Purification and characterization of the Fas-ligand that induces apoptosis.

Fas is a 45-kD cell surface protein belonging to the tumor necrosis factor/nerve growth factor receptor family, and transduces the signal for apoptosis. The cytotoxic T lymphocyte (CTL) hybridoma, PC60-d10S requires the presence of Fas on target cells to induce cytolysis in target cells. This CTL cell line was weakly but specifically stained by a chimeric protein that consisted of the extracellular domain of mouse Fas and the Fc portion of human immunoglobulin G1 (mFas-Fc). Moreover, mFas-Fc inhibited the cytotoxic activity of PC60-d10S. Sublines of d10S that were stained intensively by mFas-Fc were isolated by repetitive fluorescence-activated cell sorter sorting. A cell-surface protein of about 40 kD was specifically precipitated by mFas-Fc from the lysates of these sublines. This protein was homogeneously purified by sequential affinity chromatographies using mFas-Fc and concanavalin A beads. The purified protein exhibited cytotoxic activity against cells expressing Fas but not to the cells which do not express Fas. These results indicated that the 40-kD membrane glycoprotein expressed on PC60-d10S cells is the Fas-ligand that induces the apoptotic signal by binding to Fas.

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Localization and expression of msp130, a primary mesenchyme lineage-specific cell surface protein in the sea urchin embryo

Development ◽

10.1242/dev.101.2.255 ◽

1987 ◽

Vol 101 (2) ◽

pp. 255-265 ◽

Cited By ~ 4

Author(s):

J.A. Anstrom ◽

J.E. Chin ◽

D.S. Leaf ◽

A.L. Parks ◽

R.A. Raff

Keyword(s):

Cell Surface ◽

Sea Urchin ◽

Sea Water ◽

Surface Protein ◽

Specific Cell ◽

Cell Surface Protein ◽

Sea Urchin Embryo ◽

A Cell ◽

Mesenchyme Cells ◽

Primary Mesenchyme Cells

In this report, we use a monoclonal antibody (B2C2) and antibodies against a fusion protein (Leaf et al. 1987) to characterize msp130, a cell surface protein specific to the primary mesenchyme cells of the sea urchin embryo. This protein first appears on the surface of these cells upon ingression into the blastocoel. Immunoelectronmicroscopy shows that msp130 is present in the trans side of the Golgi apparatus and on the extracellular surface of primary mesenchyme cells. Four precursor proteins to msp130 are identified and we show that B2C2 recognizes only the mature form of msp130. We demonstrate that msp130 contains N-linked carbohydrate groups and that the B2C2 epitope is sensitive to endoglycosidase F digestion. Evidence that msp130 is apparently a sulphated glycoprotein is presented. The recognition of the B2C2 epitope of msp130 is disrupted when embryos are cultured in sulphate-free sea water. In addition, two-dimensional immunoblots show that msp130 is an acidic protein that becomes substantially less acidic in the absence of sulphate. We also show that two other independently derived monoclonal antibodies, IG8 (McClay et al. 1983; McClay, Matranga & Wessel, 1985) and 1223 (Carson et al. 1985), recognize msp130, and suggest this protein to be a major cell surface antigen of primary mesenchyme cells.

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A cell surface protein controls endocrine ring gland morphogenesis and steroid production

Developmental Biology ◽

10.1016/j.ydbio.2018.10.007 ◽

2019 ◽

Vol 445 (1) ◽

pp. 16-28 ◽

Cited By ~ 2

Author(s):

Yanina-Yasmin Pesch ◽

Ricarda Hesse ◽

Tariq Ali ◽

Matthias Behr

Keyword(s):

Cell Surface ◽

Surface Protein ◽

Cell Surface Protein ◽

Steroid Production ◽

Ring Gland ◽

A Cell ◽

Gland Morphogenesis

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The in silico human surfaceome

Proceedings of the National Academy of Sciences ◽

10.1073/pnas.1808790115 ◽

2018 ◽

Vol 115 (46) ◽

pp. E10988-E10997 ◽

Cited By ~ 44

Author(s):

Damaris Bausch-Fluck ◽

Ulrich Goldmann ◽

Sebastian Müller ◽

Marc van Oostrum ◽

Maik Müller ◽

...

Keyword(s):

Cell Surface ◽

In Silico ◽

Embryonic Stem ◽

Surface Protein ◽

Surface Proteins ◽

Cell Surface Protein ◽

Cell Surface Proteins ◽

A Cell ◽

Visualization Tools ◽

Protein Classes

Cell-surface proteins are of great biomedical importance, as demonstrated by the fact that 66% of approved human drugs listed in the DrugBank database target a cell-surface protein. Despite this biomedical relevance, there has been no comprehensive assessment of the human surfaceome, and only a fraction of the predicted 5,000 human transmembrane proteins have been shown to be located at the plasma membrane. To enable analysis of the human surfaceome, we developed the surfaceome predictor SURFY, based on machine learning. As a training set, we used experimentally verified high-confidence cell-surface proteins from the Cell Surface Protein Atlas (CSPA) and trained a random forest classifier on 131 features per protein and, specifically, per topological domain. SURFY was used to predict a human surfaceome of 2,886 proteins with an accuracy of 93.5%, which shows excellent overlap with known cell-surface protein classes (i.e., receptors). In deposited mRNA data, we found that between 543 and 1,100 surfaceome genes were expressed in cancer cell lines and maximally 1,700 surfaceome genes were expressed in embryonic stem cells and derivative lines. Thus, the surfaceome diversity depends on cell type and appears to be more dynamic than the nonsurface proteome. To make the predicted surfaceome readily accessible to the research community, we provide visualization tools for intuitive interrogation (wlab.ethz.ch/surfaceome). The in silico surfaceome enables the filtering of data generated by multiomics screens and supports the elucidation of the surfaceome nanoscale organization.

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Rosetting of activated human T lymphocytes with autologous erythrocytes. Definition of the receptor and ligand molecules as CD2 and lymphocyte function-associated antigen 3 (LFA-3).

Journal of Experimental Medicine ◽

10.1084/jem.165.3.664 ◽

1987 ◽

Vol 165 (3) ◽

pp. 664-676 ◽

Cited By ~ 76

Author(s):

M L Plunkett ◽

M E Sanders ◽

P Selvaraj ◽

M L Dustin ◽

T A Springer

Keyword(s):

Cell Adhesion ◽

T Cell ◽

T Lymphocytes ◽

Cell Surface ◽

T Lymphocyte ◽

Surface Protein ◽

Target Cells ◽

Lymphocyte Function ◽

Cell Surface Protein ◽

Definition Of

CD2, also known as LFA-2, T11, and the E rosette receptor, is a T lymphocyte surface protein functionally important in adhesion to target cells and T cell triggering. LFA-3 is a widely distributed cell surface protein that functions in adhesion on target cells. We find that LFA-3 is expressed on human E, and that CD2 is a receptor for LFA-3 that mediates T cell adhesion to human E. Pretreatment of T lymphocytes with CD2 mAb or of E with LFA-3 mAb inhibits rosetting. Purified CD2 molecules bind to human E and inhibit rosetting. 125I-CD2 binding to E is inhibited by LFA-3 mAb; reciprocally, binding of LFA-3 mAb to human E is inhibited by pretreatment with purified CD2. Higher concentrations of CD2 aggregate human E; aggregation is inhibited by mAb to LFA-3.

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