Hydrolysis of Glycosyl-Phosphatidylinositol in Response to Insulin is Reduced in Cells Bearing Kinase-Deficient Insulin Receptors

1990 ◽  
Vol 2 (2) ◽  
pp. 91-97 ◽  
Author(s):  
Mayte Villalba ◽  
Jose F. Alvarez ◽  
David S. Russell ◽  
Jose M. Mato ◽  
Ora M. Rosen
Diabetes ◽  
1993 ◽  
Vol 42 (9) ◽  
pp. 1262-1272 ◽  
Author(s):  
J. M. Ruiz-Albusac ◽  
J. A. Zueco ◽  
E. Velazquez ◽  
E. Blazquez

1993 ◽  
Vol 268 (27) ◽  
pp. 19998-20001
Author(s):  
B Draznin ◽  
L Chang ◽  
J.W. Leitner ◽  
Y Takata ◽  
J.M. Olefsky

1952 ◽  
Vol s3-93 (23) ◽  
pp. 259-268
Author(s):  
GORDON MENZIES

1. In continuation of work already reported (Menzies, 1949) further data are presented on the structure and cyto-chemistry of the granules in the oxyntic cells of the rat's stomach. 2. After multiple doses of pilocarpine or histamine, and after feeding, the phospholipine (as shown by acid haematein) is shed from some or all of the granules. The lipine first leaves the granules in cells situated in the basal part of the tubules, and finally those in the neck of the tubules, but a non-lipine lipoid remains in all the granules (as shown by sudan black). 3. The granules enlarge after prolonged starvation as they do after a single injection of pilocarpine; but after extraction of lipoids by hot pyridine and subsequent straining with iron haematoxylin, enlargement (i.e. of the non-lipoid moiety) is shown only after prolonged starvation. 4. A light, uncoloured central area is found in some of the largest granules after feeding and colouring with acid haematein. 5. An acid phosphatase appears in the oxyntic cells whose granules are about to lose their lipine component, and it disappears when they have done so. It is suggested that the acid phosphatase may cause hydrolysis of the phospholipine. 6. Only after prolonged starvation is there any apparent change in granule numbers, when they are decreased.


1985 ◽  
Vol 27 (4) ◽  
pp. 401-414 ◽  
Author(s):  
Cecilia Hofmann ◽  
Marco Crettaz ◽  
Pamela Bruns ◽  
Patricia Hessel ◽  
Gina Hadawi

2002 ◽  
Vol 68 (1) ◽  
pp. 10-19 ◽  
Author(s):  
Juan Miguel Ruiz-Albusac ◽  
Esther Velázquez ◽  
Javier Iglesias ◽  
Encarnacion Jimenez ◽  
Enrique Blázquez

The molecular events involved in the cellular actions of insulin remain unexplained. Some of the acute actions of the hormone may be due to the intracellular generation of a chemical substance which modulates certain enzyme activities. Such an enzymemodulating substance has been identified as an inositol phosphate-glycan, produced by the insulin-sensitive hydrolysis of a glycosyl-phosphatidylinositol (glycosyl-Ptdlns) precursor. This precursor glycolipid is structurally similar to the glycosylphosphoinositide membrane protein anchor. The exposure of fat, liver or muscle cells to insulin results in the hydrolysis of glycosyl-Ptdlns, giving rise to the inositol phosphate glycan and diacylglycerol. This hydrolysis reaction is catalysed by a glycosyl-PtdIns-specific phospholipase C. This enzyme has been characterized and purified from a plasma membrane fraction of liver. This reaction also results in the acute release of certain glycosyl-Ptdlns-anchored proteins from the cell surface. Elucidation of the functional role of glycosyl-phosphoinositides in the generation of second messengers or the release of proteins may provide further insights into the pleiotropic nature of insulin action.


1989 ◽  
Vol 261 (3) ◽  
pp. 811-818 ◽  
Author(s):  
N M Hooper ◽  
A J Turner

Renal dipeptidase (EC 3.4.13.11) has been solubilized from pig kidney microvillar membranes with n-octyl-beta-D-glucopyranoside and then purified by affinity chromatography on cilastatin-Sepharose. The enzyme exists as a disulphide-linked dimer of two identical subunits of Mr 45,000 each. The purified dipeptidase partitioned into the detergent-rich phase upon phase separation in Triton X-114 and reconstituted into liposomes consistent with the presence of the glycosyl-phosphatidylinositol membrane anchor. The N-terminal amino acid sequence of the amphipathic, detergent-solubilized, form of renal dipeptidase was identical with that of the hydrophilic, phospholipase-solubilized, form, locating the membrane anchor at the C-terminus of the protein. The glycosyl-phosphatidylinositol anchor of both purified and microvillar membrane renal dipeptidase was a substrate for an activity in pig plasma which displayed properties similar to those of a previously described phospholipase D. The cross-reacting determinant of the glycosyl-phosphatidylinositol anchor was generated by incubation of purified renal dipeptidase with bacterial phosphatidylinositol-specific phospholipase c, whereas the anchor-degrading activity in plasma failed to generate this determinant.


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