Primary structure of a molluscan egg-specific NADase, a second-messenger enzyme.

Glick, David L.; Hellmich, Mark R.; Beushausen, Sven; Tempst, Paul; Bayley, Hagan; Strumwasser, Felix

doi:10.1091/mbc.2.3.211

Cited by 96 publications

(44 citation statements)

References 24 publications

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“…The pooled NADase activity from this column ran as a single band on an SDS-polyacrylamide gel, whether stained by Coomassie blue (Figure 1, lane 7) or silver (not shown). After this three-column procedure, the protein was subjected to amino-acid sequencing, as described in the accompanying paper, where only a single N-terminal amino acid was observed (Glick et aL., 1991). Typically, this three-column procedure yields -1 mg of purified NADase when starting with 600 mg of total aqueous-soluble ovotestis protein, with 270/o recovery of enzyme activity.…”

Section: Resultsmentioning

confidence: 99%

Purification and characterization of a molluscan egg-specific NADase, a second-messenger enzyme.

1991

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An egg-specific NADase has been purified to homogeneity from the ovotestis of the opisthobranch mollusk Aplysia californica. Unlike other NADases, the Aplysia enzyme generates primarily cyclic-ADP-ribose (cADPR) rather than ADP-ribose from NAD. cADPR has been shown to stimulate the release of Ca2+ from microsomes prepared from sea urchin egg and, when injected into intact eggs, to activate the cortical reaction, multiple nuclear cycles, and DNA synthesis. The Aplysia enzyme was initially identified as an inhibitor of cholera and pertussis toxin-catalyzed ADP-ribosylation. By the use of an NADase assay, it was purified from the aqueous-soluble fraction of ovotestis by sequential column chromatography. The enzyme has an apparent molecular mass of 29 kDa, a Km for NAD of 0.7 mM, and a turnover rate of approximately 27,000 mol NAD.min-1.mol enzyme-1 at 30 degrees C. Monoclonal antibodies were generated to the NADase. Immunoblots of two-dimensional gels revealed multiple isoforms of the enzyme, with pls ranging from 8.1 to 9.8. The multiple isoforms were resolved with a cation exchange high-pressure liquid chromatography column and shown to generate cADPR. Immunohistochemical analysis of cryostat sections of Aplysia ovotestis shows that the enzyme is specific to the eggs and restricted to large 5- to 10-microns granules or vesicles. To date the cADPR-generating enzyme activity has been identified in various organisms, including mammals. The Aplysia enzyme is the first example in which the enzyme that generates cADPR has been purified. All of the available evidence indicates that this NADase is a second-messenger enzyme, implying that other NADases may serve a similar function.

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Section: Resultsmentioning

confidence: 99%

Purification and characterization of a molluscan egg-specific NADase, a second-messenger enzyme.

1991

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“…In 1991, a cDNA for this cyclase was cloned [54]. One year later, the similarity to human CD38 was detected by D. States et al [55].…”

Section: The Nad ϩ Connectionmentioning

confidence: 99%

The metamorphosis of a molecule: from soluble enzyme to the leukocyte receptor CD38

Ferrero

Malavasi

1999

Journal of Leukocyte Biology

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Human CD38 is a 45-kDa type II membrane glycoprotein with an intricate pattern of expression in leukocytes, although evidence is accumulating of its quite widespread expression in cells of nonvascular origin. CD38 is a member of a nascent eukaryotic gene family encoding cytosolic and membrane-bound enzymes whose substrate is NAD, a coenzyme ubiquitously distributed in nature. Functionally, CD38 is an eclectic molecule with the ability not only to catalyze but also to signal, to mobilize calcium, and to adhere to itself, to hyaluronan, and to other ligands. Interaction with CD38 on various leukocyte subpopulations has profound though diverse consequences on their life-span, but these effects seem to be independent of the enzymatic activity of the molecule. CD38 challenges our expectations of a surface molecule and we must sift through its many guises to unmask its true nature. J. Leukoc. Biol. 65: 151-161; 1999.

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“…4b). In the extracellular region, ten Cys, one Glu, one His and one Asp residues were completely conserved among Aplysia ADP ribosyl cyclase [20,21], human CD38 [22], mouse CD38 [23], rat CD38 [24], human BST-1 [l] and mouse BST-l/BP-3 [2,3] which may constitute a new family. All members of this family may physiologically contain a metal ion in a common manner, since Cys, His, Glu and Asp can readily have coordinated binding to cations.…”

Section: Enzymic Activity Of Sbst-1mentioning

confidence: 99%

ADP ribosyl cyclase activity of a novel bone marrow stromal cell surface molecule, BST‐1

Hirata¹,

Kimura²,

Sato³

et al. 1994

FEBS Letters

151

112

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Human BST-1, a bone marrow stromal cell surface molecule, is a GPI-anchored protein that facilitates the growth of pre-B cells. The deduced amino acid sequences of human and mouse BST-1 show around 30% homology with those of CD38 and Aptysia ADP ribosyl cyclase.Therefore, like CD38, BST-1 might possess ADP ribosyl cyclase activity. Here, we report the establishment of a stable transformant CHO cell line, which secretes truncated human soluble BST-1, and show that purified soluble BST-1 displays both ADP ribosyl cyclase and cADPR hydrolase activities.

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Primary structure of a molluscan egg-specific NADase, a second-messenger enzyme.

Cited by 96 publications

References 24 publications

Purification and characterization of a molluscan egg-specific NADase, a second-messenger enzyme.

Purification and characterization of a molluscan egg-specific NADase, a second-messenger enzyme.

The metamorphosis of a molecule: from soluble enzyme to the leukocyte receptor CD38

ADP ribosyl cyclase activity of a novel bone marrow stromal cell surface molecule, BST‐1

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