distribution in neuronal synapses
    Journal of Cell Biology, 1998
    Co-Authors: Yiping Hsueh, Fu Chia Yang, Viktor Kharazia, Scott Naisbitt, Alexandra R Cohen, Richard J Weinberg, Morgan Sheng
    Abstract:

    CASK, the rat homolog of a gene (LIN-2) required for vulval Differentiation in Caenorhabditis elegans, is expressed in mammalian brain, but its function in neurons is unknown. CASK is distributed in a punctate somatodendritic pattern in neurons. By immunogold EM, CASK protein is concentrated in synapses, but is also present at nonsynaptic membranes and in intracellular compartments. This immunolocalization is consistent with biochemical studies showing the presence of CASK in soluble and synaptosomal membrane fractions and its enrichment in postsynaptic density fractions of rat brain. By yeast two-hybrid screening, a specific interaction was identified between the PDZ domain of CASK and the COOH terminal tail of syndecan-2, a cell surface heparan sulfate proteoglycan (HSPG). The interaction was confirmed by coimmunoprecipitation from heterologous cells. In brain, syndecan-2 localizes specifically at synaptic junctions where it shows overlapping distribution with CASK, consistent with an interaction between these proteins in synapses. Cell surface HSPGs can bind to extracellular matrix proteins, and are required for the action of various heparin-binding polypeptide Growth/Differentiation Factors. The synaptic localization of CASK and syndecan suggests a potential role for these proteins in adhesion and signaling at neuronal synapses.

Martin M Matzuk - One of the best experts on this subject based on the ideXlab platform.

  • genetic analysis of the mammalian transforming Growth factor β superfamily
    Endocrine Reviews, 2002
    Co-Authors: Hua Chang, Chester W Brown, Martin M Matzuk
    Abstract:

    Members of the TGF-β superfamily, which includes TGF-βs, Growth Differentiation Factors, bone morphogenetic proteins, activins, inhibins, and glial cell line-derived neurotrophic factor, are synthesized as prepropeptide precursors and then processed and secreted as homodimers or heterodimers. Most ligands of the family signal through transmembrane serine/threonine kinase receptors and SMAD proteins to regulate cellular functions. Many studies have reported the characterization of knockout and knock-in transgenic mice as well as humans or other mammals with naturally occurring genetic mutations in superfamily members or their regulatory proteins. These investigations have revealed that TGF-β superfamily ligands, receptors, SMADs, and upstream and downstream regulators function in diverse developmental and physiological pathways. This review attempts to collate and integrate the extensive body of in vivo mammalian studies produced over the last decade.

  • genetic analysis of the mammalian transforming Growth factor β superfamily
    Endocrine Reviews, 2002
    Co-Authors: Hua Chang, Chester W Brown, Martin M Matzuk
    Abstract:

    Members of the TGF-beta superfamily, which includes TGF-betas, Growth Differentiation Factors, bone morphogenetic proteins, activins, inhibins, and glial cell line-derived neurotrophic factor, are synthesized as prepropeptide precursors and then processed and secreted as homodimers or heterodimers. Most ligands of the family signal through transmembrane serine/threonine kinase receptors and SMAD proteins to regulate cellular functions. Many studies have reported the characterization of knockout and knock-in transgenic mice as well as humans or other mammals with naturally occurring genetic mutations in superfamily members or their regulatory proteins. These investigations have revealed that TGF-beta superfamily ligands, receptors, SMADs, and upstream and downstream regulators function in diverse developmental and physiological pathways. This review attempts to collate and integrate the extensive body of in vivo mammalian studies produced over the last decade.

Yiping Hsueh - One of the best experts on this subject based on the ideXlab platform.

  • direct interaction of cask lin 2 and syndecan heparan sulfate proteoglycan and their overlapping distribution in neuronal synapses
    Journal of Cell Biology, 1998
    Co-Authors: Yiping Hsueh, Fu Chia Yang, Viktor Kharazia, Scott Naisbitt, Alexandra R Cohen, Richard J Weinberg, Morgan Sheng
    Abstract:

    CASK, the rat homolog of a gene (LIN-2) required for vulval Differentiation in Caenorhabditis elegans, is expressed in mammalian brain, but its function in neurons is unknown. CASK is distributed in a punctate somatodendritic pattern in neurons. By immunogold EM, CASK protein is concentrated in synapses, but is also present at nonsynaptic membranes and in intracellular compartments. This immunolocalization is consistent with biochemical studies showing the presence of CASK in soluble and synaptosomal membrane fractions and its enrichment in postsynaptic density fractions of rat brain. By yeast two-hybrid screening, a specific interaction was identified between the PDZ domain of CASK and the COOH terminal tail of syndecan-2, a cell surface heparan sulfate proteoglycan (HSPG). The interaction was confirmed by coimmunoprecipitation from heterologous cells. In brain, syndecan-2 localizes specifically at synaptic junctions where it shows overlapping distribution with CASK, consistent with an interaction between these proteins in synapses. Cell surface HSPGs can bind to extracellular matrix proteins, and are required for the action of various heparin-binding polypeptide Growth/Differentiation Factors. The synaptic localization of CASK and syndecan suggests a potential role for these proteins in adhesion and signaling at neuronal synapses.

  • direct interaction of cask lin 2 and syndecan heparan sulfate proteoglycan and their overlapping distribution in neuronal synapses
    Journal of Cell Biology, 1998
    Co-Authors: Yiping Hsueh, Fu Chia Yang, Viktor Kharazia, Scott Naisbitt, Alexandra R Cohen, Richard J Weinberg, Morgan Sheng
    Abstract:

    CASK, the rat homolog of a gene (LIN-2) required for vulval Differentiation in Caenorhabditis elegans, is expressed in mammalian brain, but its function in neurons is unknown. CASK is distributed in a punctate somatodendritic pattern in neurons. By immunogold EM, CASK protein is concentrated in synapses, but is also present at nonsynaptic membranes and in intracellular compartments. This immunolocalization is consistent with biochemical studies showing the presence of CASK in soluble and synaptosomal membrane fractions and its enrichment in postsynaptic density fractions of rat brain. By yeast two-hybrid screening, a specific interaction was identified between the PDZ domain of CASK and the COOH terminal tail of syndecan-2, a cell surface heparan sulfate proteoglycan (HSPG). The interaction was confirmed by coimmunoprecipitation from heterologous cells. In brain, syndecan-2 localizes specifically at synaptic junctions where it shows overlapping distribution with CASK, consistent with an interaction between these proteins in synapses. Cell surface HSPGs can bind to extracellular matrix proteins, and are required for the action of various heparin-binding polypeptide Growth/Differentiation Factors. The synaptic localization of CASK and syndecan suggests a potential role for these proteins in adhesion and signaling at neuronal synapses.

Hua Chang - One of the best experts on this subject based on the ideXlab platform.

  • genetic analysis of the mammalian transforming Growth factor β superfamily
    Endocrine Reviews, 2002
    Co-Authors: Hua Chang, Chester W Brown, Martin M Matzuk
    Abstract:

    Members of the TGF-β superfamily, which includes TGF-βs, Growth Differentiation Factors, bone morphogenetic proteins, activins, inhibins, and glial cell line-derived neurotrophic factor, are synthesized as prepropeptide precursors and then processed and secreted as homodimers or heterodimers. Most ligands of the family signal through transmembrane serine/threonine kinase receptors and SMAD proteins to regulate cellular functions. Many studies have reported the characterization of knockout and knock-in transgenic mice as well as humans or other mammals with naturally occurring genetic mutations in superfamily members or their regulatory proteins. These investigations have revealed that TGF-β superfamily ligands, receptors, SMADs, and upstream and downstream regulators function in diverse developmental and physiological pathways. This review attempts to collate and integrate the extensive body of in vivo mammalian studies produced over the last decade.

  • genetic analysis of the mammalian transforming Growth factor β superfamily
    Endocrine Reviews, 2002
    Co-Authors: Hua Chang, Chester W Brown, Martin M Matzuk
    Abstract:

    Members of the TGF-beta superfamily, which includes TGF-betas, Growth Differentiation Factors, bone morphogenetic proteins, activins, inhibins, and glial cell line-derived neurotrophic factor, are synthesized as prepropeptide precursors and then processed and secreted as homodimers or heterodimers. Most ligands of the family signal through transmembrane serine/threonine kinase receptors and SMAD proteins to regulate cellular functions. Many studies have reported the characterization of knockout and knock-in transgenic mice as well as humans or other mammals with naturally occurring genetic mutations in superfamily members or their regulatory proteins. These investigations have revealed that TGF-beta superfamily ligands, receptors, SMADs, and upstream and downstream regulators function in diverse developmental and physiological pathways. This review attempts to collate and integrate the extensive body of in vivo mammalian studies produced over the last decade.

Mariano Sanz - One of the best experts on this subject based on the ideXlab platform.

  • Soft tissue wound healing at teeth, dental implants and the edentulous ridge when using barrier membranes, Growth and Differentiation Factors and soft tissue substitutes
    Journal of Clinical Periodontology, 2014
    Co-Authors: Fabio Vignoletti, Javier Nunez, Mariano Sanz
    Abstract:

    AIM: To review the biological processes of wound healing following periodontal and periimplant plastic surgery when different technologies are used in a) the coverage of root and implant dehiscences, b) the augmentation of keratinized tissue (KT) and c) the augmentation of soft tissue volume.\n\nMATERIALS & METHODS: An electronic search from The National Library of Medicine (MEDLINE-PubMed) was performed: English articles with research focus in oral soft tissue regeneration, providing histological outcomes, either from animal experimental studies or human biopsy material were included.\n\nRESULTS: Barrier membranes, enamel matrix derivatives, Growth Factors, allogeneic and xenogeneic soft tissue substitutes have been used in soft tissue regeneration demonstrating different degrees of regeneration. In root coverage, these technologies were able to improve new attachment, although none has shown complete regeneration. In KT augmentation, tissue-engineered allogenic products and xenogeneic collagen matrixes demonstrated integration within the host connective tissue and promotion of keratinization. In soft tissue augmentation and peri-implant plastic surgery there are no histological data currently available.\n\nCONCLUSIONS: Soft tissue substitutes, Growth Differentiation Factors demonstrated promising histological results in terms of soft tissue regeneration and keratinization, whereas there is a need for further studies to prove their added value in soft tissue augmentation.