scholarly journals A common cell-type specific surface antigen in cultured human glial cells and fibroblasts: loss in malignant cells.

1976 ◽  
Vol 143 (1) ◽  
pp. 64-72 ◽  
Author(s):  
A Vaheri ◽  
E Ruoslahti ◽  
B Westermark ◽  
J Ponten
Keyword(s):  
Cell Surface ◽  
Glial Cells ◽  
Surface Antigen ◽  
Malignant Gliomas ◽  
Human Tumor ◽  
Cellular Protein ◽  
Oncogenic Viruses ◽  
Extracellular Medium ◽  
Cultured Fibroblasts ◽  
Tumor Material

Fibroblast surface antigen (SFA) is a high molecular weight protein antigen, first shown on the surface of cultured fibroblasts in fibrillar structures. It is shed to the extracellular medium and also present in the circulation (serum and plasma). Fibroblasts transformed by tumor viruses produce SFA but do not retain it on cell surface. In this report we show that SFA is also present in cultured nonestablished astroglial cells. The glial and fibroblast SFAs are immunologically indistinguishable. Glial cells (three different nonestablished lines) contain more SFA per milligram cellular protein than fibroblasts. SFA was located on cell surface in fibrillar striae that frequently extended out from the cell body. Fluorescence was also found intracellularly in the cytoplasm. Malignant gliomas (astrocytomas) established to grow in culture from human tumor material produced SFA into the growth medium but had very little (lines U-105 MG and U-343 MG) or no detectable (lines U-118 MG, U-251 MG, and U-343 MG-a) cell surface SFA. In cultures of the glioma cells many cells, in particular those that appeared to be in the telophase stage, stained strongly positive for intracellular cytoplasmic SFA. These data demonstrate that similar to fibroblasts transformed experimentally by oncogenic viruses, cells grown from naturally occurring human tumors (glioblastomas) produce SFA but lose ability to retain it on cell surface.

Isolation of Human Tumor-Associated Cell Surface Antigen-Binding scFvs

2003 ◽  
pp. 227-233
Author(s):  
Elvyra J. Noronha ◽  
Xinhui Wang ◽  
Soldano Ferrone
Keyword(s):  
Cell Surface ◽  
Surface Antigen ◽  
Human Tumor ◽  
Cell Surface Antigen ◽  
Antigen Binding

scholarly journals Immunolocalization of a novel, cytoskeleton-associated polypeptide of Mr 230,000 daltons (p230).

1983 ◽  
Vol 96 (3) ◽  
pp. 703-716 ◽  
Author(s):  
V P Lehto ◽  
I Virtanen
Keyword(s):  
Fluorescence Microscopy ◽  
Cell Surface ◽  
Intermediate Filaments ◽  
Neuroblastoma Cells ◽  
Human Kidney ◽  
Cellular Protein ◽  
Stress Fibers ◽  
Cultured Fibroblasts

Antibodies were raised against a cytoskeleton-associated, nonphosphorylated, 230,000-dalton bovine lens polypeptide (designated p230), and rendered monospecific by using a novel immunoaffinity technique. In immunofluorescence and electron microscopy of cultured fibroblasts, as well as of various other cells (endothelial, epithelial, lenticular, monocytes, neuroblastoma cells) and tissues (human kidney and liver), p230 was localized as a distinct subplasmalemmal layer in the peripheral cytoplasm of the cells. It constituted less than 0.3% of the total cellular protein in cultured fibroblasts and was not extractable with Triton X-100. In detergent-extracted cytoskeletal preparations of cultured fibroblasts, p230 remained as an elaborate peripheral network that showed a distribution distinctly different from that of the major cytoskeletal structures, stress fibers, cortical myosin, vinculin, and intermediate filaments (IF). The distribution was not dependent on the presence of intact stress fibers or microtubules, as shown by double-fluorescence microscopy of cells exposed to cytochalasin B or cultured in the presence of monensin and of cold-treated cells. Upon demecolcine-induced reorganization of intermediate filaments, however, the localization of p230 was rapidly altered to a dense plaque underneath the perinuclear aggregate of intermediate filaments. On the other hand, p230 seemed to colocalize with the detergent-resistant cell surface lamina, visualized in fluorescence microscopy with fluorochrome-coupled wheat germ agglutinin-lectin. The results suggest that p230 is part of a cell surface- and cytoskeleton-associated subplasmalemmal structure that may play an important role in cell surface-cytoskeleton interaction in various cells both in vitro and in vivo.

scholarly journals Apolipoprotein E5 (Glu212–>Lys): increased binding to cell surface proteoglycans but decreased uptake and lysosomal degradation in cultured fibroblasts.

1996 ◽  
Vol 37 (8) ◽  
pp. 1632-1645
Author(s):  
G Feussner ◽  
H Scharnagl ◽  
C Scherbaum ◽  
J Acar ◽  
J Dobmeyer ◽  
...  
Keyword(s):  
Cell Surface ◽  
Lysosomal Degradation ◽  
Cultured Fibroblasts

Cell surface antigen Thy-1

1989 ◽  
Vol 30 (4) ◽  
pp. 314-314
Author(s):  
H. -G. Rammensee
Keyword(s):  
Cell Surface ◽  
Surface Antigen ◽  
Cell Surface Antigen

scholarly journals A MOUSE B-CELL ALLOANTIGEN DETERMINED BY GENE(S) LINKED TO THE MAJOR HISTOCOMPATIBILITY COMPLEX

1973 ◽  
Vol 138 (6) ◽  
pp. 1289-1304 ◽  
Author(s):  
David H. Sachs ◽  
James L. Cone
Keyword(s):  
Major Histocompatibility Complex ◽  
Lymph Node ◽  
T Cell ◽  
B Cells ◽  
Cell Surface ◽  
B Cell ◽  
Surface Antigen ◽  
Major Histocompatibility ◽  
Spleen Cells ◽  
Histocompatibility Complex

Antibodies cytotoxic for only a subpopulation of C57Bl/10 lymph node and spleen cells were detected when rat antiserum against B10.D2 was exhaustively absorbed with B10.A lymphocytes. Antibodies of similar specificity were also detected in B10.A anti-B10.D2 and in B10.A anti-C57Bl/10 alloantisera. Reactions with recombinant strains of mice indicate that the cell-surface antigen(s) responsible for this specificity is determined by gene(s) in or to the left of the Ir-1 region of the major histocompatibility complex. A variety of criteria implicate B cells as the subpopulation of lymphocytes bearing this antigen. In view of these data and the recent report by others of a T-cell alloantigen determined by gene(s) in the major histocompatibility complex, it seems possible that there may be a variety of H-2-linked alloantigens expressed preferentially on subclasses of lymphocytes.

Direct IFNluence of interferon-γ on proliferation and cell-surface antigen expression of non-small cell lung cancer cells

Lung Cancer ◽  
2000 ◽  
Vol 30 (3) ◽  
pp. 169-174 ◽  
Author(s):  
Tokujiro Yano ◽  
Kenji Sugio ◽  
Koji Yamazaki ◽  
Shinichiro Kase ◽  
Masafumi Yamaguchi ◽  
...  
Keyword(s):  
Lung Cancer ◽  
Cell Surface ◽  
Small Cell Lung Cancer ◽  
Cancer Cells ◽  
Surface Antigen ◽  
Antigen Expression ◽  
Interferon Γ ◽  
Small Cell ◽  
Small Cell Lung ◽  
Surface Antigen Expression

Detection and Measurement of a Single Blood Cell Surface Antigen by Thermal Lens Microscopy

2000 ◽  
Vol 283 (1) ◽  
pp. 27-32 ◽  
Author(s):  
Hiroko Kimura ◽  
Fumiko Nagao ◽  
Asako Kitamura ◽  
Kazuya Sekiguchi ◽  
Takehiko Kitamori ◽  
...  
Keyword(s):  
Cell Surface ◽  
Blood Cell ◽  
Surface Antigen ◽  
Thermal Lens ◽  
Cell Surface Antigen ◽  
Thermal Lens Microscopy

scholarly journals Receptor-mediated endocytosis of alpha 2-macroglobulin in cultured fibroblasts.

1980 ◽  
Vol 28 (8) ◽  
pp. 818-823 ◽  
Author(s):  
M C Willingham ◽  
F R Maxfield ◽  
I Pastan
Keyword(s):  
Endoplasmic Reticulum ◽  
Cell Surface ◽  
Coated Pits ◽  
Cultured Fibroblasts ◽  
Receptor Mediated Endocytosis ◽  
Cytoplasmic Vesicles

Alpha 2-macroglobulin is internalized into cultured fibroblasts by receptor-mediated endocytosis. This ligand binds initially to diffusely distributed receptors on the cell surface which cluster rapidly into bristle-coated pits. Within a few minutes at 37 degrees C, these complexes are internalized into uncoated cytoplasmic vesicles, called receptosomes, which move about in the cell by saltatory motion. These vesicles interact with the Golgi-endoplasmic reticulum-lysosome system in the cell to deliver the ligand to newly formed lysosomes within 30--60 min.

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