U.S. Patent No. 6,399,349

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Dr. James Ryan, who sequenced the gene XPNPEP2 that codes for an important protein, membrane-bound aminopeptidase P (AmP), has received US Patent No. 6,399,349 entitled “Human Aminopeptidase P Gene” on June 4, 2002.

This gene (XPNPEP2) is disposed on chromosome X at q25. The coded protein, membrane-bound AmP is a hydrolase, specific for N-terminal imido bonds, which are common to several collagen degradation products, neuropeptides, vasoactive peptides, and cytokines. It is a significant marker for hypertension, angioedema, rejection of kidney transplants, certain tumors and other diseases.

This valuable patent covers cDNA and gDNA sequences coding AmP, a method of producing AmP, the diagnostics for detecting AmP abnormalities, and prevention and treatment of medical conditions associated with the mutation of the AmP gene, in particular, mutations that play a role in angioedemas of all types, including angiotensin converting enzyme inhibitor-induced angioedema.

U.S. Patent No. 7,273,718

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US Patent No. 7,273,718, entitled "Isolated Genomic Polynucleotide Fragments from Chromosome 10q25.3 that Encode Human Soluble Aminopeptidase P", was issued on September 25, 2007.

The '718 patent covers an isolated genomic polynucleotide fragment that encodes human soluble (cytosolic) aminopeptidase P, vectors and hosts containing the fragment and fragments hybridizing to noncoding regions, as well as antisense oligonucleotides to these fragments, and methods of using these fragments to obtain human soluble aminopeptidase P to diagnose, treat, prevent and/or ameliorate a pathological disorder. Searches for nucleotide variants within the gene are enabled by specific claims.

Human soluble aminopeptidase P, an aminoacylprolyl peptidyl hydrolase, catalyzes the removal of the N-terminal amino acid from peptides in which the second residue is proline. It is believed to act physiologically by degrading peptide hormones such as bradykinin and substance P and collagen-related peptides that have N-terminal sequences of the type Xaa-Pro-Hyp-. A functionally-related enzyme is membrane-bound aminopeptidase P, the gene for which (XPNPEP2) is disposed at chromosome Xq25. The membrane-bound enzyme is disposed, via a glycosylphosphatidylinositol lipid anchor, as an ectoenzyme on endothelia and epithelia. Soluble aminopeptidase P is disposed intracellularly in virtually all cell types, including astrocytes, lymphocytes, platelets and chromaffin cells. A form of mental retardation has been associated with subnormal concentrations of aminopeptidase P activity.

U.S. Patent No. 7,468,266

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U.S. Patent No. 7,468,266 entitled “Isolated genomic polynucleotide fragments that encode human lipoprotein-associated phospholipase A2” was awarded on December 23, 2008.

The patented gene is disposed on chromosome 6 at p21.2. Human lipoprotein-associated phospholipase A2, also known as Platelet Activating Factor Acetyl Hydrolase (PAF acetyl hydrolase), is one of a family of enzymes that catalyze release of fatty acids from membrane phospholipids and can thereby initiate synthesis of pro-inflammatory mediators. During the conversion of LDL to its oxidized form, lipoprotein-associated phospholipase A2 is responsible for producing lyso-phosphatidylcholine and an oxidatively modified fatty acid. Both of these products of lipoprotein-associated phospholipase A2 action are potent chemoattractants for circulating monocytes. The enzyme may play a central role in the development of atherosclerosis and is regarded as an independent risk factor for coronary artery disease. Specifically, this enzyme is thought to be responsible for the accumulation of cells loaded with cholesterol ester in the arteries, causing the characteristic `fatty streak` associated with the early stages of atherosclerosis.
Concentrations of PAF acetylhydrolase are altered in several disease states, such as systemic lupus erythematosus, stroke and asthma.

U.S. Patent No. 7,470,522

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U.S. Patent No. 7,470,522, titled "Isolated genomic polynucleotide fragments encoding human resistin and the human syntaxin binding protein 2” was granted on December 30, 2008.

This patent covers the resistin gene, which is disposed on chromosome 19 at p13.3 – 13.2. The protein product interferes with the actions of insulin on liver and muscle. It is found largely in white adipose tissue and in crypt epithelium of the intestine. Given its disposition in fatty tissue and its inhibition of insulin effects, resistin appears to link obesity to type 2 diabetes. Consistent with this view, antibodies to resistin improve blood sugar levels and insulin actions in mice with diet-induced obesity. Conversely, administration of recombinant resistin impairs glucose tolerance and insulin actions. The resistin cDNA is identical to the cDNAs for entities called FIZZ3 and C/EBP-epsilon regulated myeloid-specific secreted cysteine-rich protein precursor.

U.S. Patent No. 7,588,915

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U.S. Patent No. 7,588,915 titled “Isolated Genomic Polynucleotide Fragments from Chromosome 7” was granted on September 15, 2009.

The patent covers isolated genomic polynucleotide fragments that encode Human Adipocyte Enhancer Binding Protein 1 (AEBP1), its complement polynucleoptides, vectors and hosts containing these fragments and a method for obtaining AEBP1.

Adipocyte Enhancer Binding Protein 1 binds to a regulatory sequence, adipocyte enhancer 1 (AE-1), located in the promoter region of the adipose P2 (aP2) gene, which encodes the adipocyte fatty-acid binding protein. It is thought to play a role in diabetes and metabolic syndrome, obesity, inflammation, immune processes, differentiated vascular smooth muscle cells, and atherogenesis.

The patents listed above cover large segments of human chromosomes X, 6, 10 and 19; segments critical to any and all whole genome surveys as well as commercial studies of the target genes of the patents. All are available for licensing.

Ryogen’s IP portfolio includes patent applications currently pending before the US Patent and Trademark Office. These applications are directed to genes that play important roles in various cancers, diabetes and obesity, hepatitis C, atherosclerosis, Alzheimer’s and several other diseases.