Takada Lab - UC Davis
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News 36 Publications 1 Members

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...

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...

The chemokine fractalkine can activate integrins without CX3CR1 through direct binding to a ligand-binding site distinct...

Fujita, Masaaki Takada, Yoko K Takada, Yoshikazu

Published in PloS one

The chemokine domain of fractalkine (FKN-CD) binds to the classical RGD-binding site of αvβ3 and that the resulting ternary complex formation (integrin-FKN-CX3CR1) is critical for CX3CR1 signaling and FKN-induced integrin activation. However, only certain cell types express CX3CR1. Here we studied if FKN-CD can activate integrins in the absence of ...

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...

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...

The use of one-bead one-compound combinatorial library technology to discover high-affinity αvβ3 integrin and cancer tar...

Xiao, Wenwu Wang, Yan Lau, Edmond Y Luo, Juntao Yao, Nianhuan Shi, Changying Meza, Leah Tseng, Harry Maeda, Yoshiko Kumaresan, Pappanaicken ...

Published in Molecular cancer therapeutics

The αvβ3 integrin, expressed on the surface of various normal and cancer cells, is involved in numerous physiologic processes such as angiogenesis, apoptosis, and bone resorption. Because this integrin plays a key role in angiogenesis and metastasis of human tumors, αvβ3 integrin ligands are of great interest to advances in targeted therapy and can...

Direct Binding of the EGF-like Domain of Neuregulin-1 to Integrins (alphavbeta3 and alpha6beta4) Is Involved in Neuregul...

Ieguchi, K Fujita, M Ma, Z Davari, P Taniguchi, Y Sekiguchi, K Wang, B Takada, Yk Yoshikazu Takada

Published in JBIC Journal of Biological Inorganic Chemistry

A T cell-binding fragment of fibrinogen can prevent autoimmunity.

E, Maningding A, Coleman D, Ramirez-Maverakis R, Rodrigues Y, Takada E, Maverakis Y, Takada Y, Ono J, Saegusa C, Mitsiades ...

Published in Journal of Autoimmunity

The C-terminal domain of the fibrinogen gamma chain (gammaC) has been shown to bind to the integrins alphaIIbbeta3, alphaMbeta2 and alphaVbeta3. It has also been reported that a peptide derived from the alphaMbeta2-binding site of gammaC can suppress an animal model of multiple sclerosis, experimental autoimmune encephalomyelitis (EAE). Here we hav...

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...

Fibrinogen-gamma C-terminal fragments induce endothelial barrier dysfunction and microvascular leak via integrin-mediate...

Guo, Mingzhang Daines, Dayle Tang, Jing Shen, Qiang Perrin, Rachel M Takada, Yoshikazu Yuan, Sarah Y Wu, Mack H

Published in Arteriosclerosis, thrombosis, and vascular biology

The purposes of this study were to characterize the direct effect of the C-terminal fragment of fibrinogen gamma chain (gammaC) on microvascular endothelial permeability and to examine its molecular mechanism of action. Intravital microscopy was performed to measure albumin extravasation in intact mesenteric microvasculature, followed by quantifica...

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