Release of alkaline phosphatase from membranes by a phosphatidylinositol-specific phospholipase C.

Low, Martin G.; Finean, J.B.

doi:10.1042/bj1670281

Cited by 215 publications

(68 citation statements)

References 11 publications

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“…Later, human placental AP was the first protein identified to be fixed to the plasma membrane by a GPI anchor and to be released by bacterial phosphatidylinositol-specific phospholipase C (PI-PLC) [551,552]. Yet, depending on the system investigated, various percentages of the enzyme proved to be PI-PLCresistant, presumably as a result of inositol acylation [553,554].…”

Section: Glycosylationmentioning

confidence: 99%

Cellular function and molecular structure of ecto-nucleotidases

Zimmermann

Zebisch

Sträter

2012

Purinergic Signalling

878

922

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Ecto-nucleotidases play a pivotal role in purinergic signal transmission. They hydrolyze extracellular nucleotides and thus can control their availability at purinergic P2 receptors. They generate extracellular nucleosides for cellular reuptake and salvage via nucleoside transporters of the plasma membrane. The extracellular adenosine formed acts as an agonist of purinergic P1 receptors. They also can produce and hydrolyze extracellular inorganic pyrophosphate that is of major relevance in the control of bone mineralization. This review discusses and compares four major groups of ectonucleotidases: the ecto-nucleoside triphosphate diphosphohydrolases, ecto-5′-nucleotidase, ecto-nucleotide pyrophosphatase/phosphodiesterases, and alkaline phosphatases. Only recently and based on crystal structures, detailed information regarding the spatial structures and catalytic mechanisms has become available for members of these four ecto-nucleotidase families. This permits detailed predictions of their catalytic mechanisms and a comparison between the individual enzyme groups. The review focuses on the principal biochemical, cell biological, catalytic, and structural properties of the enzymes and provides brief reference to tissue distribution, and physiological and pathophysiological functions.

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Section: Glycosylationmentioning

confidence: 99%

Cellular function and molecular structure of ecto-nucleotidases

Zimmermann

Zebisch

Sträter

2012

Purinergic Signalling

878

922

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“…A few externally exposed plasma-membrane proteins from protozoan and mammalian origin, however, are anchored via a covalently attached glycolipid which contains phosphatidylinositol (PI), and these proteins can be released from the membranes by phospholipases C (PLC) [4,5]. The growing list of glycoproteins of this type comprises the variable surface glycoproteins (VSG) of trypanosomes [6,7], the p63 surface glycoprotein of Leishmania [8], the membrane forms of alkaline phosphatase [9], acetylcholinesterase [10], 5'-nucleotidase [ 1 1,12], the 120 kDa form of rodent neural-cell adhesion molecule ('NCAM') [13], and several immunologically relevant surface proteins such as decay-accelerating factor ('DAF') [14], the rat lymphocyte alloantigen RT-6.2 [15], the mouse Ly-6 antigen [16] and the Thy-I antigen of lymphocytes and brain cells [17,18]. Considerable chemical information exists about the membrane-anchoring glycolipid of VSG and Thy-i; amino-acid-sequencing studies revealed in both cases that the mature molecules lack a C-terminal stretch of hydrophobic amino acids predicted from the cDNA sequences [17,19,20].…”

Section: Introductionmentioning

confidence: 99%

Glycolipid anchors are attached to Thy-1 glycoprotein rapidly after translation

Conzelmann

Spiazzi

Bron

1987

Biochemical Journal

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The attachment of glycolipid anchors to the Thy-1 glycoprotein during biosynthesis was followed by the change of detergent-binding properties of biosynthetically labelled Thy-1 precursors upon phospholipase C treatment in the murine thymoma lines BW5147 and S1A. In S1A, 80% of the Thy-1 molecules were phospholipase-C-sensitive after a 2 min pulse with [35S]methionine, indicating that these molecules were already anchored via a glycolipid tail. In BW5147, 47% of the Thy-1 molecules had phospholipase-C-sensitive anchors attached after a 1.5 min labelling and, with longer pulses, this percentage rose to 76%. Tunicamycin did not block the addition of glycolipid anchors, and glycolipid attachment also occurred at 21 degrees C. The findings suggest that the attachment of glycolipid anchors occurs in the rough endoplasmic reticulum.

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“…Most materials and methods were as described in previous papers [4,5] or as detailed in legends to tables. Acetylcholinesterase activity was measured by a modification of the method of Ellman et al [8].…”

Section: Methodsmentioning

confidence: 99%

“…As these enzymes are generally considered to have their active sites at the outer surface of the plasma membrane it would be expected that not only would release occur from the outer surface but also that the membrane phosphatidylinositol involved in their binding, would be located here as well. However, many of the previous experiments were done with tissue slices where accessibility of the phospholipase C to the cell surface might have been restricted and under conditions where substantial cell lysis, as judged by the release of lactate dehydrogenase, appeared to have occurred [6]. These technical limitations have precluded a definitive location of the essential molecular events of this process at the outer surface of the plasma membrane.…”

Section: Introductionmentioning

confidence: 99%