Last update 01 Nov 2024

Transferase x PKC

Last update 01 Nov 2024

Basic Info

Related Targets

TransferasePKC

Drugs associated with Transferase x PKC

GO-7716

Target

PKC x Transferase

Mechanism

PKC inhibitors [+1]

Active Org.-

Originator Org.

Gödecke GmbH

Active Indication-

Inactive Indication

HIV Infections

Drug Highest PhaseDiscontinued

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with Transferase x PKC

100 Translational Medicine associated with Transferase x PKC

0 Patents (Medical) associated with Transferase x PKC

Literatures (Medical) associated with Transferase x PKC

01 Jan 2000·Clinical and Experimental MetastasisQ3 · MEDICINE

Inostamycin, an inhibitor of cytidine 5'-diphosphate 1,2-diacyl-sn-glycerol (CDP-DG): inositol transferase, suppresses invasion ability by reducing productions of matrix metalloproteinase-2 and -9 and cell motility in HSC-4 tongue carcinoma cell line.

Q3 · MEDICINE

Article

Author: Yasumasa Kato ; Naoki Sakai ; Yoji Nagashima ; Shinri Koshika ; Shigeru Furukawa ; Mamoru Tsukuda ; Yuh Baba ; Masaya Imoto ; Hiroko Kagata ; Izumi Mochimatsu

Inostamycin is an inhibitor of cytidine 5'-diphosphate 1,2-diacyl-sn-glycerol (CDP-DG): inositol transferase. It significantly reduced epidermal growth factor (EGF)-induced in vitro invasion of the tongue carcinoma cell line, HSC-4, through reconstituted basement membrane Matrigel. Since phosphatidylinositol (PI) 4,5-biphosphate is important for signal transduction through protein kinase C and actin reorganisation, we further examined the effect of inostamycin on production of two matrix metalloproteinases (MMPs), MMP-2 and -9, and on cell motility. Zymographic analysis showed that inostamycin suppressed pro-MMP-2 and pro-MMP-9 levels at a dose-dependent fashion, while MMP-2 activity was not significantly affected. By reverse transcription-polymerase chain reaction, it was found that inostamycin diminished steady state levels of MMP-2 and -9 but not membrane type 1-MMP mRNA expressions. Inostamycin partially blocked both EGF- and phorbol 12-myristate 13-acetate-stimulated pro-MMP-9 production. A cytoplasmic calcium chelator (BAPTA-AM) dramatically elevated pro- MMP-9 and slightly elevated pro-MMP-2 secretions. EGF-stimulated motility of HSC-4 cells was suppressed by inostamycin treatment along with reduction of actin cytoskeletal reorganisation, filopodia formation and cdc42 expression. These results suggested that inostamycin would be useful for an anti-invasive agent in tongue cancer.

01 Nov 1998·Biochemical and Biophysical Research CommunicationsQ3 · BIOLOGY

Requirement for Geranylgeranyl Transferase I and Acyl Transferase in the TGF-β-Stimulated Pathway Leading to Elastin mRNA Stabilization

Q3 · BIOLOGY

Article

Author: Saı̈d M Sebti ; Umberto Kucich ; Joel Rosenbloom ; William R Abrams ; Gloria Shen ; Junko Ohkanda ; Michelle A Blaskovich ; Andrew D Hamilton ; Joan C Rosenbloom

The TGF-betas are multipotent in their biological activity, modulating cell growth and differentiation as well as extracellular matrix deposition and degradation. Most of these activities involve modulation of gene transcription. However, TGF-beta1 has been shown previously to substantially increase the expression of elastin by stabilization of tropoelastin mRNA through a signaling pathway which involves a phosphatidylcholine-specific phospholipase and a protein kinase C. The present results, through the use of specific inhibitors of geranylgeranyl transferase I, farnesyl transferase, and acyl transferase, demonstrate that geranylgeranylated and acylated, but not farnesyslated protein(s) is required for this TGF-beta1 effect. In addition, the general tyrosine kinase inhibitor genistein completely blocked this TGF-beta1 effect. The results suggest that the TGF-beta1 signaling pathway requires not only receptor ser/thr kinase activity, but also tyrosine kinase and small GTPase activities.

01 Mar 1994·American Journal of Physiology-Cell Physiology

Receptor- and phorbol ester-mediated phospholipase D activation in rat parotid involves two different pathways

Article

Author: Rossignol, B. ; Guillemain, I.

We have investigated phospholipase D (PLD) activation in rat parotid acini prelabeled with [14C]stearic acid. In the presence of 2% ethanol, muscarinic and alpha-adrenergic agonists stimulated the formation of [14C]phosphatidylethanol as a result of a PLD activity. The calcium ionophore, ionomycin, and the phorbol esters, 4 beta-phorbol 12-myristate 13-acetate (PMA) and phorbol 12,13-dibutyrate (PDBu), also stimulated phosphatidylethanol accumulation, but 1-oleyl-2-acetyl-sn-glycerol (OAG), a permeant analogue of diacylglycerol did not. Chelerythrine and staurosporine, two inhibitors of protein kinase C, failed to affect any response. These results suggest that protein kinase C was not involved in the regulation of PLD activity. A difference between PLD regulation by PMA and receptor-mediated agonists was observed with regard to the extracellular calcium requirement. Our results strongly suggest that PLD activation in parotid acini involved different pathways: a calcium-dependent pathway activated by receptor-mediated agonists and a calcium-independent pathway activated by phorbol esters. Moreover, we observed that PLD activation did not result in any change in phosphatidic acid level. We propose that the phosphatidyl transferase activity of PLD reflected a metabolic pathway which may allow a base-exchange reaction in parotid gland.

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