The present invention provides an in vitro method for identifying a compound that promotes endothelial cell adhesion, endothelial cell spreading, endothelial cell migration and/or endothelial cell proliferation for the manufacture of a diagnostic or therapeutic agent. The present invention further provides the identified compounds and pharmaceutical compositions, and assays and kits for identifying a compound or using a compound that promotes endothelial cell adhesion, endothelial cell spreading, endothelial cell migration and/or endothelial cell proliferation and is useful for bioprinting.

A pharmaceutical composition for preventing or treating cartilage diseases, and pharmaceutical preparation that includes the pharmaceutical composition as an active ingredient are provided. The pharmaceutical composition includes, as an active ingredient, at least one of an integrin beta-like 1 (ITGBL1) protein, ITGBL1 DNA or RNA encoding the ITGBL1 protein.

The invention relates to thioether monomer and dimer peptide molecules which inhibit binding of α4β7 to the mucosal addressing cell adhesion molecule (MAdCAM) in vivo.

Modified integrin polypeptides are provided. Methods of identifying binding agents that bind to a modified integrin polypeptide are also provided.

The present invention relates to low affinity dual chimeric antigen receptors (CARs), which provide cytotoxicity against heterogenous tumors and alleviate on-target, off-tumor toxicities. The dual CARs are constructed to have two binding domains bearing reduced affinities of 50 nM to 50 μM, one of which is the inserted or I domain of the α.sub.L subunit of Lymphocyte function-associated antigen-1, and the other one is scFv of EpCAM antibody. The dual CAR T cells of the present invention provide enhanced anti-tumor activity and reduced rate of tumor relapse.

A peptide or salt thereof includes an amino acid sequence set forth in SEQ ID NO:1 containing an amino acid sequence in which at least one of (a) the first aspartate residue and the second aspartate residue from the N-terminus, or (b) the 17th glycine residue and the 18th aspartate residue from the N-terminus is deleted. A peptide or salt thereof includes an amino acid sequence set forth in SEQ ID NO:5 containing an amino acid sequence in which the sixth aspartate residue from the N-terminus is substituted with another amino acid residue. The peptides or salts thereof include three specific serine residues of which at least two serine residues are phosphorylated, and have an action of inhibiting biotissue calcification.

The present invention relates to fusion proteins suitable for use as a medicament or research tool. Therapeutic uses of the fusion proteins may include the prevention or treatment of acute or chronic inflammatory and immune system-driven organ and micro-vascular disorders, for example, acute kidney injury, acute myocardial infarction, acute respiratory distress or chronic obstructive pulmonary disease fibrosis and other organ injuries resulting from tissue trauma and acute and chronic injury.

The present invention provides engineered platelets with chimeric platelet receptors (CPR) with a desired target specificity. Additionally, the engineered platelets may comprise cargo which may be released upon activation of the platelet. Additionally, the platelets may be generated in vitro from megakaryocytes engineered to generate non-thrombogenic platelets.

The methods and compositions described herein address the need in the art by providing peptides and polypeptides comprising a growth factor binding domain. In some embodiments, the peptides have an amino acid sequence that is at least 80% identical to one of SEQ ID NOS:1-7, 13-15, 49-50, or 66-70, or a fragment thereof; wherein the peptide is less than 300 amino acids in length.

The present invention relates to a biologic that inhibits angiogenesis. In particular, the present invention relates to fusion proteins that inhibit the integrin activated pathway and one other angiogenic factor-activated pathway as well as formulation compositions of such fusion proteins, as well as methods for producing and using the same.