The mouse lymph node homing receptor is identical with the lymphocyte cell surface marker Ly-22: Role of the EGF domain in endothelial binding

Mark H. Siegelman; Ivan C. Cheng; Irving L. Weissman; Edward K. Wakeland

doi:10.1016/0092-8674(90)90473-R

The mouse lymph node homing receptor is identical with the lymphocyte cell surface marker Ly-22: Role of the EGF domain in endothelial binding

Mark H. Siegelman, Ivan C. Cheng, Irving L. Weissman, Edward K. Wakeland

Research output: Contribution to journal › Article › peer-review

98 Scopus citations

Abstract

The lymph node homing receptor core polypeptide (mLHR_c) is composed of a tandem collection of domains: a lectin domain, an epidermanl growth factor (EGF) domain, and two repeats common in complement regulatory proteins. Here we demonstrate localization of mLHR_c to chromosome 1, the portion syntenic with chromosome 1 in man. This locus is inseparable in mouse strains from the murine lymphocyte cell surface marker Ly-22. The data indicate that Ly-22 is an allelic determinant on the LHR resulting from a single amino acid interchange within the EGF domain. Cross-blocking experiments demonstrate that anti-Ly-22 and MEL-14 recognize independent epitopes and that Ly-22 is distinct from the carbohydrate binding region. Application of anti-Ly-22 in the in vitro binding assay shows inhibition of binding of lymphocytes to high endothelial venules (HEVs). The localization of the Ly-22 epitope in this novel chimeric protein suggests direct participation of the EGF domain in the adhesion of lymphocytes to HEV.

Original language	English (US)
Pages (from-to)	611-622
Number of pages	12
Journal	Cell
Volume	61
Issue number	4
DOIs	https://doi.org/10.1016/0092-8674(90)90473-R
State	Published - May 18 1990

ASJC Scopus subject areas

Biochemistry, Genetics and Molecular Biology(all)

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10.1016/0092-8674(90)90473-R

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title = "The mouse lymph node homing receptor is identical with the lymphocyte cell surface marker Ly-22: Role of the EGF domain in endothelial binding",

abstract = "The lymph node homing receptor core polypeptide (mLHRc) is composed of a tandem collection of domains: a lectin domain, an epidermanl growth factor (EGF) domain, and two repeats common in complement regulatory proteins. Here we demonstrate localization of mLHRc to chromosome 1, the portion syntenic with chromosome 1 in man. This locus is inseparable in mouse strains from the murine lymphocyte cell surface marker Ly-22. The data indicate that Ly-22 is an allelic determinant on the LHR resulting from a single amino acid interchange within the EGF domain. Cross-blocking experiments demonstrate that anti-Ly-22 and MEL-14 recognize independent epitopes and that Ly-22 is distinct from the carbohydrate binding region. Application of anti-Ly-22 in the in vitro binding assay shows inhibition of binding of lymphocytes to high endothelial venules (HEVs). The localization of the Ly-22 epitope in this novel chimeric protein suggests direct participation of the EGF domain in the adhesion of lymphocytes to HEV.",

author = "Siegelman, {Mark H.} and Cheng, {Ivan C.} and Weissman, {Irving L.} and Wakeland, {Edward K.}",

note = "Funding Information: This work was supported by a McDonnell Scholars Award to M. H. S., by a Bristol-Myers Cancer Research Fellowship, by the Howard Hughes Medical Institute. and in part by National Institutes of Health Grants Al09072 and CA42551 (to I. L. W.) and Al17966, GM35-978, and DK390578 (to E. K. W.).",

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doi = "10.1016/0092-8674(90)90473-R",

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AU - Weissman, Irving L.

AU - Wakeland, Edward K.

N1 - Funding Information: This work was supported by a McDonnell Scholars Award to M. H. S., by a Bristol-Myers Cancer Research Fellowship, by the Howard Hughes Medical Institute. and in part by National Institutes of Health Grants Al09072 and CA42551 (to I. L. W.) and Al17966, GM35-978, and DK390578 (to E. K. W.).

PY - 1990/5/18

Y1 - 1990/5/18

N2 - The lymph node homing receptor core polypeptide (mLHRc) is composed of a tandem collection of domains: a lectin domain, an epidermanl growth factor (EGF) domain, and two repeats common in complement regulatory proteins. Here we demonstrate localization of mLHRc to chromosome 1, the portion syntenic with chromosome 1 in man. This locus is inseparable in mouse strains from the murine lymphocyte cell surface marker Ly-22. The data indicate that Ly-22 is an allelic determinant on the LHR resulting from a single amino acid interchange within the EGF domain. Cross-blocking experiments demonstrate that anti-Ly-22 and MEL-14 recognize independent epitopes and that Ly-22 is distinct from the carbohydrate binding region. Application of anti-Ly-22 in the in vitro binding assay shows inhibition of binding of lymphocytes to high endothelial venules (HEVs). The localization of the Ly-22 epitope in this novel chimeric protein suggests direct participation of the EGF domain in the adhesion of lymphocytes to HEV.

AB - The lymph node homing receptor core polypeptide (mLHRc) is composed of a tandem collection of domains: a lectin domain, an epidermanl growth factor (EGF) domain, and two repeats common in complement regulatory proteins. Here we demonstrate localization of mLHRc to chromosome 1, the portion syntenic with chromosome 1 in man. This locus is inseparable in mouse strains from the murine lymphocyte cell surface marker Ly-22. The data indicate that Ly-22 is an allelic determinant on the LHR resulting from a single amino acid interchange within the EGF domain. Cross-blocking experiments demonstrate that anti-Ly-22 and MEL-14 recognize independent epitopes and that Ly-22 is distinct from the carbohydrate binding region. Application of anti-Ly-22 in the in vitro binding assay shows inhibition of binding of lymphocytes to high endothelial venules (HEVs). The localization of the Ly-22 epitope in this novel chimeric protein suggests direct participation of the EGF domain in the adhesion of lymphocytes to HEV.

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The mouse lymph node homing receptor is identical with the lymphocyte cell surface marker Ly-22: Role of the EGF domain in endothelial binding

Abstract

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