Monoclonal antibody AG-1 initiates platelet activation by a pathway dependent on glycoprotein IIb–IIIa and extracellular calcium

Kroll, Michael H.; Mendelsohn, Michael E.; Miller, Jonathan L.; Ballen, Karen K.; Hrbolich, Janet K.; Schafer, Andrew I.

doi:10.1016/0167-4889(92)90144-z

Cited by 17 publications

(12 citation statements)

References 46 publications

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“…Indeed, it has been proposed that a calcium-dependent mode of signaling is utilized in Thy-1-mediated neurite outgrowth . Similarly, some anti-CD9 mAbs are thought to act via calcium-and G-protein-mediated signaling Kroll et al, 1992). Although there is ample evidence that CD9 interacts with the ␣3␤1 integrin, Thy-1 has not been shown to interact with integrins.…”

Section: Discussionmentioning

confidence: 99%

An Antibody to the Tetraspan Membrane Protein CD9 Promotes Neurite Formation in a Partially α3β1 Integrin-Dependent Manner

1997

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The tetraspan cell surface glycoprotein, CD9, has been implicated in cellular signaling during growth and differentiation in the hematopoietic and nervous systems. Because CD9 expression is induced early in development in sensory and sympathetic neuroblasts, we investigated the role of CD9 in neurite outgrowth. We plated dissociated cells from neonatal sympathetic ganglia on immobilized anti-CD9 antibodies or antibodies against other cell surface molecules. We show here that B2C11, an anti-CD9 antibody that has been shown previously to activate Schwann cells in vitro, promotes robust neurite outgrowth from sympathetic neurons that is greater than that on other antibody surfaces and is comparable to neurite outgrowth on a collagen substratum. In addition, B2C11 causes dramatic morphological changes in neurons and glia from dissociated ganglia, including a flattening of these cells.Because CD9 interacts with integrins in many cell types including Schwann cells, and specifically with the ␣3␤1 integrin in some cells, we tested whether the effect of B2C11 on neurite outgrowth is mediated by this integrin. An anti-␣3␤1 antibody, Ralph 3-1, attenuates the extent of neurite outgrowth on B2C11 and collagen, but not on laminin. Because the ␣3␤1 integrin has been shown to mediate neurite outgrowth on different substrates, these results provide a functional significance for the CD9-␣3␤1 interaction; downstream signaling may be activated by this cis interaction on the cell surface in response to external cues that promote neurite outgrowth.

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Section: Discussionmentioning

confidence: 99%

An Antibody to the Tetraspan Membrane Protein CD9 Promotes Neurite Formation in a Partially α3β1 Integrin-Dependent Manner

1997

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“…Our reports suggest that the tyrosine phosphorylation of the p46 Shc isoform might be mediated by other molecules that are associated with CD9. CD9 associates with small G-proteins, and the antibody ligation of CD9 on platelets induces tyrosine phosphorylation and increases intracellular calcium concentration (Kroll et al, 1992;Yatomi et al, 1993). Tetraspanin proteins might contribute to integrin-mediated signaling (Shaw et al, 1995;Yáñez-Mó et al, 1998;Berditchdvski and Odintsova, 1999).…”

Section: Discussionmentioning

confidence: 99%

“…Tyrosine phosphorylation of signal-transducing molecules induced by CD9 ligation It is known that the antibody ligation of CD9 induces tyrosine phosphorylation in some signaling molecules in platelets (Kroll et al, 1992;Yatomi et al, 1993;Aoyama et al, 1999). We investigated the phosphorylation of several signaltransduction molecules after treatment of MKN-28 cells with ALB6.…”

Section: Antibody Ligation Of Cd9 Inhibits the Proliferation Of Humanmentioning

confidence: 99%

CD9-mediated activation of the p46 Shc isoform leads to apoptosis in cancer cells

Murayama

Miyagawa

Oritani

et al. 2004

Journal of Cell Science

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CD9, a member of the tetraspanin family, has been shown to be involved in a range of cellular activities, including migration, proliferation and adhesion, but the molecular mechanisms by which it mediates such events is unclear. Here, we found that anti-CD9 monoclonal antibody ALB6 inhibited cell proliferation, reduced cell viability and induced not only morphological changes specific to apoptosis but also molecular changes, as evidenced by TUNEL and annexin-V staining. For the possible mechanism of ALB6-induced apoptosis, ALB6 activated the c-Jun NH2-terminal kinase/stress-activated protein kinase (JNK/SAPK) and p38 mitogen-activated-protein kinase (MAPK) within 5-15 minutes, as well as caspase-3 within 24-48 hours. It is noteworthy that ALB6 induced tyrosine phosphorylation of the p46 Shc isoform specifically and that the overexpression of its dominant-negative form completely suppressed the ALB6-induced activation of JNK/SAPK, p38 MAPK and caspase-3, resulting in the inhibition of apoptotic cell death. These results suggest that CD9 might regulate apoptosis through the specialized signals in human cancer cell lines.

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“…We have characterized a cell surface constituent involved in outgrowth of neurites and astrocytic processes and migration of neuronal cell bodies and identified it as the mouse homologue of CD9, a cell surface marker of hemopoietic cells that has been implicated in aggregation of platelets (Hato et al, 1988;Jennings et al, 1990;Griffith et al, 1991;Kroll et al, 1992). CD9 is a signal transducer in that it activates Ca2+ entry into neural cells and appears to cooperate with the 016/@l integrin to promote laminindependent neurite outgrowth, possibly in a cooperative manner.…”

Section: Introductionmentioning

confidence: 97%

CD9 of mouse brain is implicated in neurite outgrowth and cell migration in vitro and is associated with the α6/β1 integrin and the neural adhesion molecule L1

Schmidt

Künemund

Wintergerst

et al. 1996

J of Neuroscience Research

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We describe here a novel monoclonal antibody (mab H6) which recognizes CD9, an integral cell surface constituent previously described in cells of the hematopoietic lineage and involved in the aggregation of platelets. Mab H6 was raised against membranes of immature mouse astrocytes and reacted with a protein of 25-27 kD in detergent extracts of adult mouse brain membranes. Sequence analysis of the N-terminal amino acids revealed an identity of 96% with CD9 from mouse kidney. CD9 was localized in the central and peripheral mouse nervous systems: in the spinal cord of 11-day-old mouse embryos, CD9 was strongly expressed in the floor and roof plates. In the adult mouse sciatic nerve, myelin sheaths were highly CD9-immunoreactive. Mab H6 reacted with the cell surfaces of both glial cells and neurons in culture and inhibited migration of neuronal cell bodies, neurite fasciculation and outgrowth of astrocytic processes from cerebellar microexplants. Neurite outgrowth from isolated small cerebellar neurons was increased in the presence of mab H6 on substrate-coated laminin, but not on substrate-coated poly-L-lysine. Addition of mab H6 elicited an increase in intracellular Ca2+ concentration in these cells on substrate-coated laminin. Immunoprecipitates of CD9 from cultured mouse neuroblastoma N2A cells contained the alpha 6/beta 1 integrin. Moreover, preparations of CD9 immunoaffinity-purified from adult mouse brain using a mab H6 column contained the neural adhesion molecule L1, but not other neural adhesion molecules. CD9 bound to L1, but not to NCAM or MAG. Both the alpha 6/beta 1 integrin and L1 could be induced to coredistribute with CD9 on the surface of cultured neuroblastoma N2A cells. The combined observations suggest that CD9 can associate with L1 and alpha 6/beta 1 integrin to influence neural cell interactions in vitro.

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Monoclonal antibody AG-1 initiates platelet activation by a pathway dependent on glycoprotein IIb–IIIa and extracellular calcium

Cited by 17 publications

References 46 publications

An Antibody to the Tetraspan Membrane Protein CD9 Promotes Neurite Formation in a Partially α3β1 Integrin-Dependent Manner

An Antibody to the Tetraspan Membrane Protein CD9 Promotes Neurite Formation in a Partially α3β1 Integrin-Dependent Manner

CD9-mediated activation of the p46 Shc isoform leads to apoptosis in cancer cells

CD9 of mouse brain is implicated in neurite outgrowth and cell migration in vitro and is associated with the α6/β1 integrin and the neural adhesion molecule L1

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