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A Proliferation-inducing Ligand (April)) also known as TNSF13A, Tall-2, and TRDL-1, is a member of the TNF ligand (TNFL) superfamily. April is most similar to B-cell activation factor (BAFF) with which it shares 30% sequence identity, compete for two receptors, TACI and BCMA. APRIL is expressed at low levels in lymphoid tissue and is over-expressed by a number of tumors. April has a proliferative effect on both normal and tumor cell lines in vitro and in vivo. APRIL seems to be involved in the regulation of death and proliferation of tumor cells, but there are still contradictory findings regarding its overall biological effects.

A Proliferation-inducing Ligand (April)) also known as TNSF13A, Tall-2, and TRDL-1, is a member of the TNF ligand (TNFL) superfamily. April is most similar to B-cell activation factor (BAFF) with which it shares 30% sequence identity, compete for two receptors, TACI and BCMA. APRIL is expressed at low levels in lymphoid tissue and is over-expressed by a number of tumors. April has a proliferative effect on both normal and tumor cell lines in vitro and in vivo. APRIL seems to be involved in the regulation of death and proliferation of tumor cells, but there are still contradictory findings regarding its overall biological effects.

A Proliferation-inducing Ligand (April)) also known as TNSF13A, Tall-2, and TRDL-1, is a member of the TNF ligand (TNFL) superfamily. April is most similar to B-cell activation factor (BAFF) with which it shares 30% sequence identity, compete for two receptors, TACI and BCMA. APRIL is expressed at low levels in lymphoid tissue and is over-expressed by a number of tumors. April has a proliferative effect on both normal and tumor cell lines in vitro and in vivo. APRIL seems to be involved in the regulation of death and proliferation of tumor cells, but there are still contradictory findings regarding its overall biological effects.

B7-1/CD80 and B7-2/CD86, together with their receptors CD28 and CTLA-4, constitute one of the dominant co-stimulatory pathways that regulate T- and B-cell responses. Although both CTLA-4 and CD28 can bind to the same ligands, CTLA-4 binds to B7-1 and B7-2 with a 20-100 fold higher affinity than CD28 and is involved in the down-regulation of the immune response. Mature human B7-1 consists of a 208 amino acid extracellular domain (ECD) with two immunoglobulin-like domains, a 21 amino acid transmembrane domain, and a 25 amino acid cytoplasmic domain. Both human and mouse B7-1 and B7-2 can bind to either human or mouse CD28 and sCTLA-4. B7-1 is expressed on activated B cells, activated T cells, and macrophages. B7-2 is constitutively expressed on interdigitating dendritic cells, Langerhans cells, peripheral blood dendritic cells, memory B cells, and germinal center B cells.

B7-1/CD80 and B7-2/CD86, together with their receptors CD28 and CTLA-4, constitute one of the dominant co-stimulatory pathways that regulate T- and B-cell responses. Although both CTLA-4 and CD28 can bind to the same ligands, CTLA-4 binds to B7-1 and B7-2 with a 20-100 fold higher affinity than CD28 and is involved in the down-regulation of the immune response. Mature human B7-1 consists of a 208 amino acid extracellular domain (ECD) with two immunoglobulin-like domains, a 21 amino acid transmembrane domain, and a 25 amino acid cytoplasmic domain. Both human and mouse B7-1 and B7-2 can bind to either human or mouse CD28 and sCTLA-4. B7-1 is expressed on activated B cells, activated T cells, and macrophages. B7-2 is constitutively expressed on interdigitating dendritic cells, Langerhans cells, peripheral blood dendritic cells, memory B cells, and germinal center B cells.

B7-1/CD80 and B7-2/CD86, together with their receptors CD28 and CTLA-4, constitute one of the dominant co-stimulatory pathways that regulate T- and B-cell responses. Although both CTLA-4 and CD28 can bind to the same ligands, CTLA-4 binds to B7-1 and B7-2 with a 20-100 fold higher affinity than CD28 and is involved in the down-regulation of the immune response. Mature human B7-1 consists of a 208 amino acid extracellular domain (ECD) with two immunoglobulin-like domains, a 21 amino acid transmembrane domain, and a 25 amino acid cytoplasmic domain. Both human and mouse B7-1 and B7-2 can bind to either human or mouse CD28 and sCTLA-4. B7-1 is expressed on activated B cells, activated T cells, and macrophages. B7-2 is constitutively expressed on interdigitating dendritic cells, Langerhans cells, peripheral blood dendritic cells, memory B cells, and germinal center B cells.

BAFF Receptor (BAFF-R), a member of the TNFR superfamily, is highly expressed in spleen, lymph node, and resting B cells and to some extent in activated B cells, resting CD4+ cells and peripheral blood leukocytes. BAFF-R is a type III transmembrane protein that binds with high specificity to BAFF (TNFSF13B). BAFF-R/BAFF signaling plays a critical role in B cell survival and maturation.

BAFF Receptor (BAFF-R), a member of the TNFR superfamily, is highly expressed in spleen, lymph node, and resting B cells and to some extent in activated B cells, resting CD4+ cells and peripheral blood leukocytes. BAFF-R is a type III transmembrane protein that binds with high specificity to BAFF (TNFSF13B). BAFF-R/BAFF signaling plays a critical role in B cell survival and maturation.

B-cell activating factor, also known as BAFF, TALL-1, TNAK, and zTNF4, is a member of theTNF ligand superfamily designated TNFSF13B. Produced by macrophages, dendritic cells, and T lymphocytes, BAFF promotes the survival of B cells and is essential for B cell maturation. BAFF binds to three TNF receptor superfamily members: B-cell maturation antigen (BCMA/TNFRSF17), transmembrane activator and calcium-modulator and cyclophilin ligand interactor (TACI/TNFRSF13B) and BAFF receptor (BAFF R/BR3/TNFRSF 13C). These receptors are type III transmembrane proteins lacking a signal peptide. Whereas TACI and BCMA bind BAFF and another TNF superfamily ligand, APRIL(a proliferation-inducing ligand), BAFF R selectively binds BAFF. The BAFF R extracellular domain lacks the TNF receptor canonical cysteine-rich domain (CRD) and contains only a partial CRD with four cysteine residues. Human and mouse BAFF R share 56% aa sequence identity. BAFF R is highly expressed in spleen, lymph node and resting B cells. It is also expressed at lower levels in activated B cell, resting CD4+ T cells, thymus and peripheral blood leukocytes.

B-cell activating factor, also known as BAFF, TALL-1, TNAK, and zTNF4, is a member of theTNF ligand superfamily designated TNFSF13B. Produced by macrophages, dendritic cells, and T lymphocytes, BAFF promotes the survival of B cells and is essential for B cell maturation. BAFF binds to three TNF receptor superfamily members: B-cell maturation antigen (BCMA/TNFRSF17), transmembrane activator and calcium-modulator and cyclophilin ligand interactor (TACI/TNFRSF13B) and BAFF receptor (BAFF R/BR3/TNFRSF 13C). These receptors are type III transmembrane proteins lacking a signal peptide. Whereas TACI and BCMA bind BAFF and another TNF superfamily ligand, APRIL(a proliferation-inducing ligand), BAFF R selectively binds BAFF. The BAFF R extracellular domain lacks the TNF receptor canonical cysteine-rich domain (CRD) and contains only a partial CRD with four cysteine residues. Human and mouse BAFF R share 56% aa sequence identity. BAFF R is highly expressed in spleen, lymph node and resting B cells. It is also expressed at lower levels in activated B cell, resting CD4+ T cells, thymus and peripheral blood leukocytes.

B-cell activating factor, also known as BAFF, TALL-1, TNAK, and zTNF4, is a member of theTNF ligand superfamily designated TNFSF13B. Produced by macrophages, dendritic cells, and T lymphocytes, BAFF promotes the survival of B cells and is essential for B cell maturation. BAFF binds to three TNF receptor superfamily members: B-cell maturation antigen (BCMA/TNFRSF17), transmembrane activator and calcium-modulator and cyclophilin ligand interactor (TACI/TNFRSF13B) and BAFF receptor (BAFF R/BR3/TNFRSF 13C). These receptors are type III transmembrane proteins lacking a signal peptide. Whereas TACI and BCMA bind BAFF and another TNF superfamily ligand, APRIL(a proliferation-inducing ligand), BAFF R selectively binds BAFF. The BAFF R extracellular domain lacks the TNF receptor canonical cysteine-rich domain (CRD) and contains only a partial CRD with four cysteine residues. Human and mouse BAFF R share 56% aa sequence identity. BAFF R is highly expressed in spleen, lymph node and resting B cells. It is also expressed at lower levels in activated B cell, resting CD4+ T cells, thymus and peripheral blood leukocytes.

CXCL13, also known as B-lymphocyte chemoattractant (BLC), is a CXC chemokine that is constitutively expressed in secondary lymphoid organs. BCA-1 cDNA encodes a protein of 109 amino acid residues with a leader sequence of 22 residues. Mature human BCA-1 shares 64% amino acid sequence similarity with the mouse protein and 23 – 34% amino acid sequence identity with other known CXC chemokines. Recombinant or chemically synthesized BCA-1 is a potent chemoattractant for B lymphocytes but not T lymphocytes, monocytes or neutrophils. BLR1, a G protein-coupled receptor originally isolated from Burkitt’s lymphoma cells, has now been shown to be the specific receptor for BCA-1. Among cells of the hematopoietic lineages, the expression of BLR1, now designated CXCR5, is restricted to B lymphocytes and a subpopulation of T helper memory cells. Mice lacking BLR1 have been shown to lack inguinal lymph nodes. These mice were also found to have impaired development of Peyer’s patches and defective formation of primary follicles and germinal centers in the spleen as a result of the inability of B lymphocytes to migrate into B cell areas.

CXCL13, also known as B-lymphocyte chemoattractant (BLC), is a CXC chemokine that is constitutively expressed in secondary lymphoid organs. BCA-1 cDNA encodes a protein of 109 amino acid residues with a leader sequence of 22 residues. Mature human BCA-1 shares 64% amino acid sequence similarity with the mouse protein and 23 – 34% amino acid sequence identity with other known CXC chemokines. Recombinant or chemically synthesized BCA-1 is a potent chemoattractant for B lymphocytes but not T lymphocytes, monocytes or neutrophils. BLR1, a G protein-coupled receptor originally isolated from Burkitt’s lymphoma cells, has now been shown to be the specific receptor for BCA-1. Among cells of the hematopoietic lineages, the expression of BLR1, now designated CXCR5, is restricted to B lymphocytes and a subpopulation of T helper memory cells. Mice lacking BLR1 have been shown to lack inguinal lymph nodes. These mice were also found to have impaired development of Peyer’s patches and defective formation of primary follicles and germinal centers in the spleen as a result of the inability of B lymphocytes to migrate into B cell areas.

Defensins (alpha and beta) are cationic peptides with a broad spectrum of antimicrobial activity that comprise an important arm of the innate immune system. The α-defensins are distinguished from the β-defensins by the pairing of their three disulfide bonds. To date, four human β-defensins have been identified; BD-1, BD-2, BD-3 and BD-4. β-defensins are expressed on some leukocytes and at epithelial surfaces. In addition to their direct antimicrobial activities, they are chemoattractant towards immature dendritic cells and memory T cells. The β-defensin proteins are expressed as the C-terminal portion of precursors and are released by proteolytic cleavage of a signal sequence and, in the case of BD-1 (36 a.a.), a propeptide region. β-defensins contain a six-cysteine motif that forms three intra-molecular disulfide bonds. β-Defensins are 3-5 kDa peptides ranging in size from 33-47 amino acid residues.

Defensins (alpha and beta) are cationic peptides with a broad spectrum of antimicrobial activity that comprise an important arm of the innate immune system. The α-defensins are distinguished from the β-defensins by the pairing of their three disulfide bonds. To date, four human β-defensins have been identified; BD-1, BD-2, BD-3 and BD-4. β-defensins are expressed on some leukocytes and at epithelial surfaces. In addition to their direct antimicrobial activities, they are chemoattractant towards immature dendritic cells and memory T cells. The β-defensin proteins are expressed as the C-terminal portion of precursors and are released by proteolytic cleavage of a signal sequence and, in the case of BD-1 (36 a.a.), a propeptide region. β-defensins contain a six-cysteine motif that forms three intra-molecular disulfide bonds. β-Defensins are 3-5 kDa peptides ranging in size from 33-47 amino acid residues.

Defensins (alpha and beta) are cationic peptides with a broad spectrum of antimicrobial activity that comprise an important arm of the innate immune system. The α-defensins are distinguished from the β-defensins by the pairing of their three disulfide bonds. To date, four human β-defensins have been identified; BD-1, BD-2, BD-3 and BD-4. β-defensins are expressed on some leukocytes and at epithelial surfaces. In addition to their direct antimicrobial activities, they are chemoattractant towards immature dendritic cells and memory T cells. The β-defensin proteins are expressed as the C-terminal portion of precursors and are released by proteolytic cleavage of a signal sequence and, in the case of BD-1 (36 a.a.), a propeptide region. β-defensins contain a six-cysteine motif that forms three intra-molecular disulfide bonds. β-Defensins are 3-5 kDa peptides ranging in size from 33-47 amino acid residues.

Defensins (alpha and beta) are cationic peptides with a broad spectrum of antimicrobial activity that comprise an important arm of the innate immune system. The α-defensins are distinguished from the β-defensins by the pairing of their three disulfide bonds. To date, four human β-defensins have been identified; BD-1, BD-2, BD-3 and BD-4. β-defensins are expressed on some leukocytes and at epithelial surfaces. In addition to their direct antimicrobial activities, they are chemoattractant towards immature dendritic cells and memory T cells. The β-defensin proteins are expressed as the C-terminal portion of precursors and are released by proteolytic cleavage of a signal sequence and, in the case of BD-1 (36 a.a.), a propeptide region. β-defensins contain a six-cysteine motif that forms three intra-molecular disulfide bonds. β-Defensins are 3-5 kDa peptides ranging in size from 33-47 amino acid residues.