Journal ArticleDOI
B61 is a ligand for the ECK receptor protein-tyrosine kinase
Timothy D. Bartley,Robert W. Hunt,Andrew A. Welcher,William J. Boyle,Vann P. Parker,Richard A. Lindberg,Hsieng Sen Lu,Anne Colombero,Robin Elliott,Brenda Guthrie,Paige Holst,James D. Skrine,Robert J. Toso,Ming Zhang,Elsa Fernandez,Geraldine Trail,Brian Varnum,Yosef Yarden,Tony Hunter,Gary M. Fox +19 more
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TLDR
It is reported here that recombinant B61 induces autophosphorylation of ECK in intact cells, consistent with B61 being an authentic ligand for ECK.Abstract:
A protein ligand for the ECK receptor protein-tyrosine kinase has been isolated by using the extracellular domain (ECK-X) of the receptor as an affinity reagent. Initially, concentrated cell culture supernatants were screened for receptor binding activity using immobilized ECK-X in a surface plasmon resonance detection system. Subsequently, supernatants from selected cell lines were fractionated directly by receptor affinity chromatography, resulting in the single-step purification of B61, a protein previously identified as the product of an early response gene induced by tumour necrosis factor-alpha. We report here that recombinant B61 induces autophosphorylation of ECK in intact cells, consistent with B61 being an authentic ligand for ECK. ECK is a member of a large orphan receptor protein-tyrosine kinase family headed by EPH, and we suggest that ligands for other members of this family will be related to B61, and can be isolated in the same way.read more
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Journal ArticleDOI
Osteoprotegerin Ligand Is a Cytokine that Regulates Osteoclast Differentiation and Activation
David L. Lacey,Emma Timms,Hong-Lin Tan,Michael J. Kelley,Colin R. Dunstan,Tim Burgess,Robin Elliott,Anne Colombero,Gary Elliott,S. Scully,Hailing Hsu,John K. Sullivan,Nessa Hawkins,E. Davy,C. Capparelli,Alana Eli,Yi-xin Qian,Steve Kaufman,Ildiko Sarosi,Victoria Shalhoub,Giorgio Senaldi,Jane Guo,John M. Delaney,William J. Boyle +23 more
TL;DR: The effects of OPGL are blocked in vitro and in vivo by OPG, suggesting that OPGl and OPG are key extracellular regulators of osteoclast development.
Journal ArticleDOI
GDNF–Induced Activation of the Ret Protein Tyrosine Kinase Is Mediated by GDNFR-α, a Novel Receptor for GDNF
Shuqian Jing,Duanzhi Wen,Yanbin Yu,Paige Holst,Yi Luo,Mei Fang,Rami Tamir,Laarni Antonio,Zheng Hu,Rod Cupples,Jean-Claude Louis,Sylvia Hu,Bruce W. Altrock,Gary M. Fox +13 more
TL;DR: In this paper, the expression cloning and characterization of GDNFR-α, a novel glycosylphosphatidylinositol-linked cell surface receptor for glial cell line-derived neurotrophic factor (GDNF), was reported.
Journal ArticleDOI
The ephrins and eph receptors in neural development
TL;DR: The ephrins and Eph receptors are implicated as positional labels that may guide the development of neural topographic maps, and may make a major contribution to the accurate spatial patterning of connections and cell position in the nervous system.
Journal ArticleDOI
Eph receptors and ephrins in cancer: bidirectional signalling and beyond
TL;DR: The Eph receptor tyrosine kinases and their ephrin ligands have intriguing expression patterns in cancer cells and tumour blood vessels, which suggest important roles for their bidirectional signals in many aspects of cancer development and progression.
Journal ArticleDOI
Eph Receptors and Ligands Comprise Two Major Specificity Subclasses and Are Reciprocally Compartmentalized during Embryogenesis
Nicholas W. Gale,Sacha J. Holland,David M. Valenzuela,Ann Flenniken,Li Pan,Terrence E Ryan,Mark Henkemeyer,Klaus Strebhardt,Hisamaru Hirai,David G. Wilkinson,Tony Pawson,Samuel Davis,George D. Yancopoulos +12 more
TL;DR: It is reported that the many Eph-related receptor tyrosine kinases, and their numerous membrane-bound ligands, can each be grouped into only two major specificity subclasses, revealing that the developing embryo is subdivided into domains defined by reciprocal and apparently mutually exclusive expression of a receptor subclass and its corresponding ligands.
References
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Journal ArticleDOI
cDNA cloning and characterization of eck, an epithelial cell receptor protein-tyrosine kinase in the eph/elk family of protein kinases.
Richard A. Lindberg,Tony Hunter +1 more
TL;DR: Analysis of RNA from 13 adult rat organs showed that the eck gene is expressed most highly in tissues that contain a high proportion of epithelial cells, e.g., skin, intestine, lung, and ovary, and prompted the name this protein kinase eck, for epithelial cell kinase, for protein-tyrosine kinase.