Isolation of LERK-5: A ligand of the eph-related receptor tyrosine kinases

Douglas Pat Cerretti; Tim Vanden Bos; Nicole Nelson; Carl J. Kozlosky; Pranhitha Reddy; Eugene Maraskovsky; Linda S. Park; Stewart D. Lyman; Neal G. Copeland; Debra J. Gilbert; Nancy A. Jenkins; Frederich A. Fletcher

doi:10.1016/0161-5890(95)00108-5

Isolation of LERK-5: A ligand of the eph-related receptor tyrosine kinases

Douglas Pat Cerretti, Tim Vanden Bos, Nicole Nelson, Carl J. Kozlosky, Pranhitha Reddy, Eugene Maraskovsky, Linda S. Park, Stewart D. Lyman, Neal G. Copeland, Debra J. Gilbert, Nancy A. Jenkins, Frederich A. Fletcher

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Abstract

Hek and elk are members of the eph-related family of receptor tyrosine kinases. Recently we isolated four cDNAs encoding membrane-bound ligands to hek and elk [Beckmann et al. (1994) EMBO J. 13, 3757-3762; Kozlosky et al. (1995) Oncogene 10, 299-306]. Because of the promiscuous nature of their binding, we have termed these proteins ligands of the eph-related kinases or LERKs. A search of GenBank revealed an expressed sequence tag (EST) with homololgy to the LERKs. Using this EST as a probe, we have isolated human and murine cDNAs that encode a protein which we call LERK-5. The human and murine cDNAs encode proteins of 333 and 336 amino acids, respectively, with a 97% amino acid identity; LERK-5 has an amino acid identity of 27-59% with the other reported LERKs. LERK-5 is a ligand for both elk and hek and induces receptor phosphorylation. It is expressed in adult lung and kidney and the fetal tissues heart, lung, kidney, and brain. In addition, Southern blot analysis of DNA from interspecific backcross mice indicated that LERK-5 (Eplg5) maps to the proximal region of mouse chromosome 8.

Original language	English (US)
Pages (from-to)	1197-1205
Number of pages	9
Journal	Molecular Immunology
Volume	32
Issue number	16
DOIs	https://doi.org/10.1016/0161-5890(95)00108-5
State	Published - Nov 1995

Keywords

eph-family
ligand
receptor tyrosine kinase

ASJC Scopus subject areas

Immunology
Molecular Biology

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10.1016/0161-5890(95)00108-5

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@article{69b0354a8f66474888e456f7e690b91d,

title = "Isolation of LERK-5: A ligand of the eph-related receptor tyrosine kinases",

abstract = "Hek and elk are members of the eph-related family of receptor tyrosine kinases. Recently we isolated four cDNAs encoding membrane-bound ligands to hek and elk [Beckmann et al. (1994) EMBO J. 13, 3757-3762; Kozlosky et al. (1995) Oncogene 10, 299-306]. Because of the promiscuous nature of their binding, we have termed these proteins ligands of the eph-related kinases or LERKs. A search of GenBank revealed an expressed sequence tag (EST) with homololgy to the LERKs. Using this EST as a probe, we have isolated human and murine cDNAs that encode a protein which we call LERK-5. The human and murine cDNAs encode proteins of 333 and 336 amino acids, respectively, with a 97% amino acid identity; LERK-5 has an amino acid identity of 27-59% with the other reported LERKs. LERK-5 is a ligand for both elk and hek and induces receptor phosphorylation. It is expressed in adult lung and kidney and the fetal tissues heart, lung, kidney, and brain. In addition, Southern blot analysis of DNA from interspecific backcross mice indicated that LERK-5 (Eplg5) maps to the proximal region of mouse chromosome 8.",

keywords = "eph-family, ligand, receptor tyrosine kinase",

author = "Cerretti, {Douglas Pat} and Bos, {Tim Vanden} and Nicole Nelson and Kozlosky, {Carl J.} and Pranhitha Reddy and Eugene Maraskovsky and Park, {Linda S.} and Lyman, {Stewart D.} and Copeland, {Neal G.} and Gilbert, {Debra J.} and Jenkins, {Nancy A.} and Fletcher, {Frederich A.}",

note = "Funding Information: Acknowledgements-We thank Marty Timour and Mary Barn-stead for excellent technical assistance and Anne Bannister, Kathy Anderson and Doug Williams for critical review of the manuscript. Part of this work was supported by the National Cancer Institute, DHHS, under contract NOl-CO-46000 with ABL (N. G. Copeland, D. J. Gilbert and N. A. Jenkins).",

year = "1995",

month = nov,

doi = "10.1016/0161-5890(95)00108-5",

language = "English (US)",

volume = "32",

pages = "1197--1205",

journal = "Molecular Immunology",

issn = "0161-5890",

publisher = "Elsevier Limited",

number = "16",

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TY - JOUR

T1 - Isolation of LERK-5

T2 - A ligand of the eph-related receptor tyrosine kinases

AU - Cerretti, Douglas Pat

AU - Bos, Tim Vanden

AU - Nelson, Nicole

AU - Kozlosky, Carl J.

AU - Reddy, Pranhitha

AU - Maraskovsky, Eugene

AU - Park, Linda S.

AU - Lyman, Stewart D.

AU - Copeland, Neal G.

AU - Gilbert, Debra J.

AU - Jenkins, Nancy A.

AU - Fletcher, Frederich A.

N1 - Funding Information: Acknowledgements-We thank Marty Timour and Mary Barn-stead for excellent technical assistance and Anne Bannister, Kathy Anderson and Doug Williams for critical review of the manuscript. Part of this work was supported by the National Cancer Institute, DHHS, under contract NOl-CO-46000 with ABL (N. G. Copeland, D. J. Gilbert and N. A. Jenkins).

PY - 1995/11

Y1 - 1995/11

N2 - Hek and elk are members of the eph-related family of receptor tyrosine kinases. Recently we isolated four cDNAs encoding membrane-bound ligands to hek and elk [Beckmann et al. (1994) EMBO J. 13, 3757-3762; Kozlosky et al. (1995) Oncogene 10, 299-306]. Because of the promiscuous nature of their binding, we have termed these proteins ligands of the eph-related kinases or LERKs. A search of GenBank revealed an expressed sequence tag (EST) with homololgy to the LERKs. Using this EST as a probe, we have isolated human and murine cDNAs that encode a protein which we call LERK-5. The human and murine cDNAs encode proteins of 333 and 336 amino acids, respectively, with a 97% amino acid identity; LERK-5 has an amino acid identity of 27-59% with the other reported LERKs. LERK-5 is a ligand for both elk and hek and induces receptor phosphorylation. It is expressed in adult lung and kidney and the fetal tissues heart, lung, kidney, and brain. In addition, Southern blot analysis of DNA from interspecific backcross mice indicated that LERK-5 (Eplg5) maps to the proximal region of mouse chromosome 8.

AB - Hek and elk are members of the eph-related family of receptor tyrosine kinases. Recently we isolated four cDNAs encoding membrane-bound ligands to hek and elk [Beckmann et al. (1994) EMBO J. 13, 3757-3762; Kozlosky et al. (1995) Oncogene 10, 299-306]. Because of the promiscuous nature of their binding, we have termed these proteins ligands of the eph-related kinases or LERKs. A search of GenBank revealed an expressed sequence tag (EST) with homololgy to the LERKs. Using this EST as a probe, we have isolated human and murine cDNAs that encode a protein which we call LERK-5. The human and murine cDNAs encode proteins of 333 and 336 amino acids, respectively, with a 97% amino acid identity; LERK-5 has an amino acid identity of 27-59% with the other reported LERKs. LERK-5 is a ligand for both elk and hek and induces receptor phosphorylation. It is expressed in adult lung and kidney and the fetal tissues heart, lung, kidney, and brain. In addition, Southern blot analysis of DNA from interspecific backcross mice indicated that LERK-5 (Eplg5) maps to the proximal region of mouse chromosome 8.

KW - eph-family

KW - ligand

KW - receptor tyrosine kinase

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DO - 10.1016/0161-5890(95)00108-5

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SN - 0161-5890

VL - 32

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EP - 1205

JO - Molecular Immunology

JF - Molecular Immunology

IS - 16

ER -

Isolation of LERK-5: A ligand of the eph-related receptor tyrosine kinases

Abstract

Keywords

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