cDNA cloning of the B cell membrane protein CD22: a mediator of B-B cell interactions.

We have cloned a full-length cDNA for the B cell membrane protein CD22, which is referred to as B lymphocyte cell adhesion molecule (BL-CAM). Using subtractive hybridization techniques, several B lymphocyte-specific cDNAs were isolated. Northern blot analysis with one of the clones, clone 66, revealed expression in normal activated B cells and a variety of B cell lines, but not in normal activated T cells, T cell lines, Hela cells, or several tissues, including brain and placenta. One major transcript of approximately 3.3 kb was found in B cells although several smaller transcripts were also present in low amounts (approximately 2.6, 2.3, and 1.6 kb). Sequence analysis of a full-length cDNA clone revealed an open reading frame of 2,541 bases coding for a predicted protein of 847 amino acids with a molecular mass of 95 kD. The BL-CAM cDNA is nearly identical to a recently isolated cDNA clone for CD22, with the exception of an additional 531 bases in the coding region of BL-CAM. BL-CAM has a predicted transmembrane spanning region and a 140-amino acid intracytoplasmic domain. Search of the National Biological Research Foundation protein database revealed that this protein is a member of the immunoglobulin super family and that it had significant homology with three homotypic cell adhesion proteins: carcinoembryonic antigen (29% identity over 460 amino acids), myelin-associated glycoprotein (27% identity over 425 amino acids), and neural cell adhesion molecule (21.5% over 274 amino acids). Northern blot analysis revealed low-level BL-CAM mRNA expression in unactivated tonsillar B cells, which was rapidly increased after B cell activation with Staphylococcus aureus Cowan strain 1 and phorbol myristate acetate, but not by various cytokines, including interleukin 4 (IL-4), IL-6, and gamma interferon. In situ hybridization with an antisense BL-CAM RNA probe revealed expression in B cell-rich areas in tonsil and lymph node, although the most striking hybridization was in the germinal centers. COS cells transfected with a BL-CAM expression vector were immunofluorescently stained positively with two different CD22 antibodies, each of which recognizes a different epitope. Additionally, both normal tonsil B cells and a B cell line were found to adhere to COS transfected with BL-CAM in the sense but not the antisense direction.(ABSTRACT TRUNCATED AT 400 WORDS)

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Homing of Human B Cells to Lymphoid Organs and B-Cell Lymphoma Engraftment Are Controlled by Cell Adhesion Molecule JAM-C

Cancer Research ◽

10.1158/0008-5472.can-12-1756 ◽

2012 ◽

Vol 73 (2) ◽

pp. 640-651 ◽

Cited By ~ 16

Author(s):

Carmen Doñate ◽

Christiane Ody ◽

Thomas McKee ◽

Sylvie Ruault-Jungblut ◽

Nicolas Fischer ◽

...

Keyword(s):

Cell Adhesion ◽

B Cells ◽

B Cell ◽

Adhesion Molecule ◽

Cell Adhesion Molecule ◽

Cell Lymphoma ◽

B Cell Lymphoma ◽

Lymphoid Organs ◽

Human B Cells

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Constitutive alternative NF-κB signaling promotes marginal zone B-cell development but disrupts the marginal sinus and induces HEV-like structures in the spleen

Blood ◽

10.1182/blood-2007-02-075143 ◽

2007 ◽

Vol 110 (7) ◽

pp. 2381-2389 ◽

Cited By ~ 38

Author(s):

Feng Guo ◽

Debra Weih ◽

Elke Meier ◽

Falk Weih

Keyword(s):

Cell Adhesion ◽

B Cells ◽

B Cell ◽

Adhesion Molecule ◽

Cell Adhesion Molecule ◽

Marginal Zone ◽

Cell Development ◽

B Cell Development ◽

Marginal Sinus ◽

Cell Adhesion Molecule 1

Nuclear factor-κB (NF-κB) plays a crucial role in B-cell and lymphoid organ development. Here, we studied the consequences of constitutive, signal-independent activation of the alternative NF-κB pathway for the splenic marginal zone (MZ). In contrast to nfkb2−/− mice, which lack both p100 and p52, mice that lack only the inhibitory p100 precursor but still express the p52 subunit of NF-κB2 (p100−/−) had markedly elevated MZ B-cell numbers. Both cell-intrinsic mechanisms and increased stromal expression of vascular cell adhesion molecule-1 (VCAM-1) contributed to the accumulation of MZ B cells in p100−/− spleens. While migration of p100−/− MZ B cells toward the lysophospholipid sphingosine-1 phosphate (S1P) was not affected, CXCL13-stimulated chemotaxis was impaired, correlating with reduced migration of MZ B cells into follicles in response to lipopolysaccharide (LPS). Strikingly, p100 deficiency resulted in the absence of a normal marginal sinus, strongly induced expression of mucosal addressin cell adhesion molecule-1 (MAdCAM-1) and glycosylated cell adhesion molecule-1 (GlyCAM-1), and the formation of nonfunctional ectopic high endothelial venule (HEV)–like structures in the red pulp. Thus, constitutive activation of the alternative NF-κB pathway favors MZ B-cell development and accumulation but leads to a disorganized spleen microarchitecture.

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Conditional Vascular Cell Adhesion Molecule 1 Deletion in Mice

Journal of Experimental Medicine ◽

10.1084/jem.193.6.741 ◽

2001 ◽

Vol 193 (6) ◽

pp. 741-754 ◽

Cited By ~ 343

Author(s):

Pandelakis A. Koni ◽

Sunil K. Joshi ◽

Ulla-Angela Temann ◽

Dian Olson ◽

Linda Burkly ◽

...

Keyword(s):

T Cells ◽

Cell Adhesion ◽

B Cells ◽

B Cell ◽

Adhesion Molecule ◽

Cell Adhesion Molecule ◽

Vascular Cell Adhesion ◽

Vascular Cell ◽

Cell Numbers ◽

Deficient Mice

We generated vascular cell adhesion molecule (VCAM)-1 “knock-in” mice and Cre recombinase transgenic mice to delete the VCAM-1 gene (vcam-1) in whole mice, thereby overcoming the embryonic lethality seen with conventional vcam-1–deficient mice. vcam-1 knock-in mice expressed normal levels of VCAM-1 but showed loss of VCAM-1 on endothelial and hematopoietic cells when interbred with a “TIE2Cre” transgene. Analysis of peripheral blood from conditional vcam-1–deficient mice revealed mild leukocytosis, including elevated immature B cell numbers. Conversely, the bone marrow (BM) had reduced immature B cell numbers, but normal numbers of pro-B cells. vcam-1–deficient mice also had reduced mature IgD+ B and T cells in BM and a greatly reduced capacity to support short-term migration of transferred B cells, CD4+ T cells, CD8+ T cells, and preactivated CD4+ T cells to the BM. Thus, we report an until now unappreciated dominant role for VCAM-1 in lymphocyte homing to BM.

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A shortened variant of red cell membrane protein 4.1

Blood ◽

10.1182/blood.v60.1.265.265 ◽

1982 ◽

Vol 60 (1) ◽

pp. 265-267 ◽

Cited By ~ 11

Author(s):

N Alloisio ◽

E Dorleac ◽

J Delaunay ◽

R Girot ◽

C Galand ◽

...

Keyword(s):

Amino Acids ◽

Cell Membrane ◽

Membrane Protein ◽

Phosphorylation Site ◽

Red Cell ◽

Heterozygous State ◽

Red Cell Membrane ◽

Protein 4.1 ◽

Protein 4.2 ◽

Cell Membrane Protein

Abstract In a healthy 32-yr-old woman with normal red cell morphology, a shortened variant of cytoskeletal membrane protein 4.1 is described at the heterozygous state. One haploid set of protein 4.1 migrates below protein 4.2 and displays a reduction in mass of approximately 8500 with regard to the normal haploid set. The shortening corresponds to a deletion of about 75 amino acids and concerns both subcomponents a and b of protein 4.1. It seems to involve some phosphorylation site(s). It was transmitted to the proposita's son (who inherited elliptocytosis with band 4.1 deficiency from his father). To our knowledge, the present abnormality is the first unequivocal variant of erythrocyte membrane protein 4.1 recognized up to now.

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Identification of a T Cell Membrane Protein Possibly Involved in IL-4-Induced B Cell Immunoglobulin Class Switching to IgE

Cellular Immunology ◽

10.1006/cimm.1994.1036 ◽

1994 ◽

Vol 153 (2) ◽

pp. 378-391

Author(s):

Sho Matsushita ◽

David H. Katz

Keyword(s):

T Cell ◽

Cell Membrane ◽

Membrane Protein ◽

B Cell ◽

Class Switching ◽

Immunoglobulin Class ◽

Immunoglobulin Class Switching ◽

Cell Membrane Protein ◽

T Cell Membrane

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A shortened variant of red cell membrane protein 4.1

Blood ◽

10.1182/blood.v60.1.265.bloodjournal601265 ◽

1982 ◽

Vol 60 (1) ◽

pp. 265-267

Author(s):

N Alloisio ◽

E Dorleac ◽

J Delaunay ◽

R Girot ◽

C Galand ◽

...

Keyword(s):

Amino Acids ◽

Cell Membrane ◽

Membrane Protein ◽

Phosphorylation Site ◽

Red Cell ◽

Heterozygous State ◽

Red Cell Membrane ◽

Protein 4.1 ◽

Protein 4.2 ◽

Cell Membrane Protein

In a healthy 32-yr-old woman with normal red cell morphology, a shortened variant of cytoskeletal membrane protein 4.1 is described at the heterozygous state. One haploid set of protein 4.1 migrates below protein 4.2 and displays a reduction in mass of approximately 8500 with regard to the normal haploid set. The shortening corresponds to a deletion of about 75 amino acids and concerns both subcomponents a and b of protein 4.1. It seems to involve some phosphorylation site(s). It was transmitted to the proposita's son (who inherited elliptocytosis with band 4.1 deficiency from his father). To our knowledge, the present abnormality is the first unequivocal variant of erythrocyte membrane protein 4.1 recognized up to now.

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