Disease relevance of PMP2

• Experimental allergic neuritis (EAN) was induced in Lewis rats by injection of 'SP26', a peptide homologous to amino acids 53-78 of bovine myelin P2 protein, in complete Freund's adjuvant [1].

High impact information on PMP2

• X-ray analyses of the structure of two family members, rat intestinal fatty acid-binding protein and bovine myelin P2 protein, indicate that they have a high degree of conformational similarity and that the carboxylate group of their bound fatty acid interacts with a delta-guanidium group of at least 1 of 2 "buried" arginine residues [2].
• The data revealed extensive sequence homology of mammary-derived growth inhibitor to a family of low molecular mass hydrophobic ligand-binding proteins, among them a fatty acid-binding protein from rat heart, myelin P2, a differentiation associated protein in adipocytes (p422) and the cellular retinoic acid-binding protein [3].
• Bovine peripheral nervous system myelin P2 protein: chemical and immunological characterization of the cyanogen bromide peptides [4].
• Induction of severe experimental autoimmune neuritis with a synthetic peptide corresponding to the 53-78 amino acid sequence of the myelin P2 protein [5].
• Structure of myelin P2 protein from equine spinal cord [6].

Biological context of PMP2

• Polyclonal rabbit antiserum raised against mammary derived growth inhibitor cross-reacts with bovine heart fatty acid binding protein and bovine peripheral myelin P2 protein [7].

Anatomical context of PMP2

• Peptide 53-78 of myelin P2 protein is a T cell epitope for the induction of experimental autoimmune neuritis [8].

Analytical, diagnostic and therapeutic context of PMP2

• The secondary structure of myelin P2 protein derived by secondary structure prediction methods, circular dichroism, and 400-MHz 1H-NMR spectroscopy: implications for tertiary structure [9].

References