LIVIVO - Search results -

Search results

Result 1 - 10 of total 48

Search options

Article: Function for NF-kB in neuronal survival: regulation by atypical protein kinase C.

Wooten, M W

1999 Volume 58, Issue 5, Page(s) 607–611

Abstract: Activation of the transcription factor nuclear factor kappa B (NF-kB) has been intensely studied in the past several years due to its role as an inducible regulator of inflammation, apoptosis, transformation, and oncogenesis. Recently, increasing ... ...

Abstract	Activation of the transcription factor nuclear factor kappa B (NF-kB) has been intensely studied in the past several years due to its role as an inducible regulator of inflammation, apoptosis, transformation, and oncogenesis. Recently, increasing evidence supports a role for NF-kB in regulation of anti-apoptotic gene expression and promotion of cell survival (May and Ghosh [1999] Science 284:272-273). Studies in the past 5 years have provided evidence that NF-kB regulates neuronal survival as well. Moreover, atypical protein kinase (aPKC) has been shown to play a novel role in modulating the NF-kB pathway. In this review, I focus on neurons and the factors that contribute to regulation of NF-kB via aPKC.
MeSH term(s)	Animals ; Cell Survival/physiology ; Humans ; NF-kappa B/genetics ; NF-kappa B/metabolism ; Neurons/chemistry ; Neurons/physiology ; Protein Kinase C/genetics ; Protein Kinase C/metabolism
Chemical Substances	NF-kappa B ; PKC-3 protein (EC 2.7.11.13) ; Protein Kinase C (EC 2.7.11.13)
Language	English
Publishing date	1999-12-01
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	195324-2
ISSN	1097-4547 ; 0360-4012
ISSN (online)	1097-4547
ISSN	0360-4012
DOI	10.1002/(sici)1097-4547(19991201)58:5<607::aid-jnr1>3.0.co;2-m
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

In stock of ZB MED Cologne/Königswinter

Zs.A 1232: 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)

Order via subito

This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

Details ▾

Article: The role of ubiquitin in neurotrophin receptor signalling and sorting.

Wooten, M W / Geetha, T

Biochemical Society transactions

2006 Volume 34, Issue Pt 5, Page(s) 757–760

Abstract: NGF (nerve growth factor) binding to TrkA (tropomyosin receptor kinase A) induces dimerization, autophosphorylation and internalization of the receptor to signalling vesicles for delivery of differentiation signals. TrkA interacts with p75 receptor ... ...

Abstract	NGF (nerve growth factor) binding to TrkA (tropomyosin receptor kinase A) induces dimerization, autophosphorylation and internalization of the receptor to signalling vesicles for delivery of differentiation signals. TrkA interacts with p75 receptor through the p62-TRAF-6 (tumour-necrosis-factor-receptor-associated factor 6) complex bridging the two receptors. The atypical protein kinase C is activated and recruited to the receptor complex as well. TrkA is Lys63-polyubiquitinated on Lys485 by the E3 (ubiquitin ligase), TRAF-6, and E2 (ubiquitin-conjugating enzyme), UbcH7. Inhibition of polyubiquitination has been observed to interrupt signalling and internalization. Furthermore, an absence of p62 prevents endosomal localization and signalling. Altogether, these findings reveal Lys63-linked polyubiquitin chains and the shuttling protein p62 co-ordinately regulate TrkA internalization, trafficking and sorting.
MeSH term(s)	Animals ; Brain-Derived Neurotrophic Factor/physiology ; Protein Kinase C/metabolism ; Receptor, trkA/metabolism ; Receptors, Nerve Growth Factor/physiology ; Signal Transduction ; Ubiquitin/physiology
Chemical Substances	Brain-Derived Neurotrophic Factor ; Receptors, Nerve Growth Factor ; Ubiquitin ; Receptor, trkA (EC 2.7.10.1) ; Protein Kinase C (EC 2.7.11.13)
Language	English
Publishing date	2006-11
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	184237-7
ISSN	1470-8752 ; 0300-5127
ISSN (online)	1470-8752
ISSN	0300-5127
DOI	10.1042/BST0340757
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 944: 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)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Of the atypical PKCs, Par-4 and p62: recent understandings of the biology and pathology of a PB1-dominated complex.

Moscat, J / Diaz-Meco, M T / Wooten, M W

Cell death and differentiation

2009 Volume 16, Issue 11, Page(s) 1426–1437

Abstract: The recent identification of a novel protein-protein interaction module, termed PB1, in critical signaling molecules such as p62 (also known as sequestosome1), the atypical PKCs, and Par-6, has unveiled the existence of a new set of signaling complexes, ... ...

Abstract	The recent identification of a novel protein-protein interaction module, termed PB1, in critical signaling molecules such as p62 (also known as sequestosome1), the atypical PKCs, and Par-6, has unveiled the existence of a new set of signaling complexes, which can be central to several biological processes from development to cancer. In this review, we will discuss the most recent advances on the role that the different components of these complexes have in vivo and that are relevant to human disease. In particular, we will review what we are learning from new data from knockout mice, and the indications from human mutations on the real role of these proteins in the physiology and biology of human diseases. The role that PKCzeta, PKClambda/iota, and Par-4 have in lung and prostate cancer in vivo and in humans will be extensively covered in this article, as will the multifunctional role of p62 as a novel hub in cell signaling during cancer and inflammation, and the mechanistic details and controversial data published on its potential role in aggregate formation and signaling. All this published information is shedding new light on the proposed pathological implications of these PB1-regulators in disease and shows their important role in cell physiology.
MeSH term(s)	Adaptor Proteins, Signal Transducing/genetics ; Adaptor Proteins, Signal Transducing/metabolism ; Animals ; Apoptosis Regulatory Proteins/genetics ; Apoptosis Regulatory Proteins/metabolism ; Humans ; Mice ; Protein Interaction Domains and Motifs ; Protein Kinase C/genetics ; Protein Kinase C/metabolism ; Sequestosome-1 Protein ; Tumor Suppressor Proteins/metabolism
Chemical Substances	Adaptor Proteins, Signal Transducing ; Apoptosis Regulatory Proteins ; PARD6A protein, human ; SQSTM1 protein, human ; Sequestosome-1 Protein ; Tumor Suppressor Proteins ; prostate apoptosis response-4 protein ; PKC-3 protein (EC 2.7.11.13) ; Protein Kinase C (EC 2.7.11.13)
Language	English
Publishing date	2009-08-28
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	1225672-9
ISSN	1476-5403 ; 1350-9047
ISSN (online)	1476-5403
ISSN	1350-9047
DOI	10.1038/cdd.2009.119
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 4230: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MG 80: Show issues

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article: Differential expression of PKC isoforms and PC12 cell differentiation.

Wooten, M W

Experimental cell research

1992 Volume 199, Issue 1, Page(s) 111–119

Abstract: Recent reports indicate that the protein kinase inhibitor H7 is capable of inducing both morphological and functional differentiation of a number of neural cell types. This investigation demonstrates that H7 potentiates the neurogenic properties of nerve ...

Abstract	Recent reports indicate that the protein kinase inhibitor H7 is capable of inducing both morphological and functional differentiation of a number of neural cell types. This investigation demonstrates that H7 potentiates the neurogenic properties of nerve growth factor (NGF) in PC12 cells with a concomitant change in the accumulation of the beta II-protein kinase C (beta IIPKC) isoform protein without changes in either alpha or gamma. However, NGF alone stimulates a coordinate increase in all three isoforms. The assay of acetylcholine esterase as a functional marker of neuronal differentiation demonstrates that H7 alone is not capable of stimulating morphological or functional differentiation in PC12 cells. H7 synergizes with NGF through a PKC-dependent pathway and by differential expression of PKC subtypes. The expression of the PKC transcripts for alpha, beta II, and gamma all undergo simultaneous yet differential changes in their patterns of expression during treatment with H7 and/or NGF. These data suggest that isoform switching is regulated primarily at the protein level. Last, these findings suggest that expression of PKC isoforms is tightly coupled with neuronal differentiation and may play a role in the maintenance of the differentiated state.
MeSH term(s)	1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine ; Acetylcholinesterase/genetics ; Acetylcholinesterase/metabolism ; Animals ; Blotting, Northern ; Blotting, Western ; Cell Differentiation/drug effects ; Drug Synergism ; Gene Expression Regulation, Enzymologic/drug effects ; Isoenzymes/genetics ; Isoquinolines/pharmacology ; Nerve Growth Factors/pharmacology ; Neurites/ultrastructure ; Neurons/cytology ; Neurons/enzymology ; PC12 Cells ; Piperazines/pharmacology ; Protein Kinase C/genetics ; Protein Kinase C/metabolism
Chemical Substances	Isoenzymes ; Isoquinolines ; Nerve Growth Factors ; Piperazines ; 1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine (84477-87-2) ; Protein Kinase C (EC 2.7.11.13) ; Acetylcholinesterase (EC 3.1.1.7)
Language	English
Publishing date	1992-03
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	1493-x
ISSN	1090-2422 ; 0014-4827
ISSN (online)	1090-2422
ISSN	0014-4827
DOI	10.1016/0014-4827(92)90468-n
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 563: 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)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article: Alterations in protein kinase C type III-alpha during heat shock of rat embryo fibroblasts.

Wooten, M W

Experimental cell research

1991 Volume 193, Issue 2, Page(s) 274–278

Abstract: Heat shock treatment of rat embryo fibroblasts resulted in a 60% increase in cytosolic protein kinase C activity, in contrast to phorbol ester-induced translocation to the membrane. During reversal of the cells back to the normal temperature a decrease ... ...

Abstract	Heat shock treatment of rat embryo fibroblasts resulted in a 60% increase in cytosolic protein kinase C activity, in contrast to phorbol ester-induced translocation to the membrane. During reversal of the cells back to the normal temperature a decrease in cytosolic PKC activity was observed and paralleled by an increase in protamine kinase activity. Cell lysates prepared from heat shock-treated cells show a marked calcium/phospholipid-dependent phosphorylation of several endogenous PKC substrate proteins, while the 28-kDa stress protein was shown to be a PKC substrate. These cells express the TYPE III-alpha isoform of PKC and, thus, the alterations induced within cells exposed to hyperthermic treatment may reflect a functional significance with regard to the regulation of this specific isoform.
MeSH term(s)	Animals ; Cell Line ; Electrophoresis, Gel, Two-Dimensional ; Heat-Shock Proteins/metabolism ; Hot Temperature ; In Vitro Techniques ; Isoenzymes/metabolism ; Molecular Weight ; Phosphoproteins/chemistry ; Phosphoproteins/metabolism ; Protamine Kinase ; Protein Kinase C/classification ; Protein Kinase C/metabolism ; Protein Kinases/metabolism ; Rats
Chemical Substances	Heat-Shock Proteins ; Isoenzymes ; Phosphoproteins ; Protein Kinases (EC 2.7.-) ; Protamine Kinase (EC 2.7.11.1) ; Protein Kinase C (EC 2.7.11.13)
Language	English
Publishing date	1991-04
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	1493-x
ISSN	1090-2422 ; 0014-4827
ISSN (online)	1090-2422
ISSN	0014-4827
DOI	10.1016/0014-4827(91)90096-d
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 563: 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)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article: Purification and characterization of a novel protamine kinase in HL60 cells.

Soh, Y / Wooten, M W

Journal of biochemistry

2000 Volume 127, Issue 1, Page(s) 95–103

Abstract: A protamine kinase from HL60 cells was purified to near homogeneity by DEAE-Sephacel, protamine-agarose, Hydroxylapatite, and S-200 chromatography. It was purified by 75.8-fold through four chromatographic steps, and 0.67% of total activity was recovered. ...

Abstract	A protamine kinase from HL60 cells was purified to near homogeneity by DEAE-Sephacel, protamine-agarose, Hydroxylapatite, and S-200 chromatography. It was purified by 75.8-fold through four chromatographic steps, and 0.67% of total activity was recovered. The purified enzyme had an apparent molecular mass of 120 kDa and was activated by Mg(2+) or Mn(2+), but inhibited by Ca(2+). Neither phospholipid nor phorbol ester significantly affected the enzyme activity. Staurosporine was the most potent inhibitor of the enzyme among the protein kinase inhibitors tested, K(252a), H(7), heparin, and staurosporine. The purified protamine kinase exhibited a maximum velocity of 5,000 pmol/min/mg and K(m) of 1.3 mM for protamine sulfate as a substrate. Myelin basic protein and protamine sulfate served as the best substrates for the protamine kinase among those tested. The activity of the protamine kinase remained unchanged upon treatment with PMA, retinoic acid, dimethyl sulfoxide, or 1,25 dihydroxy vitamin D(3) for 15 min, while treatment with a differentiating agent, 1,25 dihydroxy vitamin D(3), for one week increased its activity. These results suggest that protamine kinase in HL60 cells is involved in the late stage of the macrophage-monocytic differentiation pathway and may play a role in maintenance of the differentiation after HL60 cells are committed.
MeSH term(s)	Calcitriol/pharmacology ; Cations, Divalent/chemistry ; Chromatography, Affinity ; Chromatography, Gel ; Chromatography, Ion Exchange ; Dimethyl Sulfoxide/pharmacology ; Durapatite ; Enzyme Activation/drug effects ; HL-60 Cells/enzymology ; Humans ; Protamine Kinase/chemistry ; Protamine Kinase/isolation & purification ; Protamine Kinase/metabolism ; Protein Kinase C/metabolism ; Tetradecanoylphorbol Acetate/metabolism ; Tetradecanoylphorbol Acetate/pharmacology ; Tretinoin/pharmacology
Chemical Substances	Cations, Divalent ; Tretinoin (5688UTC01R) ; Durapatite (91D9GV0Z28) ; Protamine Kinase (EC 2.7.11.1) ; Protein Kinase C (EC 2.7.11.13) ; Calcitriol (FXC9231JVH) ; Tetradecanoylphorbol Acetate (NI40JAQ945) ; Dimethyl Sulfoxide (YOW8V9698H)
Language	English
Publishing date	2000-01
Publishing country	England
Document type	Journal Article
ZDB-ID	218073-x
ISSN	1756-2651 ; 0021-924X
ISSN (online)	1756-2651
ISSN	0021-924X
DOI	10.1093/oxfordjournals.jbchem.a022589
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Uc I Zs.202: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article: Nerve growth factor-induced differentiation of PC12 cells employs the PMA-insensitive protein kinase C-zeta isoform.

Coleman, E S / Wooten, M W

Journal of molecular neuroscience : MN

1994 Volume 5, Issue 1, Page(s) 39–57

Abstract: To elucidate the role of protein kinase C (PKC) in nerve growth factor (NGF)-induced differentiation, PMA downregulation of pheochromocytoma (PC12) cells was undertaken. Prolonged treatment (2 d) of PC12 cells with PMA (1 microM) resulted in depleting ... ...

Abstract	To elucidate the role of protein kinase C (PKC) in nerve growth factor (NGF)-induced differentiation, PMA downregulation of pheochromocytoma (PC12) cells was undertaken. Prolonged treatment (2 d) of PC12 cells with PMA (1 microM) resulted in depleting the cells of alpha, beta, delta, and epsilon-PKC isoforms, but had no effect on the expression of the atypical PKC isoform zeta. PC12 cells, which expressed only PKC zeta, were evaluated for their responses to NGF. Removal of the PMA-sensitive PKC isoforms enhanced the ability of NGF to promote neurite extension. Both the percentage cells with neurites and length of neurites were increased in the PMA-treated cells, whereas no effect was observed on the number of neurites per cell or branching of individual neurites. In addition, PMA downregulation resulted in an increase in the incorporation of 3H-thymidine without any significant effect on the expression of c-fos. Addition of NGF to PC12 cells depleted of the PMA-sensitive PKC isoforms resulted in the activation of PKC zeta (Wooten et al., 1994). To test whether the transient activation of PKC zeta is a necessary component of the neuritogenetic pathway, antisense oligonucleotide strategy was utilized to remove this particular PKC isoform. The addition of a 20-bp antisense oligonucleotide directed against the 5' coding sequence of PKC zeta attenuated NGF-induced neurite outgrowth in PC12 cells lacking PMA-sensitive PKC isoforms. Sense oligonucleotide directed at the same site was without effect on NGF responses. These data indicate that PKC zeta comprises a portion of the NGF pathway and underscores the importance of this isoform in neuronal differentiation. Moreover, these findings demonstrate that the PMA-insensitive pathway, which was previously characterized as PKC-independent, and the neurite induction pathway are synonymous and mediated by PKC zeta.
MeSH term(s)	Animals ; Cell Differentiation/drug effects ; Down-Regulation ; Genes, fos ; Isoenzymes/analysis ; Isoenzymes/physiology ; Nerve Growth Factors/pharmacology ; Neurites/drug effects ; PC12 Cells ; Protein Kinase C/analysis ; Protein Kinase C/physiology ; Rats ; Tetradecanoylphorbol Acetate/pharmacology
Chemical Substances	Isoenzymes ; Nerve Growth Factors ; Protein Kinase C (EC 2.7.11.13) ; Tetradecanoylphorbol Acetate (NI40JAQ945)
Language	English
Publishing date	1994
Publishing country	United States
Document type	Journal Article ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	1043392-2
ISSN	0895-8696
ISSN	0895-8696
DOI	10.1007/BF02736693
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 3006: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (2.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article: Heterogeneity of protein kinase C isoform expression in chemically induced HL60 cells.

Seibenhener, M L / Wooten, M W

Experimental cell research

1993 Volume 207, Issue 1, Page(s) 183–188

Abstract: Column chromatographic separation of HL60 cell lysates by hydroxylapatite and immunoblotting with protein kinase C (PKC) isoform-specific antisera revealed the presence of four peaks of activity consisting of PKC gamma, beta, epsilon, delta, alpha, and ... ...

Abstract	Column chromatographic separation of HL60 cell lysates by hydroxylapatite and immunoblotting with protein kinase C (PKC) isoform-specific antisera revealed the presence of four peaks of activity consisting of PKC gamma, beta, epsilon, delta, alpha, and zeta. In cells treated with phorbol 12-myristate 13-acetate (PMA), 1,25-dihydroxyvitamin D3, retinoic acid, or dimethyl sulfoxide differential changes in the expression of the four peak activities occurred with treatment. During PMA-induced differentiation, PKC activity diminished for peaks 2, 3, and 4 while immunoreactivity increased for beta, delta, and zeta. In addition, all inducers were found to increase the levels of each of the PKC mRNAs. These results document for the first time differential changes in the expression of PKC isoforms in one cell line elicited by different agents and suggest that alterations in substrate preference may occur, which accounts for changes in the activity of PKC.
MeSH term(s)	Amino Acid Sequence ; Cell Line/drug effects ; Cell Line/metabolism ; Dimethyl Sulfoxide/pharmacology ; Gene Expression Regulation, Enzymologic ; Humans ; Isoenzymes/metabolism ; Molecular Sequence Data ; Phorbol Esters/pharmacology ; Protein Kinase C/metabolism ; RNA, Messenger/analysis ; Substrate Specificity ; Vitamin D/pharmacology
Chemical Substances	Isoenzymes ; Phorbol Esters ; RNA, Messenger ; Vitamin D (1406-16-2) ; Protein Kinase C (EC 2.7.11.13) ; Dimethyl Sulfoxide (YOW8V9698H)
Language	English
Publishing date	1993-07
Publishing country	United States
Document type	Comparative Study ; Journal Article ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	1493-x
ISSN	1090-2422 ; 0014-4827
ISSN (online)	1090-2422
ISSN	0014-4827
DOI	10.1006/excr.1993.1178
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 563: 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)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article: pp42/44MAP kinase is a component of the neurogenic pathway utilized by nerve growth factor in PC12 cells.

Lloyd, E D / Wooten, M W

Journal of neurochemistry

1992 Volume 59, Issue 3, Page(s) 1099–1109

Abstract: Nerve growth factor-stimulated mitogen-activated protein kinase (pp42/44MAP) kinase was characterized by sequential column chromatography on DEAE-Sephacel, phenyl-Sepharose CL4B, and S-200. The kinase displayed an apparent molecular mass of 42 kDa and ... ...

Abstract	Nerve growth factor-stimulated mitogen-activated protein kinase (pp42/44MAP) kinase was characterized by sequential column chromatography on DEAE-Sephacel, phenyl-Sepharose CL4B, and S-200. The kinase displayed an apparent molecular mass of 42 kDa and reacted with an antiphosphotyrosine antibody. Peptide mapping of myelin basic protein revealed the presence of one phosphopeptide that was phosphorylated on Thr-97. pp42/44MAP kinase activity was dependent on Mg2+ and inhibited by K252a both in vitro and in vivo. Nerve growth factor-stimulated kinase activation was diminished by down-regulation of protein kinase C with 200 nM 12-phorbol 13-myristate acetate or with staurosporine (1 nM), a protein kinase C inhibitor. Genistein, a protein tyrosine kinase inhibitor, blocked nerve growth factor-mediated neurite extension as well as diminished activation of pp42/44MAP kinase. Our data demonstrate that activation of this kinase system by nerve growth factor displays a requirement for both protein kinase C as well as protein tyrosine kinase. In addition, other agents that are capable of promoting neurite outgrowth in PC12 cells, such as fibroblast growth factor or dibutyryl cyclic AMP, do so independently of activating this kinase system.
MeSH term(s)	Animals ; Axons/physiology ; Calcium-Calmodulin-Dependent Protein Kinases ; Growth Substances/pharmacology ; Magnesium/pharmacology ; Nerve Growth Factors/pharmacology ; Nerve Growth Factors/physiology ; Nerve Tissue/growth & development ; PC12 Cells/metabolism ; PC12 Cells/physiology ; Protein Kinase Inhibitors ; Protein Kinases/chemistry ; Protein Kinases/isolation & purification ; Protein Kinases/physiology
Chemical Substances	Growth Substances ; Nerve Growth Factors ; Protein Kinase Inhibitors ; Protein Kinases (EC 2.7.-) ; Calcium-Calmodulin-Dependent Protein Kinases (EC 2.7.11.17) ; Magnesium (I38ZP9992A)
Language	English
Publishing date	1992-09
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	80158-6
ISSN	1471-4159 ; 0022-3042 ; 1474-1644
ISSN (online)	1471-4159
ISSN	0022-3042 ; 1474-1644
DOI	10.1111/j.1471-4159.1992.tb08352.x
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Ui II Zs.170: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article: Alcohols synergize with NGF to induce early differentiation of PC12 cells.

Wooten, M W / Ewald, S J

Brain research

1991 Volume 550, Issue 2, Page(s) 333–339

Abstract: The role of alcohols in affecting neuromorphogenesis was investigated in a single cell type, pheochromocytoma (PC12). The effect of ethanol at physiological concentrations in this system leads to enhanced morphological and functional differentiation in ... ...

Abstract	The role of alcohols in affecting neuromorphogenesis was investigated in a single cell type, pheochromocytoma (PC12). The effect of ethanol at physiological concentrations in this system leads to enhanced morphological and functional differentiation in combination with nerve growth factor (NGF). PC12 cells treated with a suboptimal concentration of NGF (30 ng/ml) and an alcohol (87 mM) underwent rapid morphological differentiation which was dependent upon the side chain length of the alcohol MeOH less than EtOH less than PrOH less than BuOH. Pyrazole at either 5 or 10 mM had no effect on alcohol induced neurite extension. Assessment of the degree of differentiation promoted by the various alcohols was quantified by an increase in neurite extension, a decrease in the incorporation of [3H]thymidine, an increase in acetylcholine esterase (AChE) activity and immunostaining with neuron specific enolase. Thus, alcohols may function in a specific manner by interacting with transmembrane signalling pathways which promote gene expression and neuronal differentiation.
MeSH term(s)	Acetylcholinesterase/metabolism ; Adrenal Gland Neoplasms ; Alcohols/pharmacology ; Animals ; Cell Differentiation/drug effects ; Cell Line ; Drug Synergism ; Kinetics ; Nerve Growth Factors/pharmacology ; Pheochromocytoma ; Rats ; Structure-Activity Relationship
Chemical Substances	Alcohols ; Nerve Growth Factors ; Acetylcholinesterase (EC 3.1.1.7)
Language	English
Publishing date	1991-06-07
Publishing country	Netherlands
Document type	Comparative Study ; Journal Article ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	1200-2
ISSN	1872-6240 ; 0006-8993
ISSN (online)	1872-6240
ISSN	0006-8993
DOI	10.1016/0006-8993(91)91337-z
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 161: 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)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

To top

Full text online

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito