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C and Corvaia N. Tetraspanin CD151 as a target for antibody-based cancer immunotherapy. Biochem Soc Trans 2011
"... Abstract CD151 is a plasma membrane protein belonging to the tetraspanin superfamily which is expressed on normal cells such as endothelial cells and platelets and frequently overexpressed on cancer cells. It is known to be functionally linked to cancer metastasis. In humans, increased expression o ..."
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Abstract CD151 is a plasma membrane protein belonging to the tetraspanin superfamily which is expressed on normal cells such as endothelial cells and platelets and frequently overexpressed on cancer cells. It is known to be functionally linked to cancer metastasis. In humans, increased expression of CD151 is indicative of a poor prognosis in different cancer types. Whereas its mechanism of action remains obscure, CD151 was shown to regulate cell motility and adhesion through association with laminin-binding integrins such as α3β1 or α6β4. Several anti-CD151 mAbs (monoclonal antibodies) have been shown to display anti-metastatic activity in vivo. Inhibition of metastasis was not attributed to any effect of these mAbs on tumour cell growth, but was essentially attributed to inhibition of cell motility. We have generated anti-CD151 mAbs which can inhibit the tumoral growth in different xenograft cancer models. As expected, these mAbs were also able to inhibit metastasis in orthotopic cancer models. These data suggest that CD151 could function at multiple cancer stages, including not only metastasis cascade steps, but also earlier steps of primary tumour growth, thus reinforcing the interest of this innovative target in oncology. mAbs targeting CD151 may be of significant interest for cancer biotherapy.
A Report Summary
- Computing in Science & Engineering
, 2006
"... Fusion between HeLa and fibroblasts from complementation group D xeroderma pigmentosum (XPD) followed by challenge with small doses of ultraviolet light (u.v.) results in the production of hybrid cells expressing either HeLa (HD1) or XPo-like (HD2) sensitivity to u.v. and related repair capacity. As ..."
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Fusion between HeLa and fibroblasts from complementation group D xeroderma pigmentosum (XPD) followed by challenge with small doses of ultraviolet light (u.v.) results in the production of hybrid cells expressing either HeLa (HD1) or XPo-like (HD2) sensitivity to u.v. and related repair capacity. Assays used include unscheduled DNA synthesis (UDS), DNA break accumulation in the presence of inhibitors of DNA repair synthesis and host cell reactivation of irradiated adenovirus. Complementation assay in heterokaryons reveals limited ability of HD2 to restore UDS in X P D nuclei. We believe this complementation is more apparent than real since proliferating hybrids of HD2 and X P D parentage are without exception u.v.-sensitive and express limited excision repair. On the other hand hybrids between HD2 and XPc, X P E or X P F fibroblasts show true complemen-tation resulting in a return to normal u.v. sensitivity and elevated repair ability.
LATERALLY ASSOCIATED PROTEINS MODULATE α6 INTEGRIN CLEAVAGE, A PERMISSIVE PROCESS UTILIZED DURING CANCER METASTASIS. By
, 2009
"... Rights Copyright © is held by the author. Digital access to this material is made possible by the University Libraries, University of Arizona. Further transmission, reproduction or presentation (such as public display or performance) of protected items is prohibited except with permission of the aut ..."
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Rights Copyright © is held by the author. Digital access to this material is made possible by the University Libraries, University of Arizona. Further transmission, reproduction or presentation (such as public display or performance) of protected items is prohibited except with permission of the author. Downloaded 15-Sep-2016 19:32:19 Link to item
Association of the tetraspanin CD151 with the laminin-binding integrins a 3b 1, a 6b 1, a 6b 4 and
"... a 7b 1 in cells in culture and in vivo ..."
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INVESTIGATING POST-TRANSLATIONAL MODIFICATIONS OF TETRASPANINS: PALMITOYLATION OF CD81 AND GLYCOSYLATION OF TSPAN-2
, 2008
"... Members of the protein superfamily of tetraspanins are best defined by a simple structure comprising four transmembrane domains, two extracellular loops of unequal size, and short cytoplasmic regions. Despite their small size, tetraspanins are able to participate in multiple functions, as diverse as ..."
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Members of the protein superfamily of tetraspanins are best defined by a simple structure comprising four transmembrane domains, two extracellular loops of unequal size, and short cytoplasmic regions. Despite their small size, tetraspanins are able to participate in multiple functions, as diverse as B cell activation, cancer metastasis, and viral infection. To compensate for a lack of intrinsic enzymatic activity, tetraspanins have gained the fascinating ability of associating with numerous different proteins. In addition, tetraspanins interact with each other forming a network on the plasma membrane: the tetraspanin web. In this way, functionally related proteins binding to different tetraspanins can be brought into close vicinity, thereby enhancing signaling pathways. The tetraspanin web is a dynamic environment and its regulation has grasped the attention of several research groups in the past few years. Particularly, several tetraspanins have been found to be palmitoylated, a post-translational modification attaching a palmitic acid to cysteine residues in a reversible manner. Palmitoylation is thought to be important for the integrity of the tetraspanin web. We examined the effect of disrupting putative palmitoylation sites on the
For example CD9 partners (CD36, �3 and �6 integrins,
"... many tetraspanin partner proteins are also palmitoylated. ..."
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Review Article
"... and review articles in less time without much delay in the developing field of Pharmaceutical and Biological sciences. One week from the date of manuscript submission author gets the decision of acceptance and if accepted the manuscript will be processed within 3 weeks (approx.) for publication. ..."
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and review articles in less time without much delay in the developing field of Pharmaceutical and Biological sciences. One week from the date of manuscript submission author gets the decision of acceptance and if accepted the manuscript will be processed within 3 weeks (approx.) for publication.
JCB Article Tumor cell �3�1 integrin and vascular laminin-5 mediate pulmonary arrest and metastasis
"... Arrest of circulating tumor cells in distant organs is required for hematogenous metastasis, but the tumor cell surface molecules responsible have not been identified. Here, we show that the tumor cell �3�1 integrin makes an important contribution to arrest in the lung and to early colony formation. ..."
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Arrest of circulating tumor cells in distant organs is required for hematogenous metastasis, but the tumor cell surface molecules responsible have not been identified. Here, we show that the tumor cell �3�1 integrin makes an important contribution to arrest in the lung and to early colony formation. These analyses indicated that pulmonary arrest does not occur merely due to size restriction, and raised the question of how the tumor cell �3�1
�3 and �6 integrin–dependent cellular morphology
"... he �3�1 integrin shows strong, stoichiometric, direct lateral association with the tetraspanin CD151. As shown here, an extracellular CD151 site (QRD194–196) is required for strong (i.e., Triton X-100–resistant) �3�1 association and for maintenance of a key CD151 epitope (defined by monoclonal antib ..."
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he �3�1 integrin shows strong, stoichiometric, direct lateral association with the tetraspanin CD151. As shown here, an extracellular CD151 site (QRD194–196) is required for strong (i.e., Triton X-100–resistant) �3�1 association and for maintenance of a key CD151 epitope (defined by monoclonal antibody TS151r) that is blocked upon �3 integrin association. Strong CD151 association with integrin �6�1 also required the QRD194–196 T site and masked the TS151r epitope. For both �3 and �6 integrins, strong QRD/TS151r-dependent CD151 association occurred early in biosynthesis and involved � subunit precursor forms. In contrast, weaker associations of CD151 with itself, integrins, or other tetraspanins (Triton X-100–sensitive but Brij 96–resistant) were independent of the QRD/TS151r site, occurred late in biosynthesis, and involved mature integrin subunits. Presence of the CD151–QRD 194–196 →INF mutant disrupted �3 and �6 integrin–dependent formation of a network of cellular cables by Cos7 or NIH3T3 cells on basement membrane Matrigel and markedly altered cell spreading. These results provide definitive evidence that strong lateral CD151–integrin association is functionally important, identify CD151 as a key player during �3 and �6 integrin–dependent matrix remodeling and cell spreading, and support a model of CD151 as a transmembrane linker between extracellular integrin domains and intracellular cytoskeleton/signaling molecules. Address correspondence to Martin E. Hemler, Dana-Farber Cancer Institute,
