Neogenin, an avian cell surface protein expressed during terminal neuronal differentiation, is closely related to the human tumor suppressor molecule deleted in colorectal cancer.

Using a monoclonal antibody, we have identified and characterized a previously unknown cell surface protein in chicken that we call neogenin and have determined its primary sequence. The deduced amino acid sequence and structure of neogenin characterize it as a member of the immunoglobulin (Ig) superfamily. Based on amino acid sequence similarities, neogenin is closely related to the human tumor suppressor molecule DCC (deleted in colorectal cancer). Neogenin and DCC define a subgroup of Ig superfamily proteins structurally distinct from other Ig molecules such as N-CAM, Ng-CAM, and Bravo/Nr-CAM. As revealed by antibody staining of tissue sections and Western blots, neogenin expression correlates with the onset of neuronal differentiation. Neogenin is also found on cells in the lower gastrointestinal tract of embryonic chickens. DCC has been observed in human neural tissues and has been shown to be essential for terminal differentiation of specific cell types in the adult human colon. These parallels suggest that neogenin, like DCC, is functionally involved in the transition from cell proliferation to terminal differentiation of specific cell types. Since neogenin is expressed on growing neurites and downregulated at termination of neurite growth, it may also play an important role in many of the complex functional aspects of neurite extension and intercellular signaling.

Download Full-text

Appearance in confluent vascular endothelial cell monolayers of a specific cell surface protein (CSP-60) not detected in actively growing endothelial cells or in cell types growing in multiple layers

Proceedings of the National Academy of Sciences ◽

10.1073/pnas.76.9.4704 ◽

1979 ◽

Vol 76 (9) ◽

pp. 4704-4705

Keyword(s):

Endothelial Cells ◽

Endothelial Cell ◽

Vascular Endothelial Cell ◽

Surface Protein ◽

Cell Types ◽

Specific Cell ◽

Vascular Endothelial ◽

Cell Surface Protein ◽

Cell Monolayers ◽

Specific Cell Surface

Download Full-text

Appearance in confluent vascular endothelial cell monolayers of a specific cell surface protein (CSP-60) not detected in actively growing endothelial cells or in cell types growing in multiple layers.

Proceedings of the National Academy of Sciences ◽

10.1073/pnas.76.5.2306 ◽

1979 ◽

Vol 76 (5) ◽

pp. 2306-2310 ◽

Cited By ~ 35

Author(s):

I. Vlodavsky ◽

L. K. Johnson ◽

D. Gospodarowicz

Keyword(s):

Endothelial Cells ◽

Endothelial Cell ◽

Vascular Endothelial Cell ◽

Surface Protein ◽

Cell Types ◽

Specific Cell ◽

Vascular Endothelial ◽

Cell Surface Protein ◽

Cell Monolayers ◽

Specific Cell Surface

Download Full-text

Proteins on the surface of the malaria parasite and cell invasion

Parasitology ◽

10.1017/s0031182000075673 ◽

1994 ◽

Vol 108 (S1) ◽

pp. S5-S18 ◽

Cited By ~ 47

Author(s):

A. A. Holder

Keyword(s):

Amino Acid ◽

Cell Surface ◽

Malaria Parasite ◽

Surface Protein ◽

Cell Types ◽

Merozoite Surface Protein ◽

Amino Acid Sequences ◽

Specific Cell ◽

Binding Studies ◽

Erythrocyte Invasion

SUMMARYThe malaria parasite exists in an extracellular form at several stages in its life cycle. Within the vertebrate host, sporozoites and merozoites have to invade specific cell types. Proteins on the surface of the parasite or externalized from specialized organelles have been implicated as ligands for receptors on the host cell surface. Direct binding studies have identified parasite proteins that interact with the target cell surface. Examination of the deduced amino acid sequences has allowed the identification of primary structural motifs which may have roles in this process. On the sporozoite, the circum-sporozoite protein and sporozoite surface protein-2, a protein initially located within micronemes, have been found to contain an amino acid sequence thought to be involved in mediating recognition of sulphated polysaccharides on the surface of a liver cell. On the merozoite, merozoite surface protein-1 may be involved in the initial recognition of red blood cells; this protein undergoes a complex series of modifications in the time between its synthesis as a precursor molecule and successful erythrocyte invasion. Other merozoite proteins located at the apical end of the parasite have been identified as erythrocyte or reticulocyte binding proteins.

Download Full-text

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.

Download Full-text

Hybrid gold nanocube@silica@graphene-quantum-dot superstructures: synthesis and specific cell surface protein imaging applications

Chemical Communications ◽

10.1039/c3cc38776c ◽

2013 ◽

Vol 49 (25) ◽

pp. 2503 ◽

Cited By ~ 39

Author(s):

Liu Deng ◽

Ling Liu ◽

Chengzhou Zhu ◽

Dan Li ◽

Shaojun Dong

Keyword(s):

Quantum Dot ◽

Cell Surface ◽

Surface Protein ◽

Specific Cell ◽

Cell Surface Protein ◽

Graphene Quantum Dot ◽

Protein Imaging ◽

Specific Cell Surface

Download Full-text

E1a induces the expression of epithelial characteristics.

The Journal of Cell Biology ◽

10.1083/jcb.127.4.1085 ◽

1994 ◽

Vol 127 (4) ◽

pp. 1085-1096 ◽

Cited By ~ 62

Author(s):

S M Frisch

Keyword(s):

Tumor Cells ◽

Present Report ◽

Human Tumor ◽

Cell Types ◽

Suppressor Gene ◽

Specific Cell ◽

Human Tumor Cells ◽

Mammalian Embryo ◽

Adenovirus E1a ◽

Mesenchymal Differentiation

Cells closely resembling epithelia constitute the first specific cell type in a mammalian embryo. Many other cell types emerge via epithelial-mesenchymal differentiation. The transcription factors and signal transduction pathways involved in this differentiation are being elucidated. I have previously reported (Frisch, 1991) that adenovirus E1a is a tumor suppressor gene in certain human cell lines. In the present report, I demonstrate that E1a expression caused diverse human tumor cells (rhabdomyosarcoma, fibrosarcoma, melanoma, osteosarcoma) and fibroblasts to assume at least two of the following epithelial characteristics: (a) epithelioid morphology; (b) epithelial-type intercellular adhesion proteins localized to newly formed junctional complexes; (c) keratin-containing intermediate filaments; and (d) down-regulation of non-epithelial genes. E1a thus appeared to partially convert diverse human tumor cells into an epithelial phenotype. This provides a new system for molecular analysis of epithelial-mesenchymal interconversions. This effect may also contribute to E1a's tumor suppression activity, possibly through sensitization to anoikis (Frisch, S.M., and H. Francis, 1994. J. Cell Biol. 124:619-626).

Download Full-text

Biosynthesis of a phosphatidylinositol-glycan-linked membrane protein: signals for posttranslational processing of the Ly-6E antigen

Molecular and Cellular Biology ◽

10.1128/mcb.9.8.3369-3376.1989 ◽

1989 ◽

Vol 9 (8) ◽

pp. 3369-3376

Author(s):

B Su ◽

A L Bothwell

Keyword(s):

Amino Acid ◽

Surface Protein ◽

Proteolytic Cleavage ◽

Acid Sites ◽

Cell Surface Protein ◽

Mutant Proteins ◽

Cos Cells ◽

Amino Acid Peptide ◽

Peripheral T Cells ◽

Carboxy Terminal

The Ly-6E/A protein is a murine cell surface protein expressed at high levels on activated peripheral T cells. The only linkage known to be responsible for its association with the plasma membrane is a phosphatidylinositol-glycan (PI-G) moiety. To examine the biosynthesis of this structure, we constructed a series of mutants of Ly-6E that were expressed in COS cells by using transient-transfection procedures. When 12 or 20 carboxy-terminal residues were deleted from the primary translation product, the PI-G modification was completely abolished and the mutant proteins became secreted. Addition of the PI-G tail was partially inhibited when the charged 12-amino-acid peptide found as a cytoplasmic tail on the transmembrane form of LFA-3 was added to the COOH terminus of the Ly-6E protein. Proteolytic cleavage occurred on this mutant protein, but the PI-G moiety was added to only 50% of the molecules. Changing an Asn residue to a Lys at the hypothetical cleavage site resulted in a PI-G-linked protein having a detectable alteration in electrophoretic mobility. This finding raises the possibility that proteolytic cleavage at other amino acid sites may occur and that PI-G attachment can occur at this new site. A model identifying two regions that may act as necessary signals for the biosynthesis of the PI-G tail is presented.

Download Full-text

Rat liver endothelial cell glutamine transporter and glutaminase expression contrast with parenchymal cells

AJP Gastrointestinal and Liver Physiology ◽

10.1152/ajpgi.1999.276.3.g743 ◽

1999 ◽

Vol 276 (3) ◽

pp. G743-G750 ◽

Cited By ~ 5

Author(s):

Rüdiger Lohmann ◽

Wiley W. Souba ◽

Barrie P. Bode

Keyword(s):

Endothelial Cells ◽

Amino Acid ◽

Cell Types ◽

Male Rats ◽

Specific Cell ◽

Liver Endothelial Cell ◽

Glutamine Transporter ◽

Health And Disease ◽

Parenchymal Cells ◽

Functional Analyses

Despite the central role of the liver in glutamine homeostasis in health and disease, little is known about the mechanism by which this amino acid is transported into sinusoidal endothelial cells, the second most abundant hepatic cell type. To address this issue, the transport ofl-glutamine was functionally characterized in hepatic endothelial cells isolated from male rats. On the basis of functional analyses, including kinetics, cation substitution, and amino acid inhibition, it was determined that a Na+-dependent carrier distinct from system N in parenchymal cells, with properties of system ASC or B0, mediated the majority of glutamine transport in hepatic endothelial cells. These results were supported by Northern blot analyses that showed expression of the ATB0 transporter gene in endothelial but not parenchymal cells. Concurrently, it was determined that, whereas both cell types express glutamine synthetase, hepatic endothelial cells express the kidney-type glutaminase isozyme in contrast to the liver-type isozyme in parenchymal cells. This represents the first report of ATB0 and kidney-type glutaminase isozyme expression in the liver, observations that have implications for roles of specific cell types in hepatic glutamine homeostasis in health and disease.

Download Full-text