Publications - Yoshikazu Takada - Page 1

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

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

Published in JBIC Journal of Biological Inorganic Chemistry

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

A, Civra Mg, Giuffrida M, Donalisio L, Napolitano Yoshikazu Takada Bs, Coulson A, Conti D, Lembo

Published in 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...

M, Fujita K, Zhu Ck, Fujita M, Zhao Ks, Lam Mj, Kurth Yk, Takada Yoshikazu Takada

Published in 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 binding of monomeric C-reactive protein (mCRP) to Integrins αvβ3 and α4β1 is related to its pro-inflammatory action....

M, Fujita Yk, Takada Y, Izumiya Yoshikazu Takada

The prototypic acute phase reactant C-reactive protein (CRP) is not only a marker but also a potential contributor to inflammatory diseases. CRP exists as the circulating native, pentameric CRP (pCRP) and the monomeric isoform (mCRP), formed as a result of a dissociation process of pCRP. mCRP is highly pro-inflammatory, but pCRP is not. The mechani...

Galectin-3 modulates phagocytosis-induced stellate cell activation and liver fibrosis in vivo.

Jx, Jiang X, Chen Dk, Hsu K, Baghy N, Serizawa F, Scott Yoshikazu Takada Y, Takada H, Fukada J, Chen ...

Published in AJP Gastrointestinal and Liver Physiology

Hepatic stellate cells (HSC), the key fibrogenic cells of the liver, transdifferentiate into myofibroblasts upon phagocytosis of apoptotic hepatocytes. Galectin-3, a β-galactoside-binding lectin, is a regulator of the phagocytic process. In this study, our aim was to study the mechanism by which extracellular galectin-3 modulates HSC phagocytosis a...

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

J, Saegusa N, Akakura Cy, Wu C, Hoogland Z, Ma Ks, Lam Ft, Liu Yk, Takada Yoshikazu Takada

Published in 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...

Optimization of RGD-Containing Cyclic Peptides against αvβ3 Integrin.

Y, Wang W, Xiao Y, Zhang L, Meza H, Tseng Yoshikazu Takada Jb, Ames Ks, Lam

Published in Molecular Cancer Therapeutics

We have previously reported the use of one-bead-one-compound (OBOC) combinatorial technology to develop a disulfide cyclic, Arg-Gly-Asp-containing octapeptide LXW7 (cGRGDdvc), that targets αvβ3 integrin with high affinity and specificity. αvβ3 integrin is known to be overexpressed in many cancers and in tumor vasculature, and it has been establishe...

Identification of inhibitors against interaction between pro-inflammatory sPLA2-IIA protein and integrin αvβ3.

L, Ye T, Dickerson H, Kaur Yk, Takada M, Fujita R, Liu Jm, Knapp Ks, Lam Ne, Schore Mj, Kurth ...

Published in Bioorganic & Medicinal Chemistry Letters

Increased concentrations of secreted phospholipase A2 type IIA (sPLA2-IIA), have been found in the synovial fluid of patients with rheumatoid arthritis. It has been shown that sPLA2-IIA specifically binds to integrin αvβ3, and initiates a signaling pathway that leads to cell proliferation and inflammation. Therefore, the interaction between integri...

Direct interaction of the kringle domain of urokinase-type plasminogen activator (uPA) and integrin alpha v beta 3 induc...

T, Tarui N, Akakura M, Majumdar N, Andronicos J, Takagi Ap, Mazar K, Bdeir A, Kuo Sv, Yarovoi Db, Cines ...

Published in Thrombosis and Haemostasis

It has been questioned whether there are receptors for urokinase-type plasminogen activator (uPA) that facilitate plasminogen activation other than the high affinity uPA receptor (uPAR/CD87) since studies of uPAR knockout mice did not support a major role of uPAR in plasminogen activation. uPA also promotes cell adhesion, chemotaxis, and proliferat...

The integrins.

Yoshikazu Takada X, Ye S, Simon

Published in Genome Biology

The integrins are a superfamily of cell adhesion receptors that bind to extracellular matrix ligands, cell-surface ligands, and soluble ligands. They are transmembrane alphabeta heterodimers and at least 18 alpha and eight beta subunits are known in humans, generating 24 heterodimers. Members of this family have been found in mammals, chicken and z...

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

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

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...

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

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

Discovery of targeting ligands for breast cancer cells using the one-bead one-compound combinatorial method.

N, Yao W, Xiao X, Wang J, Marik Sh, Park Yoshikazu Takada Ks, Lam

Published in Journal of Medicinal Chemistry

Four "one-bead one-compound" (OBOC) combinatorial libraries were designed, synthesized, and screened against MDA-MB-231 breast cancer cells. A novel cyclic peptide 1 (LXY1) with high binding specificity to alpha3 integrin was identified. Molecular interactions between alpha3 integrin and 1 were characterized by using a series of K562 cells transfec...

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

Dr, Haudenschild E, Hong Jh, Yik B, Chromy M, Mörgelin Kd, Snow C, Acharya Yoshikazu Takada Pe, Di Cesare

Published in 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...

Enhanced Expression of Integrin αvβ3 Induced by TGF-β Is Required for the Enhancing Effect of Fibroblast Growth Factor 1...

S, Mori M, Kodaira A, Ito M, Okazaki N, Kawaguchi Y, Hamada Yoshikazu Takada N, Matsuura

Epithelial-to-mesenchymal transition (EMT) plays a critical role in cancer metastasis, and is regulated by growth factors such as transforming growth factor β (TGF-β) and fibroblast growth factors (FGF) secreted from the stromal and tumor cells. However, the role of growth factors in EMT has not been fully established. Several integrins are upregul...

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

W, Xiao Y, Wang Ey, Lau J, Luo N, Yao C, Shi L, Meza H, Tseng Y, Maeda P, Kumaresan ...

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...

Inhibition of tissue factor signaling suppresses tumor growth.

Hh, Versteeg F, Schaffner M, Kerver Hh, Petersen J, Ahamed B, Felding-Habermann Yoshikazu Takada Bm, Mueller W, Ruf

Published in Blood

Coagulation activation by tissue factor (TF) is implicated in cancer progression, cancer-associated thrombosis and metastasis. The role of direct TF signaling pathways in cancer, however, remains incompletely understood. Here we address how TF contributes to primary tumor growth by using a unique pair of isotype-matched antibodies that inhibit eith...

Potential role of kringle-integrin interaction in plasmin and uPA actions (a hypothesis).

Yoshikazu Takada

Published in Journal of Biomedicine and Biotechnology

We previously showed that the kringle domains of plasmin and angiostatin, the N-terminal four kringles (K1-4) of plasminogen, directly bind to integrins. Angiostatin blocks tumor-mediated angiogenesis and has great therapeutic potential. Angiostatin binding to integrins may be related to the antiinflammatory action of angiostatin. We reported that ...

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

M, Majumdar T, Tarui B, Shi N, Akakura W, Ruf 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...

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

M, Fujita Yk, Takada Yoshikazu Takada

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 ...