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Article ; Online: SARS-CoV-2 BA.1 and BA.2 breakthrough infections boost antibody responses to early Omicron subvariants but not BQ.1.1 or XBB.1.5.

Abbad, Anass / Yellin, Temima / Singh, Gagandeep / Fried, Miriam / Raskin, Ariel / Tcheou, Johnstone / Monahan, Brian / Gleason, Charles / Simon, Viviana / Carreño, Juan Manuel / Krammer, Florian

Cell reports. Medicine

2024 Volume 5, Issue 3, Page(s) 101474

Abstract: Subvariants of the Omicron lineage of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) efficiently escape neutralizing antibody responses induced by both vaccination and infection with antigenically distinct variants. Here, we describe the ... ...

Abstract	Subvariants of the Omicron lineage of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) efficiently escape neutralizing antibody responses induced by both vaccination and infection with antigenically distinct variants. Here, we describe the potency and breadth of neutralizing and binding antibody responses against a large panel of variants following an Omicron BA.1 or BA.2 breakthrough infection in a heterogeneous cohort of individuals with diverse exposure histories. Both BA.1 and BA.2 breakthrough infections significantly boost antibody levels and broaden antibody reactivity. However, this broader immunity induced by BA.1 and BA.2 breakthrough infections does not neutralize Omicron BQ and XBB subvariants efficiently. While these subvariants are not neutralized well by post-breakthrough sera, suggesting escape, binding non-neutralizing antibody responses are sustained. In summary, our data suggest that while BA.1 and BA.2 breakthrough infections broaden the immune response to SARS-CoV-2 spike, the induced neutralizing antibody response is still outpaced by viral evolution.
MeSH term(s)	Humans ; Antibody Formation ; Breakthrough Infections ; COVID-19 ; SARS-CoV-2 ; Antibodies, Neutralizing
Chemical Substances	Antibodies, Neutralizing
Language	English
Publishing date	2024-03-20
Publishing country	United States
Document type	Journal Article
ISSN	2666-3791
ISSN (online)	2666-3791
DOI	10.1016/j.xcrm.2024.101474
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Article ; Online: Frequent aneuploidy in primary human T cells after CRISPR-Cas9 cleavage.

Nahmad, Alessio David / Reuveni, Eli / Goldschmidt, Ella / Tenne, Tamar / Liberman, Meytal / Horovitz-Fried, Miriam / Khosravi, Rami / Kobo, Hila / Reinstein, Eyal / Madi, Asaf / Ben-David, Uri / Barzel, Adi

Nature biotechnology

2022 Volume 40, Issue 12, Page(s) 1807–1813

Abstract: Multiple clinical trials of allogeneic T cell therapy use site-specific nucleases to disrupt T cell receptor (TCR) and other ... ...

Abstract	Multiple clinical trials of allogeneic T cell therapy use site-specific nucleases to disrupt T cell receptor (TCR) and other genes
MeSH term(s)	Humans ; CRISPR-Cas Systems/genetics ; In Situ Hybridization, Fluorescence ; T-Lymphocytes ; Gene Editing/methods ; Receptors, Antigen, T-Cell/genetics ; Aneuploidy
Chemical Substances	Receptors, Antigen, T-Cell
Language	English
Publishing date	2022-06-30
Publishing country	United States
Document type	Journal Article
ZDB-ID	1311932-1
ISSN	1546-1696 ; 1087-0156
ISSN (online)	1546-1696
ISSN	1087-0156
DOI	10.1038/s41587-022-01377-0
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Article: Insulin-induced translocation of IR to the nucleus in insulin responsive cells requires a nuclear translocation sequence.

Kesten, Dov / Horovitz-Fried, Miriam / Brutman-Barazani, Tamar / Sampson, Sanford R

Biochimica et biophysica acta. Molecular cell research

2018 Volume 1865, Issue 4, Page(s) 551–559

Abstract: Insulin binding to its cell surface receptor (IR) activates a cascade of events leading to its biological effects. The Insulin-IR complex is rapidly internalized and then is either recycled back to the plasma membrane or sent to lysosomes for degradation. ...

Abstract	Insulin binding to its cell surface receptor (IR) activates a cascade of events leading to its biological effects. The Insulin-IR complex is rapidly internalized and then is either recycled back to the plasma membrane or sent to lysosomes for degradation. Although most of the receptor is recycled or degraded, a small amount may escape this pathway and migrate to the nucleus of the cell where it might be important in promulgation of receptor signals. In this study we explored the mechanism by which insulin induces IR translocation to the cell nucleus. Experiments were performed cultured L6 myoblasts, AML liver cells and 3T3-L1 adipocytes. Insulin treatment induced a rapid increase in nuclear IR protein levels within 2 to 5 min. Treatment with WGA, an inhibitor of nuclear import, reduced insulin-induced increases nuclear IR protein; IR was, however, translocated to a perinuclear location. Bioinformatics tools predicted a potential nuclear localization sequence (NLS) on IR. Immunofluorescence staining showed that a point mutation on the predicted NLS blocked insulin-induced IR nuclear translocation. In addition, blockade of nuclear IR activation in isolated nuclei by an IR blocking antibody abrogated insulin-induced increases in IR tyrosine phosphorylation and nuclear PKCδ levels. Furthermore, over expression of mutated IR reduced insulin-induced glucose uptake and PKB phosphorylation. When added to isolated nuclei, insulin induced IR phosphorylation but had no effect on nuclear IR protein levels. These results raise questions regarding the possible role of nuclear IR in IR signaling and insulin resistance.
MeSH term(s)	3T3-L1 Cells ; Active Transport, Cell Nucleus/drug effects ; Amino Acid Sequence ; Animals ; Cell Nucleus/drug effects ; Cell Nucleus/metabolism ; Glucose/metabolism ; Humans ; Insulin/pharmacology ; Mice ; Mutant Proteins/metabolism ; Nuclear Localization Signals/chemistry ; Nuclear Localization Signals/metabolism ; Phosphorylation/drug effects ; Phosphotyrosine/metabolism ; Protein Transport/drug effects ; Proto-Oncogene Proteins c-akt/metabolism ; Receptor, Insulin/chemistry ; Receptor, Insulin/metabolism
Chemical Substances	Insulin ; Mutant Proteins ; Nuclear Localization Signals ; Phosphotyrosine (21820-51-9) ; Receptor, Insulin (EC 2.7.10.1) ; Proto-Oncogene Proteins c-akt (EC 2.7.11.1) ; Glucose (IY9XDZ35W2)
Language	English
Publishing date	2018-01-06
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	60-7
ISSN	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0167-4889 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
ISSN	0167-4889 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/j.bbamcr.2018.01.004
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Article ; Online: In vivo engineered B cells secrete high titers of broadly neutralizing anti-HIV antibodies in mice.

Nahmad, Alessio D / Lazzarotto, Cicera R / Zelikson, Natalie / Kustin, Talia / Tenuta, Mary / Huang, Deli / Reuveni, Inbal / Nataf, Daniel / Raviv, Yuval / Horovitz-Fried, Miriam / Dotan, Iris / Carmi, Yaron / Rosin-Arbesfeld, Rina / Nemazee, David / Voss, James E / Stern, Adi / Tsai, Shengdar Q / Barzel, Adi

Nature biotechnology

2022 Volume 40, Issue 8, Page(s) 1241–1249

Abstract: Transplantation of B cells engineered ex vivo to secrete broadly neutralizing antibodies (bNAbs) has shown efficacy in disease models. However, clinical translation of this approach would require specialized medical centers, technically demanding ... ...

Abstract	Transplantation of B cells engineered ex vivo to secrete broadly neutralizing antibodies (bNAbs) has shown efficacy in disease models. However, clinical translation of this approach would require specialized medical centers, technically demanding protocols and major histocompatibility complex compatibility of donor cells and recipients. Here we report in vivo B cell engineering using two adeno-associated viral vectors, with one coding for Staphylococcus aureus Cas9 (saCas9) and the other for 3BNC117, an anti-HIV bNAb. After intravenously injecting the vectors into mice, we observe successful editing of B cells leading to memory retention and bNAb secretion at neutralizing titers of up to 6.8 µg ml
MeSH term(s)	Animals ; Antibodies, Neutralizing/genetics ; B-Lymphocytes ; Broadly Neutralizing Antibodies ; HIV Antibodies/genetics ; HIV Infections/therapy ; HIV-1 ; Mice ; Staphylococcus aureus
Chemical Substances	Antibodies, Neutralizing ; Broadly Neutralizing Antibodies ; HIV Antibodies
Language	English
Publishing date	2022-06-09
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	1311932-1
ISSN	1546-1696 ; 1087-0156
ISSN (online)	1546-1696
ISSN	1087-0156
DOI	10.1038/s41587-022-01328-9
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Zs.A 2167: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
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Article ; Online: Engineered B cells expressing an anti-HIV antibody enable memory retention, isotype switching and clonal expansion.

Nahmad, Alessio D / Raviv, Yuval / Horovitz-Fried, Miriam / Sofer, Ilan / Akriv, Tal / Nataf, Daniel / Dotan, Iris / Carmi, Yaron / Burstein, David / Wine, Yariv / Benhar, Itai / Barzel, Adi

Nature communications

2020 Volume 11, Issue 1, Page(s) 5851

Abstract: HIV viremia can be controlled by chronic antiretroviral therapy. As a potentially single-shot alternative, B cells engineered by CRISPR/Cas9 to express anti-HIV broadly neutralizing antibodies (bNAbs) are capable of secreting high antibody titers. Here, ... ...

Abstract	HIV viremia can be controlled by chronic antiretroviral therapy. As a potentially single-shot alternative, B cells engineered by CRISPR/Cas9 to express anti-HIV broadly neutralizing antibodies (bNAbs) are capable of secreting high antibody titers. Here, we show that, upon immunization of mice, adoptively transferred engineered B cells home to germinal centers (GC) where they predominate over the endogenous response and differentiate into memory and plasma cells while undergoing class switch recombination (CSR). Immunization with a high affinity antigen increases accumulation in GCs and CSR rates. Boost immunization increases the rate of engineered B cells in GCs and antibody secretion, indicating memory retention. Finally, antibody sequences of engineered B cells in the spleen show patterns of clonal selection. Therefore, B cells can be engineered into what could be a living and evolving drug.
MeSH term(s)	AIDS Vaccines/genetics ; AIDS Vaccines/immunology ; Animals ; Antibodies, Monoclonal/blood ; Antibodies, Monoclonal/genetics ; Antibodies, Monoclonal/immunology ; B-Lymphocytes/immunology ; B-Lymphocytes/physiology ; B-Lymphocytes/transplantation ; Broadly Neutralizing Antibodies/blood ; Broadly Neutralizing Antibodies/genetics ; Broadly Neutralizing Antibodies/immunology ; Genetic Engineering/methods ; HIV Antibodies/blood ; HIV Antibodies/genetics ; HIV Antibodies/immunology ; Immunization ; Immunoglobulin Isotypes/genetics ; Immunologic Memory/genetics ; Mice, Inbred C57BL ; Mice, Transgenic ; Mutation
Chemical Substances	AIDS Vaccines ; Antibodies, Monoclonal ; Broadly Neutralizing Antibodies ; HIV Antibodies ; Immunoglobulin Isotypes ; VRC01 monoclonal antibody
Language	English
Publishing date	2020-11-17
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-020-19649-1
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Article: Involvement of PKCalpha in insulin-induced PKCdelta expression: Importance of SP-1 and NFkappaB transcription factors.

Horovitz-Fried, Miriam / Sampson, Sanford R

Biochemical and biophysical research communications

2007 Volume 352, Issue 1, Page(s) 78–83

Abstract: Protein kinase C delta (PKCdelta) is a key molecule in insulin signaling essential for insulin-induced glucose transport in skeletal muscle. Recent studies in our laboratory have shown that insulin rapidly stimulates PKCdelta activity and increases ... ...

Abstract	Protein kinase C delta (PKCdelta) is a key molecule in insulin signaling essential for insulin-induced glucose transport in skeletal muscle. Recent studies in our laboratory have shown that insulin rapidly stimulates PKCdelta activity and increases PKCdelta protein and RNA levels, and that the SP-1 transcription factor is involved in insulin-induced transcription of the PKCdelta gene. Activation of SP-1 involves serine phosphorylation and translocation to the nucleus. In this study we examined the possibility that PKCalpha might be involved in serine phosphorylation and activation of SP-1. We found that insulin rapidly phosphorylates and translocates SP-1. In the cytoplasm, SP-1 was constitutively associated with PKCalpha, and insulin stimulation caused these proteins to dissociate. In contrast, in the nucleus insulin induced an increase in association between PKCalpha and SP-1. PKCalpha inhibition blocked insulin-induced serine phosphorylation of SP-1 and its association with PKCalpha in the nucleus. Inhibition of PKCalpha also reduced the insulin-induced increase in PKCdelta RNA and protein in the cytoplasmic and nuclear fractions. We also attempted to determine if another transcription factor might be involved in regulation of PKCdelta expression. We earlier showed that insulin did not affect nuclear NFkappaB levels. Inhibition of NFkappaB, however, increased insulin-induced increase in PKCdelta RNA and protein in the cytoplasmic and nuclear fractions. Surprisingly, this inhibition reduced the insulin-induced increase in cytoplasmic and nuclear PKCalpha RNA and protein. Inhibition of PKCdelta reduced IkappaBalpha phosphorylation as well as NFkappaB activation. Thus, PKCalpha regulates insulin-induced PKCdelta expression levels and this regulation involves activation of SP-1 and NFkappaB.
MeSH term(s)	Animals ; Cell Line ; Gene Expression Regulation/drug effects ; Insulin/pharmacology ; NF-kappa B/metabolism ; Phosphorylation ; Phosphoserine/metabolism ; Protein Binding ; Protein Kinase C-alpha/metabolism ; Protein Kinase C-delta/genetics ; Protein Kinase C-delta/metabolism ; Rats ; Sp1 Transcription Factor/metabolism ; Transcription, Genetic/genetics
Chemical Substances	Insulin ; NF-kappa B ; Sp1 Transcription Factor ; Phosphoserine (17885-08-4) ; Protein Kinase C-alpha (EC 2.7.11.13) ; Protein Kinase C-delta (EC 2.7.11.13)
Language	English
Publishing date	2007-01-05
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	205723-2
ISSN	0006-291X ; 0006-291X
ISSN (online)	0006-291X
ISSN	0006-291X
DOI	10.1016/j.bbrc.2006.10.149
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Article ; Online: Protein kinase Cδ but not PKCα is involved in insulin-induced glucose metabolism in hepatocytes.

Brutman-Barazani, Tamar / Horovitz-Fried, Miriam / Aga-Mizrachi, Shlomit / Brand, Chagit / Brodie, Chaya / Rosa, Jagoda / Sampson, Sanford R

Journal of cellular biochemistry

2012 Volume 113, Issue 6, Page(s) 2064–2076

Abstract: The liver is a major insulin-responsive tissue responsible for glucose regulation. One important mechanism in this phenomenon is insulin-induced glycogen synthesis. Studies in our laboratory have shown that protein kinase Cs delta (PKCδ) and alpha (α) ... ...

Abstract	The liver is a major insulin-responsive tissue responsible for glucose regulation. One important mechanism in this phenomenon is insulin-induced glycogen synthesis. Studies in our laboratory have shown that protein kinase Cs delta (PKCδ) and alpha (α) have important roles in insulin-induced glucose transport in skeletal muscle, and that their expression and activity are regulated by insulin. Their importance in glucose regulation in liver cells is unclear. In this study we investigated the possibility that these isoforms are involved in the mediation of insulin-induced glycogen synthesis in hepatocytes. Studies were done on rat hepatocytes in primary culture and on the AML-12 (alpha mouse liver) cell line. Insulin increased activity and tyrosine phosphorylation of PKCδ within 5 min. In contrast, activity and tyrosine phosphorylation of PKCα were not increased by insulin. PKCδ was constitutively associated with IR, and this was increased by insulin stimulation. Suppression of PKCδ expression by transfection with RNAi, or overexpression of kinase dead (dominant negative) PKCδ reduced both the insulin-induced activation of PKB/Akt and the phosphorylation of glycogen synthase kinase 3 (GSK3) and reduced significantly insulin-induced glucose uptake. In addition, treatment of primary rat hepatocytes with rottlerin abrogated insulin-induced increase in glycogen synthesis. Neither overexpression nor inhibition of PKCα appeared to alter activation of PKB, phosphorylation of GSK3 or glucose uptake in response to insulin. We conclude that PKCδ, but not PKCα, plays an essential role in insulin-induced glucose uptake and glycogenesis in hepatocytes.
MeSH term(s)	Acetophenones/pharmacology ; Animals ; Benzopyrans/pharmacology ; Cells, Cultured ; Glucose/metabolism ; Glycogen/biosynthesis ; Glycogen Synthase Kinase 3/metabolism ; Hepatocytes/drug effects ; Hepatocytes/metabolism ; Insulin/metabolism ; Liver/metabolism ; Male ; Mice ; Muscle, Skeletal/metabolism ; Phosphorylation ; Protein Kinase C-alpha/genetics ; Protein Kinase C-alpha/metabolism ; Protein Kinase C-delta/genetics ; Protein Kinase C-delta/metabolism ; Proto-Oncogene Proteins c-akt/metabolism ; RNA Interference ; RNA, Small Interfering ; Rats ; Rats, Wistar ; Signal Transduction
Chemical Substances	Acetophenones ; Benzopyrans ; Insulin ; RNA, Small Interfering ; Glycogen (9005-79-2) ; rottlerin (E29LP3ZMUH) ; Proto-Oncogene Proteins c-akt (EC 2.7.11.1) ; Protein Kinase C-alpha (EC 2.7.11.13) ; Protein Kinase C-delta (EC 2.7.11.13) ; Glycogen Synthase Kinase 3 (EC 2.7.11.26) ; Glucose (IY9XDZ35W2)
Language	English
Publishing date	2012-06
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	392402-6
ISSN	1097-4644 ; 0730-2312
ISSN (online)	1097-4644
ISSN	0730-2312
DOI	10.1002/jcb.24078
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Article: Insulin increases nuclear protein kinase Cdelta in L6 skeletal muscle cells.

Horovitz-Fried, Miriam / Brutman-Barazani, Tamar / Kesten, Dov / Sampson, Sanford R

Endocrinology

2008 Volume 149, Issue 4, Page(s) 1718–1727

Abstract: Protein kinase C (PKC) isoforms are involved in the transduction of a number of signals important for the regulation of cell growth, differentiation, apoptosis, and other cellular functions. PKC proteins reside in the cytoplasm in an inactive state ... ...

Abstract	Protein kinase C (PKC) isoforms are involved in the transduction of a number of signals important for the regulation of cell growth, differentiation, apoptosis, and other cellular functions. PKC proteins reside in the cytoplasm in an inactive state translocate to various membranes to become fully activated in the presence of specific cofactors. Recent evidence indicates that PKC isoforms have an important role in the nucleus. We recently showed that insulin rapidly increases PKCdelta RNA and protein. In this study we initially found that insulin induces an increase in PKCdelta protein in the nuclear fraction. We therefore attempted to elucidate the mechanism of the insulin-induced increase in nuclear PKCdelta. Studies were performed on L6 skeletal myoblasts and myotubes. The increase in nuclear PKCdelta appeared to be unique to insulin because it was not induced by other growth factors or rosiglitazone. Inhibition of transcription or translation blocked the insulin-induced increase in nuclear PKCdelta, whereas inhibition of protein import did not. Inhibition of protein export from the nucleus reduced the insulin-induced increase in PKCdelta in the cytoplasm and increased it in the nucleus. The increase in nuclear PKCdelta induced by insulin was reduced but not abrogated by treatment of isolated nuclei by trypsin digestion. Finally, we showed that insulin induced incorporation of (35)S-methionine into nuclear PKCdelta protein; this effect was not blocked by inhibition of nuclear import. Thus, these results suggest that insulin may induce nuclear-associated, or possibly nuclear, translation of PKCdelta protein.
MeSH term(s)	Active Transport, Cell Nucleus ; Animals ; Cell Nucleus/metabolism ; Cells, Cultured ; Insulin/pharmacology ; Methionine/metabolism ; Muscle, Skeletal/drug effects ; Muscle, Skeletal/metabolism ; Protein Kinase C-delta/analysis ; Protein Kinase C-delta/biosynthesis ; Rats
Chemical Substances	Insulin ; Methionine (AE28F7PNPL) ; Prkcd protein, rat (EC 2.7.1.-) ; Protein Kinase C-delta (EC 2.7.11.13)
Language	English
Publishing date	2008-04
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	427856-2
ISSN	1945-7170 ; 0013-7227
ISSN (online)	1945-7170
ISSN	0013-7227
DOI	10.1210/en.2007-1572
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Article: Activation of the nuclear transcription factor SP-1 by insulin rapidly increases the expression of protein kinase C delta in skeletal muscle.

Horovitz-Fried, Miriam / Jacob, Avraham I / Cooper, Denise R / Sampson, Sanford R

Cellular signalling

2007 Volume 19, Issue 3, Page(s) 556–562

Abstract: SP-1, a ubiquitous transcription factor involved in regulation of target genes participating in specific signaling pathways, is utilized by insulin for induction of gene transcription. Transcriptional activation generally occurs only after several (14-24) ...

Abstract	SP-1, a ubiquitous transcription factor involved in regulation of target genes participating in specific signaling pathways, is utilized by insulin for induction of gene transcription. Transcriptional activation generally occurs only after several (14-24) hours. A major element rapidly activated by insulin in skeletal muscle is PKCdelta, which plays a positive regulatory role in insulin signaling. We recently reported that insulin stimulation of skeletal muscle increases PKCdelta RNA expression and PKCdelta protein levels within 5 min. These effects were blocked by inhibitors of either translation or transcription. In this study, we investigated the possibility that SP-1 may participate in this unusually rapid effect. Studies were performed on myoblasts and myotubes of the L6 skeletal muscle cell line. Insulin rapidly increased SP-1 levels and stimulated SP-1 phosphorylation in the nuclear fraction of L6 myotubes. The increase in nuclear SP-1 was blocked by inhibition of nuclear import. Inhibition of SP-1, either pharmacologically or by suppression of SP-1 by RNAi, nearly completely abrogated insulin-induced increase in PKCdelta promoter activity. Insulin induced a rapid association of SP-1 with the PKCalpha promoter. In addition, SP-1 inhibition blocked insulin-induced increases in both PKCdelta RNA expression and PKCdelta protein levels. We conclude that insulin rapidly stimulates SP-1, which mediates the ability of this hormone to induce the rapid transcription of a major target gene utilized in the insulin signaling cascade.
MeSH term(s)	Animals ; Cell Line ; Humans ; Hypoglycemic Agents/pharmacology ; Insulin/genetics ; Insulin/pharmacology ; Kinetics ; Muscle Fibers, Skeletal/drug effects ; Muscle Fibers, Skeletal/enzymology ; Muscle, Skeletal/drug effects ; Muscle, Skeletal/enzymology ; Myoblasts/drug effects ; Myoblasts/enzymology ; Promoter Regions, Genetic ; Protein Kinase C-delta/genetics ; Protein Kinase C-delta/metabolism ; RNA Interference ; Rats ; Recombinant Proteins/pharmacology ; Sp1 Transcription Factor/metabolism
Chemical Substances	Hypoglycemic Agents ; Insulin ; Recombinant Proteins ; Sp1 Transcription Factor ; Protein Kinase C-delta (EC 2.7.11.13)
Language	English
Publishing date	2007-03
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	1002702-6
ISSN	0898-6568
ISSN	0898-6568
DOI	10.1016/j.cellsig.2006.08.005
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Article ; Online: The regulatory domain of protein kinase C delta positively regulates insulin receptor signaling.

Jacob, Avraham I / Horovitz-Fried, Miriam / Aga-Mizrachi, Shlomit / Brutman-Barazani, Tamar / Okhrimenko, Hana / Zick, Yehiel / Brodie, Chaya / Sampson, Sanford R

Journal of molecular endocrinology

2010 Volume 44, Issue 3, Page(s) 155–169

Abstract: Protein kinase C delta (PKCdelta) is induced by insulin to rapidly associate with insulin receptor (IR) and upregulates insulin signaling. We utilized specific JM and CT receptor domains and chimeras of PKCalpha and PKCdelta regulatory and catalytic ... ...

Abstract	Protein kinase C delta (PKCdelta) is induced by insulin to rapidly associate with insulin receptor (IR) and upregulates insulin signaling. We utilized specific JM and CT receptor domains and chimeras of PKCalpha and PKCdelta regulatory and catalytic domains to elucidate which components of PKCdelta are responsible for positive regulatory effects of PKCdelta on IR signaling. Studies were performed on L6 and L8 skeletal muscle myoblasts and myotubes. PKCdelta was preferentially bound to the JM domain of IR, and insulin stimulation increased this binding. Both PKCdelta/alpha and PKCalpha/delta chimeras (regulatory/catalytic) were bound preferentially to the JM but not to the CT domain of IR. Although IR-PKCdelta binding was higher in cells expressing either the PKCdelta/alpha or PKCalpha/delta chimera than in control cells, upregulation of IR signaling was observed only in PKCdelta/alpha cells. Thus, in response to insulin increases in tyrosine phosphorylation of IR and insulin receptor substrate-1, downstream signaling to protein kinase B and glycogen synthase kinase 3 (GSK3) and glucose uptake were greater in cells overexpressing PKCdelta/alpha and the PKCdelta/delta domains than in cells expressing the PKCalpha/delta domains. Basal binding of Src to PKCdelta was higher in both PKCdelta/alpha- and PKCalpha/delta-expressing cells compared to control. Binding of Src to IR was decreased in PKCalpha/delta cells but remained elevated in the PKCdelta/alpha cells in response to insulin. Finally, insulin increased Src activity in PKCdelta/alpha-expressing cells but decreased it in PKCalpha/delta-expressing cells. Thus, the regulatory domain of PKCdelta via interaction with Src appears to determine the role of PKCdelta as a positive regulator of IR signaling in skeletal muscle.
MeSH term(s)	Animals ; Biological Transport/drug effects ; Blotting, Western ; Cell Line ; Glycogen Synthase Kinase 3/metabolism ; Immunoprecipitation ; In Vitro Techniques ; Insulin/pharmacology ; Insulin Receptor Substrate Proteins/metabolism ; Muscle Fibers, Skeletal/cytology ; Muscle Fibers, Skeletal/drug effects ; Muscle Fibers, Skeletal/metabolism ; Muscle, Skeletal/drug effects ; Muscle, Skeletal/metabolism ; Myoblasts/cytology ; Myoblasts/drug effects ; Myoblasts/metabolism ; Phosphorylation/drug effects ; Protein Binding/genetics ; Protein Binding/physiology ; Protein Kinase C-delta/chemistry ; Protein Kinase C-delta/genetics ; Protein Kinase C-delta/metabolism ; Protein Structure, Tertiary/genetics ; Protein Structure, Tertiary/physiology ; Proto-Oncogene Proteins c-akt/metabolism ; Rats ; Receptor, Insulin/metabolism
Chemical Substances	Insulin ; Insulin Receptor Substrate Proteins ; Receptor, Insulin (EC 2.7.10.1) ; Proto-Oncogene Proteins c-akt (EC 2.7.11.1) ; Protein Kinase C-delta (EC 2.7.11.13) ; Glycogen Synthase Kinase 3 (EC 2.7.11.26)
Language	English
Publishing date	2010-03
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	645012-x
ISSN	1479-6813 ; 0952-5041
ISSN (online)	1479-6813
ISSN	0952-5041
DOI	10.1677/JME-09-0119
Database	MEDical Literature Analysis and Retrieval System OnLINE

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