Abstract
| Originalsprog | Engelsk |
|---|---|
| Tidsskrift | Journal of Cell Biology |
| Vol/bind | 149 |
| Udgave nummer | 5 |
| Sider (fra-til) | 1143-56 |
| Antal sider | 13 |
| ISSN | 0021-9525 |
| Status | Udgivet - 2000 |
Bibliografisk note
Keywords: ADAM Proteins; Actins; Animals; Antibodies, Monoclonal; Antigens, CD29; Breast Neoplasms; Cell Adhesion; Cell Size; Chick Embryo; Chondrocytes; Colonic Neoplasms; Cysteine; Cytoskeleton; Humans; Magnesium; Membrane Glycoproteins; Membrane Proteins; Mesoderm; Metalloendopeptidases; Mice; Mice, Inbred Strains; Muscle, Skeletal; Osteoblasts; Osteosarcoma; Protein Structure, Tertiary; Proteoglycans; Receptor Cross-Talk; Rhabdomyosarcoma; Signal Transduction; Stress, Mechanical; Syndecans; Tumor Cells, CulturedCitationsformater
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The cysteine-rich domain of human ADAM 12 supports cell adhesion through syndecans and triggers signaling events that lead to beta1 integrin-dependent cell spreading. / Iba, K; Albrechtsen, R; Gilpin, B; Frohlich, Camilla; Loechel, F; Zolkiewska, A; Ishiguro, K; Kojima, T; Liu, W; Langford, J K; Sanderson, R D; Brakebusch, C; Fässler, R; Wewer, U M.
I: Journal of Cell Biology, Bind 149, Nr. 5, 2000, s. 1143-56.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › peer review
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TY - JOUR
T1 - The cysteine-rich domain of human ADAM 12 supports cell adhesion through syndecans and triggers signaling events that lead to beta1 integrin-dependent cell spreading.
AU - Iba, K
AU - Albrechtsen, R
AU - Gilpin, B
AU - Frohlich, Camilla
AU - Loechel, F
AU - Zolkiewska, A
AU - Ishiguro, K
AU - Kojima, T
AU - Liu, W
AU - Langford, J K
AU - Sanderson, R D
AU - Brakebusch, C
AU - Fässler, R
AU - Wewer, U M
N1 - Keywords: ADAM Proteins; Actins; Animals; Antibodies, Monoclonal; Antigens, CD29; Breast Neoplasms; Cell Adhesion; Cell Size; Chick Embryo; Chondrocytes; Colonic Neoplasms; Cysteine; Cytoskeleton; Humans; Magnesium; Membrane Glycoproteins; Membrane Proteins; Mesoderm; Metalloendopeptidases; Mice; Mice, Inbred Strains; Muscle, Skeletal; Osteoblasts; Osteosarcoma; Protein Structure, Tertiary; Proteoglycans; Receptor Cross-Talk; Rhabdomyosarcoma; Signal Transduction; Stress, Mechanical; Syndecans; Tumor Cells, Cultured
PY - 2000
Y1 - 2000
N2 - The ADAMs (a disintegrin and metalloprotease) family of proteins is involved in a variety of cellular interactions, including cell adhesion and ecto- domain shedding. Here we show that ADAM 12 binds to cell surface syndecans. Three forms of recombinant ADAM 12 were used in these experiments: the cys-teine-rich domain made in Escherichia coli (rADAM 12-cys), the disintegrin-like and cysteine-rich domain made in insect cells (rADAM 12-DC), and full-length human ADAM 12-S tagged with green fluorescent protein made in mammalian cells (rADAM 12-GFP). Mesenchymal cells specifically and in a dose-dependent manner attach to ADAM 12 via members of the syndecan family. After binding to syndecans, mesenchymal cells spread and form focal adhesions and actin stress fibers. Integrin beta1 was responsible for cell spreading because function-blocking monoclonal antibodies completely inhibited cell spreading, and chondroblasts lacking beta1 integrin attached but did not spread. These data suggest that mesenchymal cells use syndecans as the initial receptor for the ADAM 12 cysteine-rich domain-mediated cell adhesion, and then the beta1 integrin to induce cell spreading. Interestingly, carcinoma cells attached but did not spread on ADAM 12. However, spreading could be efficiently induced by the addition of either 1 mM Mn(2+) or the beta1 integrin-activating monoclonal antibody 12G10, suggesting that in these carcinoma cells, the ADAM 12-syndecan complex fails to modulate the function of beta1 integrin.
AB - The ADAMs (a disintegrin and metalloprotease) family of proteins is involved in a variety of cellular interactions, including cell adhesion and ecto- domain shedding. Here we show that ADAM 12 binds to cell surface syndecans. Three forms of recombinant ADAM 12 were used in these experiments: the cys-teine-rich domain made in Escherichia coli (rADAM 12-cys), the disintegrin-like and cysteine-rich domain made in insect cells (rADAM 12-DC), and full-length human ADAM 12-S tagged with green fluorescent protein made in mammalian cells (rADAM 12-GFP). Mesenchymal cells specifically and in a dose-dependent manner attach to ADAM 12 via members of the syndecan family. After binding to syndecans, mesenchymal cells spread and form focal adhesions and actin stress fibers. Integrin beta1 was responsible for cell spreading because function-blocking monoclonal antibodies completely inhibited cell spreading, and chondroblasts lacking beta1 integrin attached but did not spread. These data suggest that mesenchymal cells use syndecans as the initial receptor for the ADAM 12 cysteine-rich domain-mediated cell adhesion, and then the beta1 integrin to induce cell spreading. Interestingly, carcinoma cells attached but did not spread on ADAM 12. However, spreading could be efficiently induced by the addition of either 1 mM Mn(2+) or the beta1 integrin-activating monoclonal antibody 12G10, suggesting that in these carcinoma cells, the ADAM 12-syndecan complex fails to modulate the function of beta1 integrin.
M3 - Journal article
C2 - 10831617
VL - 149
SP - 1143
EP - 1156
JO - Journal of Cell Biology
JF - Journal of Cell Biology
SN - 0021-9525
IS - 5
ER -