A Novel Acidic Form of the Phosphatidylinositol Transfer Protein Is Preferentially Retained in Permeabilized Swiss Mouse 3T3 Fibroblasts

1994 ◽  
Vol 215 (1) ◽  
pp. 109-113 ◽  
Author(s):  
K.J. de Vries ◽  
A. Momchilova-Pankova ◽  
G.T. Snoek ◽  
K.W.A. Wirtz
Keyword(s):  
Swiss Mouse ◽  
Transfer Protein ◽  
3T3 Fibroblasts ◽  
Acidic Form ◽  
Phosphatidylinositol Transfer Protein ◽  
Phosphatidylinositol Transfer

scholarly journals Phosphorylation and redistribution of the phosphatidylinositol-transfer protein in phorbol 12-myristate 13-acetate- and bombesin-stimulated Swiss mouse 3T3 fibroblasts

1993 ◽  
Vol 291 (2) ◽  
pp. 649-656 ◽  
Author(s):  
G T Snoek ◽  
J Westerman ◽  
F S Wouters ◽  
K W A Wirtz
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Swiss Mouse ◽  
Quiescent Cells ◽  
Transfer Protein ◽  
Kinase C ◽  
Phosphatidylinositol Transfer Protein ◽  
Phosphatidylinositol Transfer ◽  
Stimulation Of

By immunofluorescence microscopy it was shown that the phosphatidylinositol-transfer protein (PI-TP) becomes associated with the Golgi membranes when confluent (quiescent) Swiss mouse 3T3 fibroblast cells are stimulated with phorbol 12-myristate 13-acetate (PMA) and bombesin. Dibutyryl cyclic AMP or dexamethasone had no effect on the intracellular redistribution of PI-TP. In exponentially growing cells and in serum-starved (semi-quiescent) cells, PI-TP is already associated with Golgi structures. Stimulation of semi-quiescent cells by PMA resulted in a rapid redistribution of PI-TP. A similar yet slower response was observed after stimulation with bombesin. Stimulation of semi-quiescent 3T3 cells by PMA significantly increased the phosphorylation of PI-TP, as shown by immunoprecipitation of PI-TP from pre-labelled cells. No significant increase in phosphorylation of PI-TP was observed after stimulation of these cells by bombesin. Purified PI-TP was shown to be a substrate for protein kinase C in vitro. The possibility that the phosphorylation of PI-TP after activation of protein kinase C is involved in the observed redistribution of PI-TP is discussed.

scholarly journals An isoform of the phosphatidylinositol-transfer protein transfers sphingomyelin and is associated with the Golgi system

1995 ◽  
Vol 310 (2) ◽  
pp. 643-649 ◽  
Author(s):  
K J de Vries ◽  
A A J Heinrichs ◽  
E Cunningham ◽  
F Brunink ◽  
J Westerman ◽  
...  
Keyword(s):  
Molecular Mass ◽  
Bovine Brain ◽  
Beta Activity ◽  
Cytosol Fraction ◽  
Transfer Protein ◽  
3T3 Fibroblasts ◽  
Golgi System ◽  
Phosphatidylinositol Transfer Protein ◽  
Terminal Amino ◽  
Phosphatidylinositol Transfer

An isoform of the phosphatidylinositol-transfer protein (PI-TP) was identified in the cytosol fraction of bovine brain. This protein, designated PI-TP beta, has an apparent molecular mass of 36 kDa and an isoelectric point of 5.4. The N-terminal amino acid sequence (21 residues) is 90% similar to that of bovine brain PI-TP, henceforth designated PI-TP alpha (molecular mass 35 kDa and pI 5.5). As observed for PI-TP alpha, PI-TP beta has a distinct preference for phosphatidylinositol over phosphatidylcholine. In addition, it expresses a high transfer activity towards sphingomyelin. PI-TP alpha lacks this activity completely. By indirect immunofluorescence we demonstrated that, in Swiss mouse 3T3 fibroblasts, PI-TP beta is preferentially associated with the Golgi system whereas PI-TP alpha is predominantly present in the cytoplasm and the nucleus. In cytosol-depleted HL60 cells, both PI-TP alpha and PI-TP beta were equally effective at reconstituting guanosine 5′-[gamma-thio]triphosphate-mediated phospholipase C beta activity.

An essential role for phosphatidylinositol transfer protein in phospholipase C-Mediated inositol lipid signaling

Cell ◽  
1993 ◽  
Vol 74 (5) ◽  
pp. 919-928 ◽  
Author(s):  
Geraint M.H. Thomas ◽  
Emer Cunningham ◽  
Amanda Fensome ◽  
Andrew Ball ◽  
Nicholas F. Totty ◽  
...  
Keyword(s):  
Phospholipase C ◽  
Essential Role ◽  
Lipid Signaling ◽  
Transfer Protein ◽  
Phosphatidylinositol Transfer Protein ◽  
Phosphatidylinositol Transfer

scholarly journals Phosphatidylinositol Transfer Protein Expression Altered by Aging and Parkinson Disease

2006 ◽  
Vol 26 (7-8) ◽  
pp. 1151-1164 ◽  
Author(s):  
Małgorzata Chalimoniuk ◽  
Gerry T. Snoek ◽  
Agata Adamczyk ◽  
Andrzej Małecki ◽  
Joanna B. Strosznajder
Keyword(s):  
Protein Expression ◽  
Parkinson Disease ◽  
Transfer Protein ◽  
Phosphatidylinositol Transfer Protein ◽  
Phosphatidylinositol Transfer
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