Localization of an arginine‐specific mono‐ADP‐ribosyltransferase in skeletal muscle sarcolemma and transverse tubules

Klebl, Bert; Matsushita, Shigeki; Pette, Dirk

doi:10.1016/0014-5793(94)80586-5

Cited by 8 publications

(3 citation statements)

References 35 publications

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“…Other mono(ADP-ribosyl)transferases, including rat cardiac-muscle membrane mono(ADP-ribosyl)transferase [13] and the enzyme from the cell surface of cultured mouse skeletal-muscle cells [14], can be released by hydrolysis of the GPI anchor with PI-PLC. In contrast, an arginine-specific mono(ADP-ribosyl)transferase found in skeletal-muscle sarcolemma has an activity which is predominantly orientated towards the cytoplasm [15].…”

Section: Introductionmentioning

confidence: 91%

Arginine-specific mono(ADP-ribosyl)transferase activity on the surface of human polymorphonuclear neutrophil leucocytes

Donnelly

Rendell

Murray

et al. 1996

Biochemical Journal

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An Arg-specific mono(ADP-ribosyl)transferase activity on the surface of human polymorphonuclear neutrophil leucocytes (PMNs) was confirmed by the use of diethylamino-(benzylidineamino)guanidine (DEA-BAG) as an ADP-ribose acceptor. Two separate HPLC systems were used to separate ADP-ribosyl-DEA-BAG from reaction mixtures, and its presence was confirmed by electrospray mass spectrometry. ADP-ribosyl-DEA-BAG was produced in the presence of PMNs, but not in their absence. Incubation of DEA-BAG with ADP-ribose (0.1-10 mM) did not yield ADP-ribosyl-DEA-BAG, which indicates that ADP-ribosyl-DEA-BAG formed in the presence of PMNs was not simply a product of a reaction between DEA-BAG and free ADP-ribose, due possibly to the hydrolysis of NAD+ by an NAD+ glycohydrolase. The assay of mono(ADP-ribosyl)transferase with agmatine as a substrate was modified for intact PMNs, and the activity was found to be approx. 50-fold lower than that in rabbit cardiac membranes. The Km of the enzyme for NAD+ was 100.1 30.4 microM and the Vmax 1.4 0.2 pmol of ADP-ribosylagmatine/h per 10(6) cells. The enzyme is likely to be linked to the cell surface via a glycosylphosphatidylinositol anchor, since incubation of intact PMNs with phosphoinositol-specific phospholipase C (PI-PLC) led to a 98% decrease in mono(ADP-ribosyl)transferase activity in the cells. Cell surface proteins were labelled after exposure of intact PMNs to [32P]NAD+. Their molecular masses were 79, 67, 46, 36 and 26 kDa. The time course for labelling was non-linear under these conditions over a period of 4 h. The labelled products were identified as mono(ADP-ribosyl)ated proteins by hydrolysis with snake venom phosphodiesterase to yield 5'-AMP.

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Section: Introductionmentioning

confidence: 91%

Arginine-specific mono(ADP-ribosyl)transferase activity on the surface of human polymorphonuclear neutrophil leucocytes

Donnelly

Rendell

Murray

et al. 1996

Biochemical Journal

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“…T-cadherin Is ADP-ribosylated by an Endogenous Transferase in the T-CAV Fraction-An ADP-monoribosyltransferase has been identified in skeletal muscle sarcolemma (30,31) and has been proposed to be GPI-linked and to ribosylate the adhesion protein integrin-␣7 in this tissue (32). RNA hybridization analysis indicated that an mRNA with a similar molecular size is present in heart (30).…”

Section: Fig 3 the 120-and 100-kda Proteins React With Anti-t-cadhementioning

confidence: 99%

T-cadherin Is a Major Glycophosphoinositol-anchored Protein Associated with Noncaveolar Detergent-insoluble Domains of the Cardiac Sarcolemma

Doyle¹,

Goings²,

Upshaw-Earley³

et al. 1998

Journal of Biological Chemistry

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Sucrose-density flotation analysis of Triton-insoluble membrane domains isolated from highly purified sheep ventricular sarcolemma revealed the presence of two major 120- and 100-kDa proteins. Both species migrated in two-dimensional isoelectric focussing/SDS gels with an apparent pI of approximately 4.3, suggesting that they might be related. Microsequence analysis of peptides derived from the 100-kDa protein yielded amino acid sequences with high homology to T-cadherin, a truncated cadherin lacking a cytoplasmic domain. The similarity was confirmed using antibodies to chicken T-cadherin that reacted with both proteins on immunoblots. T-cadherin was released from the detergent-insoluble sarcolemmal fraction by phospholipase C treatment indicating that it is linked to the membrane by a glycophosphoinositol anchor. T-cadherin could be ADP-ribosylated by a transferase that was also present in the caveolin-enriched Triton-insoluble fraction. T-cadherin-containing membrane fragments cofractionated on sucrose gradients with caveolin-3, a marker protein for myocyte caveolae. However, immunopurified caveolin-3-containing membranes contained no associated T-cadherin. Immunocytochemical analysis of cultured rat atrial myocytes revealed that T-cadherin and caveolin have related but nonoverlapping staining patterns. These results suggest that T-cadherin is a major glycophosphoinositol-linked protein in cardiac myocytes and that it may be located in plasma membrane "rafts" distinct from but possibly adjacent to caveolae.

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“…ϩ also leads to labeling of serveral protein bands (50,51). In the canine system, the intracellular G␣ subunit of the G s protein regulating adenylate cyclase was identified as the most efficient target for arginine-linked ADPribosylation (51).…”

Section: P]nadmentioning

confidence: 99%

Mouse T Cell Membrane Proteins Rt6−1 and Rt6−2 Are Arginine/Protein Mono(ADPribosyl)transferases and Share Secondary Structure Motifs with ADP-ribosylating Bacterial Toxins

Koch-Nolte

Petersen

Balasubramanian

et al. 1996

Journal of Biological Chemistry

122

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Mono ADP-ribosylation is a posttranslational protein modification that has been implicated in the regulation of key biological functions in bacteria as well as in animals. Recently, the first cDNAs for eucaryotic mono-(ADPribosyl)transferases were cloned and found to exhibit significant sequence similarity only to one other known protein, the T cell differentiation antigen Rt6. In this paper we describe secondary structure analyses of Rt6 and related proteins and show conserved structure motifs and amino acid residues consistent with a common ancestry of these eucaryotic proteins and bacterial ADP-ribosyltransferases. Moreover, we have expressed soluble mouse Rt6 -1 and Rt6 -2 gene products in which C-terminal tags (FLAG-His 6 ) replace the native glycosylphosphatidylinositol anchor signal sequences. Purified recombinant Rt6 -2, but not Rt6 -1, shows NAD ؉ glycohydrolase activity, which is inhibited by the arginine analogue agmatine. Immunoprecipitation of recombinant Rt6 -1 and Rt6 -2 with anti-FLAG M2 antibody followed by incubation with [ P]NAD؉ leads to rapid and covalent incorporation of radioactivity into the light chain of the M2 antibody. The bound label is resistant to treatment with HgCl 2 but sensitive to NH 2 OH, characteristic of arginine-linked ADP-ribosylation. These results demonstrate that Rt6 -1 and Rt6 -2 possess the enzymatic activities typical for NAD ؉ -dependent arginine/ protein mono(ADPribosyl)transferases (EC 2.4.2.31). They are the first such enzymes to be molecularly characterized in the immune system.

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Localization of an arginine‐specific mono‐ADP‐ribosyltransferase in skeletal muscle sarcolemma and transverse tubules

Cited by 8 publications

References 35 publications

Arginine-specific mono(ADP-ribosyl)transferase activity on the surface of human polymorphonuclear neutrophil leucocytes

Arginine-specific mono(ADP-ribosyl)transferase activity on the surface of human polymorphonuclear neutrophil leucocytes

T-cadherin Is a Major Glycophosphoinositol-anchored Protein Associated with Noncaveolar Detergent-insoluble Domains of the Cardiac Sarcolemma

Mouse T Cell Membrane Proteins Rt6−1 and Rt6−2 Are Arginine/Protein Mono(ADPribosyl)transferases and Share Secondary Structure Motifs with ADP-ribosylating Bacterial Toxins

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