[26] A genetic selection for isolating cDNA clones that encode signal peptides

Ka, Jacobs; La, Collins-Racie; Colbert, Maureen; Duckett, McKeough; Evans, Clive; Golden-Fleet, Margaret; Kelleher, Kerry; Kriz, Ronald; Er, La Vallie; Merberg, David; Spaulding,; Stover, Julia; Mj, Williamson; Jm, McCoy

doi:10.1016/s0076-6879(99)03028-1

Cited by 14 publications

(24 citation statements)

References 15 publications

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“…Lymph node partial cDNAs were placed under genetic selection for signal peptides using the signal sequence trap method (3). Of a total of 333 cDNA:invertase fusion clones isolated and sequenced, one partial cDNA clone with limited sequence identity with B7-1 was identified and termed mGL50.…”

Section: Resultsmentioning

confidence: 99%

Cutting Edge: Identification of GL50, a Novel B7-Like Protein That Functionally Binds to ICOS Receptor

Ling¹,

Wu²,

Finnerty³

et al. 2000

The Journal of Immunology

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131

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By the genetic selection of mouse cDNAs encoding secreted proteins, a B7-like cDNA clone termed mouse GL50 (mGL50) was isolated encoding a 322-aa polypeptide identical with B7h. Isolation of the human ortholog of this cDNA (hGL50) revealed a coding sequence of 309 aa residues with 42% sequence identity with mGL50. Northern analysis indicated GL50 to be present in many tissues including lymphoid, embryonic yolk sac, and fetal liver samples. Of the CD28, CTLA4, and ICOS fusion constructs tested, flow cytometric analysis demonstrated only mouse ICOS-IgG binding to mGL50 cell transfectants. Subsequent phenotyping demonstrated high levels of ICOS ligand staining on splenic CD19+ B cells and low levels on CD3+ T cells. These results indicate that GL50 is a specific ligand for the ICOS receptor and suggest that the GL50-ICOS interaction functions in lymphocyte costimulation.

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Section: Resultsmentioning

confidence: 99%

Cutting Edge: Identification of GL50, a Novel B7-Like Protein That Functionally Binds to ICOS Receptor

Ling¹,

Wu²,

Finnerty³

et al. 2000

The Journal of Immunology

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223

131

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“…1) (Jacobs et al, 1997;Jacobs et al, 1999). Blast search revealed a match with clone taa05h01 (CA303262) from the hydra EST collection (http:// mpc.uci.edu/hampson/public_html/blastlif9).…”

Section: Cloning Of Hydkk1/2/4mentioning

confidence: 99%

“…Hydra in a yeast signal peptide secretion screen In order to identify growth factors and their antagonists in Hydra, we performed a signal peptide secretion screen (Jacobs et al, 1999;Klein et al, 1996). Because Marcum and Campbell (Marcum and Campbell, 1978) have shown that Hydra lacking nerve cells, nematocytes and interstitial cells develop normally, we tried to eliminate the highly abundant transcripts of this cell line.…”

Section: Identification Of a Dickkopf-related Molecule Frommentioning

confidence: 99%

An ancient Wnt-Dickkopf antagonism inHydra

et al. 2006

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The dickkopf (dkk) gene family encodes secreted antagonists of Wnt signalling proteins, which have important functions in the control of cell fate, proliferation, and cell polarity during development. Here, we report the isolation, from a regeneration-specific signal peptide screen, of a novel dickkopf gene from the fresh water cnidarian Hydra. Comparative sequence analysis demonstrates that the Wnt antagonistic subfamily Dkk1/Dkk2/Dkk4 and the non-modulating subfamily Dkk3 separated prior to the divergence of cnidarians and bilaterians. In steady-state Hydra, hydkk1/2/4-expression is inversely related to that of hywnt3a. hydkk1/2/4 is an early injury and regeneration responsive gene, and hydkk1/2/4-expressing gland cells are essential for head regeneration in Hydra, although once the head has regenerated they are excluded from it. Activation of Wnt/␤-Catenin signalling leads to the complete downregulation of hydkk1/2/4 transcripts. When overexpressed in Xenopus, HyDkk1/2/4 has similar Wnt-antagonizing activity to the Xenopus gene Dkk1. Based on the corresponding expression patterns of hydkk1/2/4 and neuronal genes, we suggest that the body column of Hydra is a neurogenic environment suppressing Wnt signalling and facilitating neurogenesis.

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“…Using this cDNA screening method, many molecules on the secretory pathway with a wide variety of functions have been efficiently isolated, for example, SDF-1 (31), ESOP-1/MD2 (32), DANCE (33), FKBP23 (34), calumenin (35), syncytin (36), and so on. We conducted a modified version of signal sequence trap screening (37) to vascular cells, and succeeded in cloning several novel transmembrane or secretory proteins. One of these, ESDN, is a novel type-I transmembrane protein, has a characteristic domain structure reminding us of neuropilins, and will be described here.…”

Section: The Nucleotide Sequence(s) Reported In This Paper Has Been Smentioning

confidence: 99%

ESDN, a Novel Neuropilin-like Membrane Protein Cloned from Vascular Cells with the Longest Secretory Signal Sequence among Eukaryotes, Is Up-regulated after Vascular Injury

Kobuke¹,

Furukawa²,

Sugai³

et al. 2001

Journal of Biological Chemistry

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A novel cDNA has been isolated from primary culture of human coronary arterial cells by a signal sequence trap method, and designated ESDN (endothelial and smooth muscle cell-derived neuropilin-like molecule). ESDN is a type-I transmembrane protein with the longest cleavable secretory signal sequence among eukaryotes. ESDN contains a CUB domain and a coagulation factor V/VIII homology domain, which reminds us of the structure of neuropilins. ESDN also harbors an LCCL domain, which is shared by Limulus factor C and Coch. Mouse and rat counterparts were also identified revealing >84% amino acid identity with human ESDN. The human ESDN gene was mapped between D3S1552 and D3S1271. Northern blot analysis showed that ESDN mRNA was expressed in various tissues; particularly highly expressed in cultured vascular smooth muscle cells. The ESDN expression was up-regulated in plateletderived growth factor-BB-stimulated vascular smooth muscle cells in vitro and neointima of the ballooninjured carotid artery in vivo. Overexpression of ESDN in 293T cells suppressed their bromodeoxyuridine uptake. In addition, ESDN protein was strongly expressed in nerve bundles in rodents. Thus, ESDN is considered to play a role in regulation of vascular cell growth and may have a wide variety of functions in other tissues including the nervous system, like neuropilins.

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[26] A genetic selection for isolating cDNA clones that encode signal peptides

Cited by 14 publications

References 15 publications

Cutting Edge: Identification of GL50, a Novel B7-Like Protein That Functionally Binds to ICOS Receptor

Cutting Edge: Identification of GL50, a Novel B7-Like Protein That Functionally Binds to ICOS Receptor

An ancient Wnt-Dickkopf antagonism inHydra

ESDN, a Novel Neuropilin-like Membrane Protein Cloned from Vascular Cells with the Longest Secretory Signal Sequence among Eukaryotes, Is Up-regulated after Vascular Injury

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