Takada Lab - UC Davis
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Pro-inflammatory secretory phospholipase A2 type IIA binds to integrins alphavbeta3 and alpha4beta1 and induces prolifer...

Saegusa, Jun Akakura, Nobuaki Wu, Chun-Yi Hoogland, Case Ma, Zi Lam, Kit S Liu, Fu-Tong Takada, Yoko K Takada, Yoshikazu

Published in The Journal of biological chemistry

Secretory phospholipase A2 group IIA (sPLA2-IIA) plays an important role in the pathogenesis of inflammatory diseases. Catalytic activity of this enzyme that generates arachidonic acid is a major target for development of anti-inflammatory agents. Independent of its catalytic activity, sPLA2-IIA induces pro-inflammatory signals in a receptor-mediat...

Plasmin-induced migration requires signaling through protease-activated receptor 1 and integrin alpha(9)beta(1).

Majumdar, M Tarui, T Shi, B Akakura, N Ruf, W Yoshikazu Takada

Published in Journal of Biological Chemistry

Plasmin is a major extracellular protease that elicits intracellular signals to mediate platelet aggregation, chemotaxis of peripheral blood monocytes, and release of arachidonate and leukotriene from several cell types in a G protein-dependent manner. Angiostatin, a fragment of plasmin(ogen), is a ligand and an antagonist for integrin alpha(9)beta...

An integrin binding-defective mutant of insulin-like growth factor-1 (R36E/R37E IGF1) acts as a dominant-negative antago...

Fujita, M Ieguchi, K Cedano-Prieto, Dm Fong, A Wilkerson, C Chen, Jq Wu, M Lo, Sh Cheung, At Wilson, Md ...

Published in Journal of Biological Chemistry

Insulin-like growth factor-1 (IGF1) is a major therapeutic target for cancer. We recently reported that IGF1 directly binds to integrins (αvβ3 and α6β4) and induces ternary complex formation (integrin-IGF1-IGF1 receptor (IGF1R)) and that the integrin binding-defective mutant of IGF1 (R36E/R37E) is defective in signaling and ternary complex formatio...

Insulin-like growth factor (IGF) signaling requires αvβ3-IGF1-IGF type 1 receptor (IGF1R) ternary complex formation in a...

Fujita, Masaaki Takada, Yoko K Takada, Yoshikazu

Published in The Journal of biological chemistry

Integrin αvβ3 plays a role in insulin-like growth factor 1 (IGF1) signaling (integrin-IGF1 receptor (IGF1R) cross-talk) in non-transformed cells in anchorage-dependent conditions. We reported previously that IGF1 directly binds to αvβ3 and induces αvβ3-IGF1-IGF1R ternary complex formation in these conditions. The integrin-binding defective IGF1 mut...

Identification of Equine Lactadherin-derived Peptides That Inhibit Rotavirus Infection via Integrin Receptor Competition...

Civra, Andrea Giuffrida, Maria Gabriella Donalisio, Manuela Napolitano, Lorenzo Takada, Yoshikazu Coulson, Barbara S Conti, Amedeo Lembo, David

Published in The Journal of biological chemistry

Human rotavirus is the leading cause of severe gastroenteritis in infants and children under the age of 5 years in both developed and developing countries. Human lactadherin, a milk fat globule membrane glycoprotein, inhibits human rotavirus infection in vitro, whereas bovine lactadherin is not active. Moreover, it protects breastfed infants agains...

Cross-talk between integrin α6β4 and insulin-like growth factor-1 receptor (IGF1R) through direct α6β4 binding to IGF1 a...

Fujita, M Ieguchi, K Davari, P Yamaji, S Taniguchi, Y Sekiguchi, K Takada, Yk Yoshikazu Takada

Published in Journal of Biological Chemistry

Integrin αvβ3 plays a role in insulin-like growth factor-1 (IGF1) signaling (integrin-IGF1 receptor (IGF1R) cross-talk). The specifics of the cross-talk are, however, unclear. In a current model, "ligand occupancy" of αvβ3 (i.e. the binding of extracellular matrix proteins) enhances signaling induced by IGF1 binding to IGF1R. We recently reported t...

The direct binding of insulin-like growth factor-1 (IGF-1) to integrin alphavbeta3 is involved in IGF-1 signaling.

J, Saegusa S, Yamaji K, Ieguchi Cy, Wu Ks, Lam Ft, Liu Yk, Takada Y, Takada

Published in Journal of Biological Chemistry

It has been proposed that ligand occupancy of integrin alphavbeta3 with extracellular matrix ligands (e.g. vitronectin) plays a critical role in insulin-like growth factor-1 (IGF-1) signaling. We found that expression of alphavbeta3 enhanced IGF-1-induced proliferation of Chinese hamster ovary cells in serum-free conditions (in the absence of vitro...

Non-cytotoxic cobra cardiotoxin A5 binds to alpha(v)beta3 integrin and inhibits bone resorption. Identification of cardi...

Wu, Pl Lee, Sc Chuang, Cc Mori, S Akakura, N Wu, Wg Yoshikazu Takada

Published in Journal of Biological Chemistry

Severe tissue necrosis with a retarded wound healing process is a major symptom of a cobra snakebite. Cardiotoxins (CTXs) are major components of cobra venoms that belong to the Ly-6 protein family and are implicated in tissue damage. The interaction of the major CTX from Taiwan cobra, i.e. CTX A3, with sulfatides in the cell membrane has recently ...

Proinflammatory secreted phospholipase A2 type IIA (sPLA-IIA) induces integrin activation through direct binding to a ne...

Fujita, Masaaki Zhu, Kan Fujita, Chitose K Zhao, Min Lam, Kit S Kurth, Mark J Takada, Yoko K Takada, Yoshikazu

Published in The Journal of biological chemistry

Integrins are activated by signaling from inside the cell (inside-out signaling) through global conformational changes of integrins. We recently discovered that fractalkine activates integrins in the absence of CX3CR1 through the direct binding of fractalkine to a ligand-binding site in the integrin headpiece (site 2) that is distinct from the clas...

Enhanced activity of transforming growth factor β1 (TGF-β1) bound to cartilage oligomeric matrix protein.

Haudenschild, Dominik R Hong, Eunmee Yik, Jasper H N Chromy, Brett Mörgelin, Matthias Snow, Kaylene D Acharya, Chitrangada Takada, Yoshikazu Di Cesare, Paul E

Published in The Journal of biological chemistry

Cartilage oligomeric matrix protein (COMP) is an important non-collagenous cartilage protein that is essential for the structural integrity of the cartilage extracellular matrix. The repeated modular structure of COMP allows it to "bridge" and assemble multiple cartilage extracellular matrix components such as collagens, matrilins, and proteoglycan...

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