NAD glycohydrolases and the metabolism of cyclic ADP-ribose

Unifying mechanism for Aplysia ADP-ribosyl cyclase and CD38/NAD+ glycohydrolases

“…When using intermediate amounts of enzyme (50 munits ; Figure 1A) the substrate was essentially transformed into cADP-ribose and only limited amounts of ADP-ribose were measured (less than 10 % of the reaction products under these experimental conditions). This is in agreement with several authors who have also observed the limited contribution of a hydrolytic activity to the overall reaction [3,22,23]. However, with higher amounts of cyclase, the situation was quite different ( Figure 1B) ; in this case, after a transient formation cADPribose declined with the concomitant formation of ADP-ribose, indicative of a hydrolytic step via either NAD + glycohydrolase or cADP-ribose hydrolase pathways, or by a combination of both.…”

Unifying mechanism for Aplysia ADP-ribosyl cyclase and CD38/NAD+ glycohydrolases

“…When using intermediate amounts of enzyme (50 munits ; Figure 1A) the substrate was essentially transformed into cADP-ribose and only limited amounts of ADP-ribose were measured (less than 10 % of the reaction products under these experimental conditions). This is in agreement with several authors who have also observed the limited contribution of a hydrolytic activity to the overall reaction [3,22,23]. However, with higher amounts of cyclase, the situation was quite different ( Figure 1B) ; in this case, after a transient formation cADPribose declined with the concomitant formation of ADP-ribose, indicative of a hydrolytic step via either NAD + glycohydrolase or cADP-ribose hydrolase pathways, or by a combination of both.…”

Isolation of hematopoietic stem cells and the effect of CD38 expression during the early erythroid progenitor cell development process

“…NAD + glycohydrolase is usually found partially in cell and partially in nucleus (24). CD38 has also been determined in erythrocytes, the liver, pancreas, brain, muscle cells, plasma cells, monocyte/macrophages and HSCs (24)(25).…”

The NAD-glycohydrolase (nga) gene ofStreptococcus pyogenes

“…Eukaryotic NAD‐glycohydrolases are able to synthesize cyclic ADP‐ribose (cADPR) from NAD [2,3]. Furthermore, most of these enzymes are bifunctional and can catalyze both synthesis and hydrolysis of cADPR [4,5]. Cyclic ADP‐ribose belongs to a family of regulatory molecules and is known to function in cellular calcium signaling [5–9].…”

“…Furthermore, most of these enzymes are bifunctional and can catalyze both synthesis and hydrolysis of cADPR [4,5]. Cyclic ADP‐ribose belongs to a family of regulatory molecules and is known to function in cellular calcium signaling [5–9]. Activation of surface receptors of several types of eukaryotic cells results in an increased concentration of intracellular cADPR which leads to an increased concentration of intracellular Ca 2+ .…”

Unifying mechanism for Aplysia ADP-ribosyl cyclase and CD38/NAD+ glycohydrolases

“…When using intermediate amounts of enzyme (50 munits ; Figure 1A) the substrate was essentially transformed into cADP-ribose and only limited amounts of ADP-ribose were measured (less than 10 % of the reaction products under these experimental conditions). This is in agreement with several authors who have also observed the limited contribution of a hydrolytic activity to the overall reaction [3,22,23]. However, with higher amounts of cyclase, the situation was quite different ( Figure 1B) ; in this case, after a transient formation cADPribose declined with the concomitant formation of ADP-ribose, indicative of a hydrolytic step via either NAD + glycohydrolase or cADP-ribose hydrolase pathways, or by a combination of both.…”

Isolation of hematopoietic stem cells and the effect of CD38 expression during the early erythroid progenitor cell development process

“…NAD + glycohydrolase is usually found partially in cell and partially in nucleus (24). CD38 has also been determined in erythrocytes, the liver, pancreas, brain, muscle cells, plasma cells, monocyte/macrophages and HSCs (24)(25).…”

The NAD-glycohydrolase (nga) gene ofStreptococcus pyogenes

“…Eukaryotic NAD‐glycohydrolases are able to synthesize cyclic ADP‐ribose (cADPR) from NAD [2,3]. Furthermore, most of these enzymes are bifunctional and can catalyze both synthesis and hydrolysis of cADPR [4,5]. Cyclic ADP‐ribose belongs to a family of regulatory molecules and is known to function in cellular calcium signaling [5–9].…”

“…Furthermore, most of these enzymes are bifunctional and can catalyze both synthesis and hydrolysis of cADPR [4,5]. Cyclic ADP‐ribose belongs to a family of regulatory molecules and is known to function in cellular calcium signaling [5–9]. Activation of surface receptors of several types of eukaryotic cells results in an increased concentration of intracellular cADPR which leads to an increased concentration of intracellular Ca 2+ .…”

Unifying mechanism for Aplysia ADP-ribosyl cyclase and CD38/NAD+ glycohydrolases

“…When using intermediate amounts of enzyme (50 munits ; Figure 1A) the substrate was essentially transformed into cADP-ribose and only limited amounts of ADP-ribose were measured (less than 10 % of the reaction products under these experimental conditions). This is in agreement with several authors who have also observed the limited contribution of a hydrolytic activity to the overall reaction [3,22,23]. However, with higher amounts of cyclase, the situation was quite different ( Figure 1B) ; in this case, after a transient formation cADPribose declined with the concomitant formation of ADP-ribose, indicative of a hydrolytic step via either NAD + glycohydrolase or cADP-ribose hydrolase pathways, or by a combination of both.…”

Isolation of hematopoietic stem cells and the effect of CD38 expression during the early erythroid progenitor cell development process

“…NAD + glycohydrolase is usually found partially in cell and partially in nucleus (24). CD38 has also been determined in erythrocytes, the liver, pancreas, brain, muscle cells, plasma cells, monocyte/macrophages and HSCs (24)(25).…”

The NAD-glycohydrolase (nga) gene ofStreptococcus pyogenes

“…Eukaryotic NAD‐glycohydrolases are able to synthesize cyclic ADP‐ribose (cADPR) from NAD [2,3]. Furthermore, most of these enzymes are bifunctional and can catalyze both synthesis and hydrolysis of cADPR [4,5]. Cyclic ADP‐ribose belongs to a family of regulatory molecules and is known to function in cellular calcium signaling [5–9].…”

“…Furthermore, most of these enzymes are bifunctional and can catalyze both synthesis and hydrolysis of cADPR [4,5]. Cyclic ADP‐ribose belongs to a family of regulatory molecules and is known to function in cellular calcium signaling [5–9]. Activation of surface receptors of several types of eukaryotic cells results in an increased concentration of intracellular cADPR which leads to an increased concentration of intracellular Ca 2+ .…”