Selectin Expression
Published by Anonymous on 2007/9/27 (2035 reads)
1: Adv Exp Med Biol. 2001;491:267-78.
Transcriptional regulation of expression of carbohydrate ligands for cell adhesion molecules in the selectin family.
Kannagi R.
Program of Molecular Pathology, Aichi Cancer Center, Research Institute, Nagoya 464-8681, Japan. rkannagi@aichi-cc.pref.aichi.jp
Cell adhesion mediated by selectins and their carbohydrate ligands is involved in the adhesion of cancer cells to endothelial cells during the course of hematogenous metastasis of cancer. In patients with leukemia, this adhesion is involved in the extravascular infiltration of leukemic cells. Extravasation and tissue infiltration of malignant cells in patients with adult T-cell leukemia is mediated by the interaction of selectins and their carbohydrate ligand sialyl Lewis X, which is strongly and constitutively expressed on the leukemic cells. Constitutive expression of Lewis X in these cells is due to the transcriptional activation of Fuc-T VII, the rate-limiting enzyme in the sialyl Lewis X synthesis, induced by the Tax protein encoded by the human T-cell leukemia virus-1, the etiological virus for this leukemia. This transactivation is in clear contrast to the regulation of typical CRE-element found in various cellular genes in that it is independent of phosphorylation-dependent regulation. This must be the reason for the strong and constitutive expression of sialyl Lewis X, which exacerbates the tissue infiltration of leukemic cells. This is a good example corroborating the proposition that the abnormal expression of carbohydrate determinant at the surface of malignant cells is intimately associated with the genetic mechanism of malignant transformation of cells.
Publication Types:
Research Support, Non-U.S. Gov't
Review
PMID: 14533803 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
2: Leuk Lymphoma. 2001 Jun;42(1-2):5-12.
Impaired transendothelial migration of B-CLL lymphocytes: a defect linked to low L-selectin expression.
Gu B, Dao LP, Wiley J.
Sydney University, Department of Medicine, Nepean Hospital, Penrith, NSW 2750, Australia.
The emigration of lymphocytes from blood into lymph nodes is regulated by the expression of the adhesion molecule, L-selectin on the lymphocyte surface which arrests the rolling of the cell on the vessel wall and allows firmer adhesive interactions to develop. The expression of L-selectin on B-CLL lymphocytes is less than half that on normal lymphocytes and this difference correlates with an impaired capacity of B-CLL lymphocytes to migrate beneath a monolayer of human umbilical vein endothelial cells. Both the B-cell and T-cell lymphocytes from normal subjects and B-CLL patients show down-regulation of L-selectin and CD23 after transendothelial migration. The reduced expression of L-selectin on B-CLL lymphocytes leads to a relative "trapping" of these cells in the vascular space and is one factor contributing to the elevation of peripheral lymphocyte count.
Publication Types:
Review
PMID: 11699221 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
3: Leuk Lymphoma. 1998 Jan;28(3-4):399-404.
L-selectin expression in CD34 positive cells in chronic myeloid leukemia.
Kimura A, Kawaishi K, Sasaki A, Hyodo H, Oguma N.
Department of Hematology and Oncology, Research Institute for Radiation Biology and Medicine, Hiroshima University, Japan.
L-selectin is a cell adhesion molecule, expressed on leukocytes and involved in the regulation of leukocyte traffic. This adhesion receptor is implicated in hematopoiesis by the interaction of hematopoietic stem cells and progenitors to stroma in the bone marrow microenvironment. We found that L-selectin expression on CD34++ cells from patients with chronic myelogenous leukemia (CML) is decreased or deficient, reflecting one of the features of malignant CML progenitors. In this review, we briefly describe the structure and function of L-selectin, and its role in hematopoiesis and its expression in leukemia and lymphoma. Finally, we discuss the abnormal adhesiveness of CML progenitor cells, and the role of L-selectin in this defect.
Publication Types:
Review
PMID: 9517512 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
4: Acta Haematol. 1997;97(1-2):22-8.
Expression of an L-selectin ligand on hematopoietic progenitor cells.
Sackstein R.
Division of Bone Marrow Transplantation, H. Lee Moffitt Cancer Center and Research Institute, Tampa, FL 33612-9497, USA.
The process of hematopoiesis is dependent on discrete cell-cell and cell-matrix interactions which are tightly regulated by expression of adhesion molecules. L-selectin, an adhesion protein best known for regulating leukocyte attachment to endothelium, is characteristically expressed on the earliest hematopoietic progenitor cells. Ligands for L-selectin have been extensively characterized on endothelial cells. We recently identified a ligand for L-selectin expressed on the human hematopoietic progenitor cell line KG1a. This molecule is an integral membrane glycoprotein which is structurally different from all ligands previously described. We hypothesize that this molecule may mediate L-selectin-specific adhesive interactions during hematopoiesis. This article discusses the biology of L-selectin and its ligands, and reviews our current understanding of the structure and distribution of the L-selectin ligand expressed on hematopoietic cells.
Publication Types:
Review
PMID: 8980607 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
5: Haemostasis. 1996;26 Suppl 1:60-5.
P-selectin induction of tissue factor biosynthesis and expression.
Furie B, Furie BC.
Center for Hemostasis and Thrombosis Research, Division of Hematology-Oncology, New England Medical Center, Tufts University School of Medicine, Boston, Massachusetts 02111, USA.
P-selectin on activated platelets and stimulated endothelial cells mediates cell adhesion with monocytes and neutrophils. Since activated platelets induce tissue factor on monocytes, we examined the effect of P-selectin on this activity. Chinese hamster ovary cells expressing P-selectin stimulated tissue factor activity in purified monocytes whereas untransfected Chinese hamster ovary cells and CHO cells expressing E-selectin did not. Anti-P-selectin antibodies inhibited these effects. Incubation of CHO:P-selectin with monocytes stimulates tissue factor mRNA development and the expression of tissue factor antigen on the monocyte surface. These results indicate that P-selectin upregulates the expression of tissue factor on monocytes.
Publication Types:
Review
PMID: 8904175 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
6: Agents Actions Suppl. 1995;47:117-9.
Regulation of function and expression of P-selectin.
McEver RP.
W.K. Warren Medical Research Institute, University of Oklahoma Health Sciences Center, Oklahoma City 73104, USA.
P-selectin is an adhesion receptor for leukocytes that is expressed on activated platelets and endothelial cells. The surface expression of P-selectin is tightly regulated through signals in the cytoplasmic domain that mediate sorting into secretory granules, internalization into coated pits, and targeting to lysosomes for degradation. Like the other selectins, P-selectin binds sialylated, fucosylated carbohydrate ligands such as sialyl Lewis x. However, it binds with much higher affinity to PSGL-1, a sialomucin-like glycoprotein on myeloid cells. Binding of PSGL-1 to P-selectin may be essential for leukocytes to roll on P-selectin-expressing cells under shear forces.
Publication Types:
Review
PMID: 7540351 [PubMed - indexed for MEDLINE]
Transcriptional regulation of expression of carbohydrate ligands for cell adhesion molecules in the selectin family.
Kannagi R.
Program of Molecular Pathology, Aichi Cancer Center, Research Institute, Nagoya 464-8681, Japan. rkannagi@aichi-cc.pref.aichi.jp
Cell adhesion mediated by selectins and their carbohydrate ligands is involved in the adhesion of cancer cells to endothelial cells during the course of hematogenous metastasis of cancer. In patients with leukemia, this adhesion is involved in the extravascular infiltration of leukemic cells. Extravasation and tissue infiltration of malignant cells in patients with adult T-cell leukemia is mediated by the interaction of selectins and their carbohydrate ligand sialyl Lewis X, which is strongly and constitutively expressed on the leukemic cells. Constitutive expression of Lewis X in these cells is due to the transcriptional activation of Fuc-T VII, the rate-limiting enzyme in the sialyl Lewis X synthesis, induced by the Tax protein encoded by the human T-cell leukemia virus-1, the etiological virus for this leukemia. This transactivation is in clear contrast to the regulation of typical CRE-element found in various cellular genes in that it is independent of phosphorylation-dependent regulation. This must be the reason for the strong and constitutive expression of sialyl Lewis X, which exacerbates the tissue infiltration of leukemic cells. This is a good example corroborating the proposition that the abnormal expression of carbohydrate determinant at the surface of malignant cells is intimately associated with the genetic mechanism of malignant transformation of cells.
Publication Types:
Research Support, Non-U.S. Gov't
Review
PMID: 14533803 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
2: Leuk Lymphoma. 2001 Jun;42(1-2):5-12.
Impaired transendothelial migration of B-CLL lymphocytes: a defect linked to low L-selectin expression.
Gu B, Dao LP, Wiley J.
Sydney University, Department of Medicine, Nepean Hospital, Penrith, NSW 2750, Australia.
The emigration of lymphocytes from blood into lymph nodes is regulated by the expression of the adhesion molecule, L-selectin on the lymphocyte surface which arrests the rolling of the cell on the vessel wall and allows firmer adhesive interactions to develop. The expression of L-selectin on B-CLL lymphocytes is less than half that on normal lymphocytes and this difference correlates with an impaired capacity of B-CLL lymphocytes to migrate beneath a monolayer of human umbilical vein endothelial cells. Both the B-cell and T-cell lymphocytes from normal subjects and B-CLL patients show down-regulation of L-selectin and CD23 after transendothelial migration. The reduced expression of L-selectin on B-CLL lymphocytes leads to a relative "trapping" of these cells in the vascular space and is one factor contributing to the elevation of peripheral lymphocyte count.
Publication Types:
Review
PMID: 11699221 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
3: Leuk Lymphoma. 1998 Jan;28(3-4):399-404.
L-selectin expression in CD34 positive cells in chronic myeloid leukemia.
Kimura A, Kawaishi K, Sasaki A, Hyodo H, Oguma N.
Department of Hematology and Oncology, Research Institute for Radiation Biology and Medicine, Hiroshima University, Japan.
L-selectin is a cell adhesion molecule, expressed on leukocytes and involved in the regulation of leukocyte traffic. This adhesion receptor is implicated in hematopoiesis by the interaction of hematopoietic stem cells and progenitors to stroma in the bone marrow microenvironment. We found that L-selectin expression on CD34++ cells from patients with chronic myelogenous leukemia (CML) is decreased or deficient, reflecting one of the features of malignant CML progenitors. In this review, we briefly describe the structure and function of L-selectin, and its role in hematopoiesis and its expression in leukemia and lymphoma. Finally, we discuss the abnormal adhesiveness of CML progenitor cells, and the role of L-selectin in this defect.
Publication Types:
Review
PMID: 9517512 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
4: Acta Haematol. 1997;97(1-2):22-8.
Expression of an L-selectin ligand on hematopoietic progenitor cells.
Sackstein R.
Division of Bone Marrow Transplantation, H. Lee Moffitt Cancer Center and Research Institute, Tampa, FL 33612-9497, USA.
The process of hematopoiesis is dependent on discrete cell-cell and cell-matrix interactions which are tightly regulated by expression of adhesion molecules. L-selectin, an adhesion protein best known for regulating leukocyte attachment to endothelium, is characteristically expressed on the earliest hematopoietic progenitor cells. Ligands for L-selectin have been extensively characterized on endothelial cells. We recently identified a ligand for L-selectin expressed on the human hematopoietic progenitor cell line KG1a. This molecule is an integral membrane glycoprotein which is structurally different from all ligands previously described. We hypothesize that this molecule may mediate L-selectin-specific adhesive interactions during hematopoiesis. This article discusses the biology of L-selectin and its ligands, and reviews our current understanding of the structure and distribution of the L-selectin ligand expressed on hematopoietic cells.
Publication Types:
Review
PMID: 8980607 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
5: Haemostasis. 1996;26 Suppl 1:60-5.
P-selectin induction of tissue factor biosynthesis and expression.
Furie B, Furie BC.
Center for Hemostasis and Thrombosis Research, Division of Hematology-Oncology, New England Medical Center, Tufts University School of Medicine, Boston, Massachusetts 02111, USA.
P-selectin on activated platelets and stimulated endothelial cells mediates cell adhesion with monocytes and neutrophils. Since activated platelets induce tissue factor on monocytes, we examined the effect of P-selectin on this activity. Chinese hamster ovary cells expressing P-selectin stimulated tissue factor activity in purified monocytes whereas untransfected Chinese hamster ovary cells and CHO cells expressing E-selectin did not. Anti-P-selectin antibodies inhibited these effects. Incubation of CHO:P-selectin with monocytes stimulates tissue factor mRNA development and the expression of tissue factor antigen on the monocyte surface. These results indicate that P-selectin upregulates the expression of tissue factor on monocytes.
Publication Types:
Review
PMID: 8904175 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
6: Agents Actions Suppl. 1995;47:117-9.
Regulation of function and expression of P-selectin.
McEver RP.
W.K. Warren Medical Research Institute, University of Oklahoma Health Sciences Center, Oklahoma City 73104, USA.
P-selectin is an adhesion receptor for leukocytes that is expressed on activated platelets and endothelial cells. The surface expression of P-selectin is tightly regulated through signals in the cytoplasmic domain that mediate sorting into secretory granules, internalization into coated pits, and targeting to lysosomes for degradation. Like the other selectins, P-selectin binds sialylated, fucosylated carbohydrate ligands such as sialyl Lewis x. However, it binds with much higher affinity to PSGL-1, a sialomucin-like glycoprotein on myeloid cells. Binding of PSGL-1 to P-selectin may be essential for leukocytes to roll on P-selectin-expressing cells under shear forces.
Publication Types:
Review
PMID: 7540351 [PubMed - indexed for MEDLINE]
| Navigate through the articles | |
Selectin Structure
|
|
|
|