The role of protein phosphorylation in the control of cell growth and differentiation

Lord, Janet M.; Bunce, Christopher M.; Brown, Geoffrey

doi:10.1038/bjc.1988.256

Cited by 23 publications

(17 citation statements)

References 73 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The isoforms showed restricted tissue and subcellular distributions suggesting that PKC isoenzymes have specific cellular functions.The function of kinases can be altered upon activation, since their subcellular distribution can change providing access to various substrates [48]. Furthermore, a subcellular translocation of PKC has been observed during activation of the enzyme [17].…”

Section: Activation and Proliferation Of Dense And Buoyant Cellsmentioning

confidence: 99%

“…The direction of the translocation of a particular PKC isoenzyme (e.g. to cell or nuclear membrane) might be specific for the induction signal leading to different, but specific events [48]. In this context, it is of interest that differences in the protein phosphorylation patterns induced by PMA and bryostatin 1 have been found [19].…”

Section: Activation and Proliferation Of Dense And Buoyant Cellsmentioning

confidence: 99%

See 1 more Smart Citation

Synergistic action of calcium ionophore A23187 and protein kinase C activator bryostatin 1 on human B cell activation and proliferation

et al. 1990

View full text Add to dashboard Cite

In this study we have examined the immunostimulatory effects of the macrocyclic lactone bryostatin 1 on various aspects of B cell activation and proliferation using human tonsillar B cells. Bryostatin 1 is an activator of protein kinase C (PKC) and its properties were compared to those of the classical PKC activator phorbol 12-myristate 13-acetate (PMA), a phorbol ester. Time-course kinetics and dose-response curves of RNA and DNA synthesis induced by bryostatin 1 or PMA were comparable, albeit the phorbol ester was significantly more potent. The responses triggered by both bryostatin 1 and PMA could be blocked by the PKC inhibitor H7. Bryostatin 1 and PMA mediated similar effects with regard to the activation parameters, increase in cell size, expression of activation-associated antigens and hyperexpression of major histocompatibility complex class II antigens. Addition of the calcium ionophore A23187 to bryostatin 1-treated cultures resulted in synergistically enhanced activation and proliferation responses, and this potentiation by A23187 could be inhibited by cyclosporin A. Bryostatin 1 antagonized the effects of PMA-triggered stimulation in a time- and dose-dependent manner. The basis for this modulation of PMA-induced effects and the reason for the difference in the abilities of the two agents to stimulate B cells is unclear; possibly, bryostatin 1 and PMA activate different isoforms of PKC and elicit different signals on intracellular biochemical pathways. Bryostatin 1 lacks the tumor-promoting activity of PMA and is a potent anti-neoplastic substance. These features together with its immunomodulatory properties qualify bryostatin 1 as a candidate for in vivo use as a biological response modifier.

show abstract

Section: Activation and Proliferation Of Dense And Buoyant Cellsmentioning

confidence: 99%

Section: Activation and Proliferation Of Dense And Buoyant Cellsmentioning

confidence: 99%

Synergistic action of calcium ionophore A23187 and protein kinase C activator bryostatin 1 on human B cell activation and proliferation

et al. 1990

View full text Add to dashboard Cite

show abstract

“…Studies of inositol polyphosphates have revealed that growing HL60 cells contain a substantial concentration of inositol 1,3,4,S16-pentakisphosphate [Ins (1,3,4,5,6)P5] (27 ,UM) and very high levels of inositol hexakisphosphate ( > 50 p~) , as compared with the level of the calcium-mobilizing second messenger inositol 1,4,5 trisphosphate, which is approximately 0.4 ,UM [13]. While the function of these abundant inositol polyphosphates remains unknown, HL60 cells represent a system in which their levels can be predictably regulated and correlated with changes in cell status.…”

Section: Lnositol Transport and Metabolismmentioning

confidence: 99%

“…Protein kinases, such as the cdc2 serinekhreonine protein kinase, have been shown to regulate the progression of cells through the cell cycle [S] and several proteins which fluctuate in concentration through the cell cycle (cyclins) appear to be regulatory subunits of the cdc2 kinase. In addition, a number of cell-cycle-related proteins and enzymes involved in DNA replication are phosphoproteins [6]. Both DNA replication and mitosis are co-ordinated by the activity of various kinases, and progress is being made in delineating the molecular pathways which effect this control.…”

mentioning

confidence: 99%

Protein phosphorylation events and changes in inositol metabolism during HL60 cell differentiation

Lord

Bunce

French

et al. 1991

Biochemical Society Transactions

View full text Add to dashboard Cite

“…Such a cascade would presumably activate a process of redirection of nuclear genetic programs leading to the control of given cellular functions like the control of cell growth (12,17,20,28,29).…”

mentioning

confidence: 99%

Nuclear Phosphoinositide Signalling Enzyme in Human B Lymphoid Cells.

Cataldi¹,

Pietro²,

Robuffo³

et al. 1994

Cell Struct. Funct.

View full text Add to dashboard Cite

ABSTRACT. The modulation of phosphoinositidase C (PIC) beta activity upon interferon treatment in Burkitt lymphoma cells (Daudi) and its localization and expression have been analyzed by Western blotting, immunocytochemical and immunoelectronmicroscopy analysis. Results have disclosed an early increase of phosphatidyl-inositol-bisphosphate (PIP2) hydrolysis at nuclear level upon interferon (IFN) treatment paralleled by the evidence of an increase of PIC beta 1 expression. PIC beta 1 expression has been detected in the nuclear compartment also in a clone of Daudicells selected for the resistance to the antiproliferative action of interferon alpha but no modulation of the enzymehas been detected upon interferon treatment. Since no changes in terms of PIP2 hydrolysis have been found at nuclear level in this selected line, we suggest that the antiproliferative action of interferon on Burkitt lymphomacells is mediated by a possible recruitment of nuclear PIC beta 1 expression.The control and modulation of cell growth by the interaction of specific agents with cell surface receptors is an intriguing phenomenon certainly driven by cascades of several molecular events able to transduce biological signals to the cell nucleus. Such a cascade would presumably activate a process of redirection of nuclear genetic programs leading to the control of given cellular functions like the control of cell growth (12,17,20,28,29).Amongthe pathways involved in the signal transduction system from the plasma membraneto the nucleus and inside the nucleus itself, inositol lipids have been recently shown to be possible regulatory molecules in the control of signals related to cell metabolism (2, ll, 13, 15, 16, 18, 21, 26). This signalling system generating second messengers has been recently found involved mainly at nuclear level in the metabolic events related to the growth inhibitory action of interferon alpha in Daudi lymphoma cells (5, 10,22,27). The response of the cytoplasmic compartment to interferon treatment in terms of inositol lipids, in fact, has been reported to display different features compared to the nucleus suggesting the recruitment of different routes at plasma membrane and nuclear level (7). These results have prompted the question of the intracellular localization and distribution of phosphoinositidase C in Daudi lymphomacells and the modulation, if any, of its expression upon inter- plemented with 10% fetal calf serum, glutamine, penicillinstreptomycin and neomycin. Cells from Daudi resistant clones were continuously maintained in culture in the presence of recombinant interferon alpha 2A (La Roche). The resistant phenotype was stable without any interferon treatment for up to six culture doublings and resistant cells underwent at least three doublings without interferon prior to use in experiments. Viability was determined by the trypan blue exclusion test. R interferon alpha 2A treatment of the cells (500 I.U. /ml) was performed for different intervals up to 24 hr. Cellfractionation. Cells were resuspended in a bu...

show abstract

The role of protein phosphorylation in the control of cell growth and differentiation

Cited by 23 publications

References 73 publications

Synergistic action of calcium ionophore A23187 and protein kinase C activator bryostatin 1 on human B cell activation and proliferation

Synergistic action of calcium ionophore A23187 and protein kinase C activator bryostatin 1 on human B cell activation and proliferation

Protein phosphorylation events and changes in inositol metabolism during HL60 cell differentiation

Nuclear Phosphoinositide Signalling Enzyme in Human B Lymphoid Cells.

Contact Info

Product

Resources

About