Molecular cloning and expression of Pgp-1. The mouse homology of the human H-CAM (Hermes) lymphocyte homing receptor

D. F H Zhou, J. F. Ding, Louis Picker, R. F. Bargatze, E. C. Butcher, D. V. Goeddel

Research output: Contribution to journalArticle

92 Citations (Scopus)

Abstract

Mouse phagocytic glycoprotein-1 (Pgp-1; Ly-24) is a 95-kDa glycoprotein of unknown function that has served as an important T cell/leukocyte differentiation marker. Recent work has suggested that it may be related to a human 85- to 95-kDa glycoprotein (termed variously the Hermes Ag/lymphocyte homing receptor, ECMRIII, P80, and CD44) that is involved in lymphocyte binding to high endothelial venules in the process of lymphocyte homing, and has been implicated in other cell adhesion events. The widespread expression of this molecular class in diverse organ systems suggests a broad role in cellular adhesion, and has led to the unifying designating homing-cellular adhesion molecule (H-CAM). By using human H-CAM cDNA probes, we have isolated a full-length cDNA for the mouse homolog. Comparison of the human and mouse sequences reveals that an N-terminal domain homologous to cartilage proteoglycan core and link proteins, as well as the C-terminal transmembrane and cytoplasmic sequences, are highly conserved (89% and 86% identity, respectively). In contrast, a proximal extracellular domain thought to serve as a target for O-glycosylation and chondroitin sulfate attachment has undergone substantial divergence (only 42% identity). Transient expression of the cDNA in CHO cells followed by immunologic staining confirms that this mouse H-CAM cDNA encodes Pgp-1.1, one of two known Pgp-1 alloantigens.

Original languageEnglish (US)
Pages (from-to)3390-3395
Number of pages6
JournalJournal of Immunology
Volume143
Issue number10
StatePublished - 1989
Externally publishedYes

Fingerprint

Lymphocyte Homing Receptors
Molecular Cloning
Complementary DNA
Glycoproteins
Lymphocytes
Isoantigens
Venules
CHO Cells
Chondroitin Sulfates
Conserved Sequence
Differentiation Antigens
Proteoglycans
Glycosylation
Cell Adhesion
Cartilage
Cell Differentiation
Leukocytes
Staining and Labeling
T-Lymphocytes

ASJC Scopus subject areas

  • Immunology

Cite this

Zhou, D. F. H., Ding, J. F., Picker, L., Bargatze, R. F., Butcher, E. C., & Goeddel, D. V. (1989). Molecular cloning and expression of Pgp-1. The mouse homology of the human H-CAM (Hermes) lymphocyte homing receptor. Journal of Immunology, 143(10), 3390-3395.

Molecular cloning and expression of Pgp-1. The mouse homology of the human H-CAM (Hermes) lymphocyte homing receptor. / Zhou, D. F H; Ding, J. F.; Picker, Louis; Bargatze, R. F.; Butcher, E. C.; Goeddel, D. V.

In: Journal of Immunology, Vol. 143, No. 10, 1989, p. 3390-3395.

Research output: Contribution to journalArticle

Zhou, DFH, Ding, JF, Picker, L, Bargatze, RF, Butcher, EC & Goeddel, DV 1989, 'Molecular cloning and expression of Pgp-1. The mouse homology of the human H-CAM (Hermes) lymphocyte homing receptor', Journal of Immunology, vol. 143, no. 10, pp. 3390-3395.
Zhou, D. F H ; Ding, J. F. ; Picker, Louis ; Bargatze, R. F. ; Butcher, E. C. ; Goeddel, D. V. / Molecular cloning and expression of Pgp-1. The mouse homology of the human H-CAM (Hermes) lymphocyte homing receptor. In: Journal of Immunology. 1989 ; Vol. 143, No. 10. pp. 3390-3395.
@article{85a164ed4922464fab249df9a5b0772f,
title = "Molecular cloning and expression of Pgp-1. The mouse homology of the human H-CAM (Hermes) lymphocyte homing receptor",
abstract = "Mouse phagocytic glycoprotein-1 (Pgp-1; Ly-24) is a 95-kDa glycoprotein of unknown function that has served as an important T cell/leukocyte differentiation marker. Recent work has suggested that it may be related to a human 85- to 95-kDa glycoprotein (termed variously the Hermes Ag/lymphocyte homing receptor, ECMRIII, P80, and CD44) that is involved in lymphocyte binding to high endothelial venules in the process of lymphocyte homing, and has been implicated in other cell adhesion events. The widespread expression of this molecular class in diverse organ systems suggests a broad role in cellular adhesion, and has led to the unifying designating homing-cellular adhesion molecule (H-CAM). By using human H-CAM cDNA probes, we have isolated a full-length cDNA for the mouse homolog. Comparison of the human and mouse sequences reveals that an N-terminal domain homologous to cartilage proteoglycan core and link proteins, as well as the C-terminal transmembrane and cytoplasmic sequences, are highly conserved (89{\%} and 86{\%} identity, respectively). In contrast, a proximal extracellular domain thought to serve as a target for O-glycosylation and chondroitin sulfate attachment has undergone substantial divergence (only 42{\%} identity). Transient expression of the cDNA in CHO cells followed by immunologic staining confirms that this mouse H-CAM cDNA encodes Pgp-1.1, one of two known Pgp-1 alloantigens.",
author = "Zhou, {D. F H} and Ding, {J. F.} and Louis Picker and Bargatze, {R. F.} and Butcher, {E. C.} and Goeddel, {D. V.}",
year = "1989",
language = "English (US)",
volume = "143",
pages = "3390--3395",
journal = "Journal of Immunology",
issn = "0022-1767",
publisher = "American Association of Immunologists",
number = "10",

}

TY - JOUR

T1 - Molecular cloning and expression of Pgp-1. The mouse homology of the human H-CAM (Hermes) lymphocyte homing receptor

AU - Zhou, D. F H

AU - Ding, J. F.

AU - Picker, Louis

AU - Bargatze, R. F.

AU - Butcher, E. C.

AU - Goeddel, D. V.

PY - 1989

Y1 - 1989

N2 - Mouse phagocytic glycoprotein-1 (Pgp-1; Ly-24) is a 95-kDa glycoprotein of unknown function that has served as an important T cell/leukocyte differentiation marker. Recent work has suggested that it may be related to a human 85- to 95-kDa glycoprotein (termed variously the Hermes Ag/lymphocyte homing receptor, ECMRIII, P80, and CD44) that is involved in lymphocyte binding to high endothelial venules in the process of lymphocyte homing, and has been implicated in other cell adhesion events. The widespread expression of this molecular class in diverse organ systems suggests a broad role in cellular adhesion, and has led to the unifying designating homing-cellular adhesion molecule (H-CAM). By using human H-CAM cDNA probes, we have isolated a full-length cDNA for the mouse homolog. Comparison of the human and mouse sequences reveals that an N-terminal domain homologous to cartilage proteoglycan core and link proteins, as well as the C-terminal transmembrane and cytoplasmic sequences, are highly conserved (89% and 86% identity, respectively). In contrast, a proximal extracellular domain thought to serve as a target for O-glycosylation and chondroitin sulfate attachment has undergone substantial divergence (only 42% identity). Transient expression of the cDNA in CHO cells followed by immunologic staining confirms that this mouse H-CAM cDNA encodes Pgp-1.1, one of two known Pgp-1 alloantigens.

AB - Mouse phagocytic glycoprotein-1 (Pgp-1; Ly-24) is a 95-kDa glycoprotein of unknown function that has served as an important T cell/leukocyte differentiation marker. Recent work has suggested that it may be related to a human 85- to 95-kDa glycoprotein (termed variously the Hermes Ag/lymphocyte homing receptor, ECMRIII, P80, and CD44) that is involved in lymphocyte binding to high endothelial venules in the process of lymphocyte homing, and has been implicated in other cell adhesion events. The widespread expression of this molecular class in diverse organ systems suggests a broad role in cellular adhesion, and has led to the unifying designating homing-cellular adhesion molecule (H-CAM). By using human H-CAM cDNA probes, we have isolated a full-length cDNA for the mouse homolog. Comparison of the human and mouse sequences reveals that an N-terminal domain homologous to cartilage proteoglycan core and link proteins, as well as the C-terminal transmembrane and cytoplasmic sequences, are highly conserved (89% and 86% identity, respectively). In contrast, a proximal extracellular domain thought to serve as a target for O-glycosylation and chondroitin sulfate attachment has undergone substantial divergence (only 42% identity). Transient expression of the cDNA in CHO cells followed by immunologic staining confirms that this mouse H-CAM cDNA encodes Pgp-1.1, one of two known Pgp-1 alloantigens.

UR - http://www.scopus.com/inward/record.url?scp=0024398743&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0024398743&partnerID=8YFLogxK

M3 - Article

C2 - 2681416

AN - SCOPUS:0024398743

VL - 143

SP - 3390

EP - 3395

JO - Journal of Immunology

JF - Journal of Immunology

SN - 0022-1767

IS - 10

ER -