Association of an integral membrane protein with glucose transport and with anion transport

1984 ◽  
Vol 67 (1) ◽  
pp. 45-62
Author(s):  
M.R. Banyard ◽  
M.K. White
Keyword(s):  
Monoclonal Antibody ◽  
Membrane Protein ◽  
Cell Surface ◽  
Glucose Transport ◽  
Integral Membrane Protein ◽  
Anion Transport ◽  
Covalent Attachment ◽  
Cell Surface Glycoprotein ◽  
A Cell ◽  
Cytoplasmic Determinant

A monoclonal antibody that recognizes a cell-surface glycoprotein associated with glucose transport was reported previously. Additional information about the function and intracellular distribution of the antigen recognized by this antibody is presented. The monoclonal antibody recognizes a cell-surface and a cytoplasmic determinant. The density of the cell-surface determinant is heterogeneous within the cell population. The subpopulation of cells that carry the cell-surface determinant at high density correspond with a subset of cells that incorporate 2-deoxy-D-[3H]glucose more rapidly than the population as a whole. The monoclonal antibody is used, with cell-affinity chromatography, to isolate this subset of cells. The cytoplasmic determinant, to which the antibody binds, is associated with the cytoplasmic microfilaments but the antibody is not absorbed by actin. The cell-surface and cytoplasmic components are not identical since the apparent affinity of the antibody for each site is different. The portion of the antigen in the membrane behaves as an integral membrane protein while the remainder is tightly associated with the detergent-insoluble cytoskeleton. The expression of the antigen on the cell surface is modified by covalent attachment of an inhibitor of anion transport, 4,4′-diisothiocyano-2,2′-disulphonic stilbene. The possible interaction of the anion/lactate transporter with the glucose transporter is discussed.

scholarly journals ERM family members as molecular linkers between the cell surface glycoprotein CD44 and actin-based cytoskeletons.

1994 ◽  
Vol 126 (2) ◽  
pp. 391-401 ◽  
Author(s):  
S Tsukita ◽  
K Oishi ◽  
N Sato ◽  
J Sagara ◽  
A Kawai ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Cell Surface ◽  
Plasma Membranes ◽  
Immunofluorescence Microscopy ◽  
Family Members ◽  
Integral Membrane Protein ◽  
Surface Glycoprotein ◽  
Cell Surface Glycoprotein ◽  
Bhk Cells ◽  
Triton X

The ERM family members, ezrin, radixin, and moesin, localizing just beneath the plasma membranes, are thought to be involved in the actin filament/plasma membrane association. To identify the integral membrane protein directly associated with ERM family members, we performed immunoprecipitation studies using antimoesin mAb and cultured baby hamster kidney (BHK) cells metabolically labeled with [35S]methionine or surface-labeled with biotin. The results indicated that moesin is directly associated with a 140-kD integral membrane protein. Using BHK cells as antigens, we obtained a mAb that recognized the 140-kD membrane protein. We next cloned a cDNA encoding the 140-kD membrane protein and identified it as CD44, a broadly distributed cell surface glycoprotein. Immunoprecipitation with various anti-CD44 mAbs showed that ezrin and radixin, as well as moesin, are associated with CD44, not only in BHK cells, but also in mouse L fibroblasts. Furthermore, immunofluorescence microscopy revealed that in both BHK and L cells, the Triton X-100-insoluble CD44 is precisely colocalized with ERM family members. We concluded that ERM family members work as molecular linkers between the cytoplasmic domain of CD44 and actin-based cytoskeletons.

Cloning of the gene encoding TROP-2, a cell-surface glycoprotein expressed by human carcinomas

1995 ◽  
Vol 62 (5) ◽  
pp. 610-618 ◽  
Author(s):  
Mara Fornaro ◽  
Roberta Dell' Arciprete ◽  
Manuela Stella ◽  
Cecilia Bucci ◽  
Michele Nutini ◽  
...  
Keyword(s):  
Cell Surface ◽  
Surface Glycoprotein ◽  
Gene Encoding ◽  
Cell Surface Glycoprotein ◽  
Human Carcinomas ◽  
A Cell

Expression of a surface epitope on cells that link branches in the tracheal network of Manduca sexta

Development ◽  
1990 ◽  
Vol 110 (3) ◽  
pp. 681-688 ◽  
Author(s):  
J.B. Nardi
Keyword(s):  
Monoclonal Antibody ◽  
Cell Surface ◽  
Manduca Sexta ◽  
Abdominal Segment ◽  
Western Blots ◽  
Tracheal Epithelial Cells ◽  
A Cell ◽  
Tracheal Epithelial ◽  
Thoracic And Abdominal ◽  
Small Subpopulation

A monoclonal antibody (MAb 2F5) to a cell surface epitope labels a small subpopulation of tracheal epithelial cells in each thoracic and abdominal segment of Manduca. These cells (nodes) represent the sites within the tracheal network at which invaginating tracheal tubes join during embryonic establishment of the tracheal network. Tracheal nodes are also the sites at which tracheal cuticle fractures during each molt. Since tracheal cuticle is shed through each spiracle, a tracheal node lies between each pair of contralateral spiracles within a segment (commissural node) and between each pair of adjacent, ipsilateral spiracles (lateral longitudinal node). MAb 2F5 first labels presumptive nodal cells of tracheal epithelium immediately prior to the linking of epithelial tubes from successive and opposite spiracles. One cell at the tip of each invaginating tracheal branch labels with MAb 2F5. The highly localized expression of the cell surface epitope recognized by MAb 2F5 may be instrumental in the orderly coupling of tracheal branches during embryonic development. On the basis of immunolabeling of Western blots and tissues, MAb 2F5 is believed to recognize Manduca fasciclin II, a member of a class of molecules involved in cell adhesion/recognition.

scholarly journals A monoclonal antibody identifying a cell surface antigen shared by common acute lymphoblastic leukemias and B lineage cells

Blood ◽  
1980 ◽  
Vol 56 (6) ◽  
pp. 1141-1144 ◽  
Author(s):  
MF Greaves ◽  
W Verbi ◽  
J Kemshead ◽  
R Kennett
Keyword(s):  
Monoclonal Antibody ◽  
B Cells ◽  
Cell Surface ◽  
Lymphoblastic Leukemia ◽  
Blast Crisis ◽  
Fetal Brain ◽  
Lymphocytic Leukemia ◽  
Cell Surface Antigens ◽  
A Cell ◽  
B Lineage

Abstract A monoclonal antibody designated PI153/3, which reacts with neuroblastoma and fetal brain, is shown to identify also a cell surface determinant shared by pre-B and mature B cells and their corresponding leukemias including chronic lymphocytic leukemia, non-Hodgkin's lymphoma, B acute lymphoblastic leukemia, and hairy cell leukemia, but not plasmacytoma. Almost all non-T, non-B acute “lymphoid” leukemias bind PI153/3. The latter includes 71 of 74 common ALL tested, most but not all “unclassified” or “null” ALL and cases of both acute undifferentiated leukemia and Ph1 positive chronic myeloid leukemia in blast crisis with common ALL phenotypes. The antigen is absent or present at very low density on normal and leukemic T lymphocyte, myeloid and erythroid cells. The determinant appears to co-redistribute with cell surface immunoglobulin in B lymphocytes and segregates independently of other cell surface antigens associated with B cells and/or cALL including HLA-DR (Ia-like antigens) and the cALL (gp 100) antigen.

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