The General Hospital Corporation

Other

Shiseido Company, Limited

Paul F Goetinck

Tadahito Takahashi

Toshihiko Hibino

Peter C Baciu

Mehrdad Tondravi

Francois Binette

M Mehrdad Tondravi

Izumi Horii

A method of modulating cell proliferation or apoptosis comprising modulating psoriastatin activity.

Two novel genes from psoriatic epidermis: psoriastatin type I and psoriastatin type II

The invention features a method of modulating, e.g., inhibiting or promoting, the spatial or positional relationship of a cell to a substrate, or modulating the intracellular response of a cell to a substrate, in vitro or in vivo. The method includes administering an agent which modulates the interaction, e.g., the binding, of the syndecan-4 ectodomain with a counterligand, thereby modulating the spatial or positional relationship of a cell to a substrate, or modulating the intracellular response of a cell to a substrate. The preferred counterligand is an ECM component, e.g., the heparin-binding domain of a component of the extracellular matrix (ECM) such as fibronectin, vitronectin, a laminin or a collagen. The invention also features methods of identifying compounds which modulate, e.g., inhibit or promote, the spatial or positional relationship of a cell to a substrate, or modulate the intracellular response of a cell to a substrate, and methods of treating a subject having a disorder characterized by unwanted or abnormal cell adhesion or spreading, e.g., cancer.

Methods of modulating cell attachment and migration

The present invention relates to a gene encoding a novel protein, syndecan-4 binding protein (S4BP), which binds to syndecan-4. S4BP polypeptides play a role in cell matrix interactions. Described herein are isolated and antisense nucleic acids molecules, recombinant expression vectors, host cells and non-human transgenic animals containing an insertion or a disruption of the S4BP gene. Diagnostic, screening and therapeutic methods utilizing the compositions of the invention are also provided.

Syndecan-4 binding protein (S4BP) and uses thereof

Purified uPA peptides having, mitogenic activity and containing as few as six amino acids of the EGF-like domain of uPA.

Urokinase plasminogen activator fragments

Link protein and cartilage matrix protein, which are two major components of the extracellular cartilage matrix, have been found to bind to each other. Polypeptide fragments of cartilage matrix protein and link protein are produced. A recombinant fusion polypeptide is prepared containing a fragment of cartilage matrix protein that binds to link protein and a fragment of link protein that binds to cartilage matrix protein. The cartilage matrix protein fragment may bind to collagen and contain the CMP-1 or CMP-2 domain, and the link protein may bind to a complex of hyaluronic acid and proteoglycan. The fragments or fusion polypeptide can be administered for repair of diseased or injured cartilaginous and non-cartilaginous tissue by promoting binding of a complex of proteoglycan and hyaluronic acid to collagen. The fragments or fusion polypeptide can be anchored to the surface of a prosthetic device, implant or tissue graft to promote adherence of tissue and biocompatibility. By anchoring a fragment of cartilage matrix protein or link protein on a surface, cartilaginous tissue, cartilage matrix protein or link protein may be attached to the surface.

Fusion polypeptide containing fragments of cartilage matrix protein and

Link protein and cartilage matrix protein, which are two major components of the extracellular cartilage matrix, have been found to bind to each other. Cartilaginous tissue is attached to a surface by anchoring on the surface a fragment of cartilage matrix protein capable of binding to link protein or to collagen and link protein, or a fragment of link protein capable of binding to cartilage matrix protein or to cartilage matrix protein and a complex or proteoglycan and hyaluronic acid, and contacting the surface with cartilaginous tissue. Cartilage matrix protein is attached to a surface by anchoring on the surface a fragment of link protein capable of binding to cartilage matrix protein, and contacting the surface with cartilage matrix protein. Link protein is attached to a surface by anchoring on the surface a fragment of cartilage matrix protein capable of binding to link protein, and contacting the surface with link protein. Human cartilage matrix protein, link protein and fragments thereof are used, and the fragments may be recombinantly made. A recombinant fusion polypeptide is prepared that contains the fragments of cartilage matrix protein and link protein. The fragments or fusion polypeptide can be administered for repair of diseased or injured cartilaginous and non-cartilaginous tissue by promoting the binding of a complex of proteoglycan and hyaluronic acid to collagen. The fragments or fusion polypeptide can also be anchored to the surface of a prosthetic device, implant or tissue graft to promote adherence of tissue and biocompatibility.

Method for attaching cartilaginous tissue, cartilage matrix protein or

DNA constructs coding for a chimeric polypeptides containing fragments of cartilage matrix proteins that can bind collagen and their protein products are described. Also, the invention relates to purified chimeric polypeptides, and methods of their production and purification from transformed cells as well as their use as agents in therapeutics and clinical imaging. In addition, the invention disclosed a method for forming collagen fibrils using the chimetic polypeptide.

Cartilage matrix protein and methods for use

DNA constructs coding for a chimeric polypeptides containing fragments of cartilage matrix proteins that can bind collagen and their protein products are described. Also, the invention relates to purified chimeric polypeptides, and methods of their production and purification from transformed cells as well as their use as agents in therapeutics and clinical imaging. In addition, the invention disclosed a method for forming collagen fibrils using the chimeric polypeptide.

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Boston, MA, United States of America

Paul F Goetinck