Anamar Medical Ab

Anamar Ab

Nordic Boiscience A/s

Nordic Bioscience A/s

Pilar Lorenzo

Dick Heinegard

Dick Heinegård

Tore Saxne

Emma Åhrman

Patrik Önnerfjord

Dick Heineg{dot Over (a)}rd

The present embodiments relate to methods for determining or detecting pathological cartilage turnover by detection of Cartilage Oligomeric Matrix Protein (COMP) neoepitopes, both released into body fluids and present in the tissue. Furthermore the embodiments relate to antibodies against COMP neoepitopes and to fragments and peptides containing COMP neoepitopes for generation of such antibody.

Determining pathological cartilage turnover

A method for differentiation of osteoarthritis from rheumatoid arthritis and non-disease conditions in a sample, comprising measuring in the sample the concentration of human cartilage intermediate layer protein 2 (CILP-2) in body fluids and more specifically, measuring in the sample the concentration of the N-terminal part of CILP-2 (2C1) or fragments thereof.

Cartilage intermediate layer protein 2 C1 and its use to differentiate osteoarthritis from rheumatoid arthritis and non-disease conditions

A method for differentiation of osteoarthritis from rheumatoid arthritis and non-disease conditions in a sample, comprising measuring in the sample the concentration of human cartilage intermediate layer protein 2(CILP-2) in body fluids and more specifically, measuring in the sample the concentration of the N-terminal part of CILP-2 (2C1) or fragments thereof.

A novel, N-oligosaccharide-substituted-specific protein of approximately 91.5 kDa was purified from extracts of human articular cartilage and designated Cartilage Intermediate Layer Protein (CILP). The protein is a chondrocyte product which is deposited in the interterritorial matrix. The gene encoding CILP, as well as its mRNA, were isolated and characterized. A single 4.2 kb mRNA detected in human articular cartilage encodes a polypeptide of 1184 amino acids with a calculated molecular weight of 132.5 kDa. The protein has a putative signal peptide of 21 amino acids, and is a proform of two polypeptides. The amino-terminal half corresponds to CILP (molecular weight of 78.5 kDa, not including post-translational modifications) and the carboxy-terminal half corresponds to a protein homologous to a porcine nucleotide pyrophosphohydrolase, NTPPHase (molecular weight of 51.8 kDa, not including post-translational modifications).

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Lund, Sweden

Pilar Lorenzo