Cloning and Characterization of HB2, a Candidate High Density Lipoprotein Receptor

Matsumoto, Akiyo; Mitchell, Amy M.; Kurata, Hiroyuki; Pyle, Louise E.; Kondo, Kazuo; Itakura, Hiroshige; Fidge, Noel

doi:10.1074/jbc.272.27.16778

Cited by 56 publications

(27 citation statements)

References 23 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…At least two other HDLbinding proteins, HB-2/ALCAM and SR-BI, have been reported to be extensively glycosylated, having approximately 55-66 kDa deglycosylated forms (3,14). Gp96/ GRP94 is less extensively glycosylated with only 1-2 kDa of glycosylation.…”

Section: Rt-pcr Analyses Of Known Hdl-binding Proteins In Various Tismentioning

confidence: 98%

Characterization of a 95 kDa High Affinity Human High Density Lipoprotein-Binding Protein

et al. 2001

View full text Add to dashboard Cite

A new human 95 kDa high density lipoprotein (HDL)-binding protein (HBP) corresponding to a high affinity HDL-binding site with K(d) = 1.67 microg/mL and a capacity of 13.4 ng/mg was identified in human fetal hepatocytes. The HDL binding with the 95 kDa HBP plateaus at 2.5-5 microg/mL under reducing and nonreducing conditions. The association of HDL(3) with the 95 kDa HBP plateaued in 15-30 min while dissociation was complete in 30 min. HDL(3), apoA-I, and apoA-II were recognized by the 95 kDa HBP while low density lipoproteins (LDL) and tetranitromethane-modified HDL were not. The 95 kDa HBP predominantly resides on the surface of cells since trypsin treatment of HepG2 cells eliminated nearly 70% of HDL binding. All studied human cells and cell lines (HepG2, Caco-2, HeLa, fibroblasts, SKOV-3, PA-I) demonstrated the presence of the 95 kDa protein. Both RT-PCR and Western blotting for HB-2/ALCAM were negative in human fetal hepatocytes while Gp96/GRP94 was clearly differentiated from the 95 kDa HBP by two-dimensional electrophoretic mobility. Moreover, deglycosylation of HepG2 membrane preparations did not affect either HDL binding to the 95 kDa HBP or its size, while in contrast it affected the molecular weights of HB-2/ALCAM and SR-BI/CLA-1. We conclude that the 95 kDa HBP is a new HDL receptor candidate widely expressed in human cells and cell lines.

show abstract

Section: Rt-pcr Analyses Of Known Hdl-binding Proteins In Various Tismentioning

confidence: 98%

Characterization of a 95 kDa High Affinity Human High Density Lipoprotein-Binding Protein

et al. 2001

View full text Add to dashboard Cite

show abstract

“…Other potential apo receptor candidates are HBP (vigilin) (28) and HB 2 (29), recently reviewed by Fidge (30). Both annexin I and annexin VII also can bind apoAI in vitro in a calcium-dependent fashion (31), and although these may play a role in this pathway, their expression in RAW264 cells did not depend on cAMP treatment.…”

Section: Discussionmentioning

confidence: 99%

Cholesterol efflux to apolipoprotein AI involves endocytosis and resecretion in a calcium-dependent pathway

Takahashi

Smith

1999

Proc. Natl. Acad. Sci. U.S.A.

224

171

View full text Add to dashboard Cite

We previously have described the cAMPmediated induction of cholesterol and phospholipid eff lux from the murine macrophage RAW264 cell line to lipid-free apolipoprotein acceptors. This induction of cholesterol eff lux is associated with increased binding and association of apolipoprotein to the cells. In the present study, using primarily apolipoprotein AI (apoAI) as the acceptor, cAMP-dependent cholesterol eff lux to apolipoprotein acceptors was associated with apoAI binding to coated pits, cellular uptake, and resecretion. After cell association and washing, 58% of the apoAI was resecreted during a 90-min chase period. In addition, after apoAI uptake and washing, cholesterol eff lux was observed during a chase period without additional acceptors. Cholesterol eff lux was partially blocked by chlorpromazine and hypertonic media, two inhibitors of coated pit endocytosis. Cholesterol eff lux to apoAI was found to depend on extracellular calcium. By temporally separating the cAMP induction phase from the apoAI chase phase, calcium was found to be required during the apoAI chase phase rather than during the cAMP induction period. In the absence of calcium the 8-Br-cAMP-mediated induction of apoAI binding was maintained, but the specific apoAI cellular association was inhibited. The data are consistent with a model for cholesterol eff lux to apolipoproteins that involves a calcium-dependent endocytic pathway, followed by recycling and the subsequent release of the nascent lipoprotein particle from the cell.

show abstract

“…It has over 90% homology with the chicken adhesion molecule BEN/SC1/DM-GRASP (3)(4)(5), and it has 30% identity and 50% similarity with the human melanoma cell adhesion molecule Mel-CAM/MUC18/CD146 (6). Furthermore, ALCAM has 93% sequence identity with the candidate liver high density lipoprotein receptor HB2 (7). ALCAM is involved in various physiological processes including hematopoiesis (8,9), thymus development (10), the immune response (11), neurite extension (12), neural cell migration (13), and osteogenesis (14).…”

mentioning

confidence: 97%

Molecular Basis for the Homophilic Activated Leukocyte Cell Adhesion Molecule (ALCAM)-ALCAM Interaction

Kempen¹,

Nelissen²,

Degen³

et al. 2001

Journal of Biological Chemistry

145

143

View full text Add to dashboard Cite

Activated leukocyte cell adhesion molecule (ALCAM/ CD166), a member of the immunoglobulin superfamily with five extracellular immunoglobulin-like domains, facilitates heterophilic (ALCAM-CD6) and homophilic (ALCAM-ALCAM) cell-cell interactions. While expressed in a wide variety of tissues and cells, ALCAM is restricted to subsets of cells usually involved in dynamic growth and/or migration processes. A structure-function analysis, using two monoclonal anti-ALCAM antibodies and a series of amino-terminally deleted ALCAM constructs, revealed that homophilic cell adhesion depended on ligand binding mediated by the membranedistal amino-terminal immunoglobulin domain and on avidity controlled by ALCAM clustering at the cell surface involving membrane-proximal immunoglobulin domains. Co-expression of a transmembrane ALCAM deletion mutant, which lacks the ligand binding domain, and endogenous wild-type ALCAM inhibited homophilic cell-cell interactions by interference with ALCAM avidity, while homophilic, soluble ligand binding remained unaltered. The extracellular structures of ALCAM thus provide two structurally and functionally distinguishable modules, one involved in ligand binding and the other in avidity. Functionality of both modules is required for stable homophilic ALCAM-ALCAM cell-cell adhesion.Adhesion molecules play an important role in development, leukocyte function, and homeostasis in multicellular organisms, which are mainly governed by inter-and intracellular communication via cell-cell interactions. Alterations in cellular adhesion and communication can contribute to uncontrolled cell growth (1) and life-threatening syndromes like leukocyte adhesion deficiency (2). Activation of adhesion molecules generally involves both modulation of affinity and avidity. The affinity of adhesion molecules often reflects a specific conformation of the extracellular ligand-binding domain. Avidity modulation involves changes in the cell surface distribution of adhesion molecules (e.g. lateral oligomerization), which leads to clusters of molecules and thereby specifically increases the number of available receptors at the site of cell-cell interaction.Activated leukocyte cell adhesion molecule (ALCAM/MEMD/ CD166) 1 is a type I transmembrane protein and a member of the Ig superfamily. It has over 90% homology with the chicken adhesion molecule BEN/SC1/DM-GRASP (3-5), and it has 30% identity and 50% similarity with the human melanoma cell adhesion molecule Mel-CAM/MUC18/CD146 (6). Furthermore, ALCAM has 93% sequence identity with the candidate liver high density lipoprotein receptor HB2 (7). ALCAM is involved in various physiological processes including hematopoiesis (8, 9), thymus development (10), the immune response (11), neurite extension (12), neural cell migration (13), and osteogenesis (14).ALCAM has a short cytoplasmic tail and its extracellular part comprises five Ig domains: two amino-terminal variable (V) type Ig domains followed by three constant (C) type Ig domains (V 1 V 2 C 1 C 2 C 3 ). ALCAM was first ident...

show abstract

Cloning and Characterization of HB2, a Candidate High Density Lipoprotein Receptor

Cited by 56 publications

References 23 publications

Characterization of a 95 kDa High Affinity Human High Density Lipoprotein-Binding Protein

Characterization of a 95 kDa High Affinity Human High Density Lipoprotein-Binding Protein

Cholesterol efflux to apolipoprotein AI involves endocytosis and resecretion in a calcium-dependent pathway

Molecular Basis for the Homophilic Activated Leukocyte Cell Adhesion Molecule (ALCAM)-ALCAM Interaction

Contact Info

Product

Resources

About