Phoenix Pharmaceuticals, Inc.

Other

University of California

Leland Stanford Junior University

Peninsula Laboratories, Inc.

Jaw-Kang Chang

Rong-Ming Lyu

Nancy M Lee

Horace H Loh

Ding Chang

Edward Tak Wei

Karl A Folkers

Jack D Barchas

Conny B Bogentoft

Michael D Culler

Bruce L Currie

Eckard Weber

Christopher J Evans

Hans Sievertsson

Yoshio Hosobuchi

Kevin A Roth

Robin G Lorenz

Akira Arimura

Human phoenixin peptides, analogs and mimetics useful in production of anti-phoenixin antibodies, diagnostic screening and assays, and in modulating cellular concentration of cAMP, and treatment of disorders related to cAMP or Caconcentration in cells, modulating hypertension and cardiovascular function, modulating gonadotrophs and gastric emptying.

Diagnostic kit

Phoenixin peptides

Cell permeable bioactive peptide conjugates having a first bioactive peptide region coupled to a second transport peptide region allowing transfer of the first bioactive peptide region and the second transport peptide region across biological membranes to enter intact living cells for regulation of biological responses.

Cell permeable bioactive peptide conjugates

Stable water soluble polypeptides which are potent inhibitors of endothelial cell proliferation and of angiogenesis. Polypeptide inhibitors of endothelial cell growth may have important uses in the elucidation of the mechanism of angiogenesis, disease diagnosis and prognostication, and drug therapies for use in animals and humans.

Angiogenesis regulation system

Cell growth regulation system

Biologically active atrial peptide analogs having 21 or 22 amino acid residues are provided with potent diuretic and natriuretic activities, and which lower blood pressure. These analogs have a .beta.-mercaptopropanoic acid derivative moiety at the N-terminus and have D-Alanine at the 3 position of the amino acid sequence.

Potent synthetic atrial peptide analogs

A method of treatment for patients suffering from cerebral ischemia is provided by administering an opioid peptide. Particulary preferred is the administration of dynorphin, or dynorphin-related peptides, in the acid or amidated form. Practice of the invention is useful in prolonging survival.

Method of treating cerebral ischemia

Novel peptides having gastrin releasing peptide-like activity having the structures Ala-Pro-Val-Ser-Val-Gly-Gly-Gly-Thr-Val-Leu-Ala-Lys-Met-Tyr-Pro-NH.sub.2 and Gly-Asn-His-Trp-Ala-Val-Gly-His-Leu-Met-NH.sub.2, have been isolated from rat and guinea pig brain extracts and synthesized by a solid phase peptide synthesis methods. The GRP-like peptides are useful as pharmaceuticals to lower body temperature, increase respiratory activity, reduce food intake, stimulate pancreatic hormone release, stimulate pituitary hormone release and suppress thyroid hormone release in mammals.

Gastrin releasing peptide-like peptides

A synthetic peptide growth hormone releasing factor having substantially the following amino acid sequence: ##STR1## methods of inducing growth in an animal and growth inducing pharmaceutical compositions, including animal feed compositions, are disclosed.

Synthetic peptides

A method is provided for treating high blood pressure and disturbances of cardiac function by administering a therapeutically effective dosage of dynorphin-related opioid peptides, such as dynorphin(1-13) and dynorphin(1-10) amide, having at least ten amino acids linked sequentially by peptide bonds and with the five amino acids from the N-terminal end being the same as, or mimicking, Leu-enkephalin. Administration may be over a period of time, as for individuals with chronic high blood pressure, and may be by dispensing the medicament in aerosol form.

Method for controlling blood pressure

Dynorphin(1-13) has been previously reported to antagonize the analgesia induced by narcotics in naive hosts. Novel compounds are provided which differ from dynorphin(1-13) by neither potentiating nor antagonizing narcotics, such as morphine, in naive animals. In tolerant hosts the new compounds potentiate narcotic or peptide induced analgesia, and in addition are less susceptible to degradation than dynorphin(1-13). Particularly preferred of the new compounds are polypeptides having ten amino acids with nitrogen containing moieties at both termini.

Dynorphin amide analogs

A synthetic decapeptide, L-pglutamyl-L-histidyl-L-tryptophanyl-L-seryl-L-tyrosyl-glycyl-L-leucyl-L- arginyl-L-prolyl-glycinamide which has the hormonal activities of the luteinizing hormone releasing hormone (LRH) of the hypothalamus gland of mammals is produced by utilizing as the key starting materials, the amino acids, glutamic acid or pyroglutamic acid, histidine, tryptophan, serine, tyrosine, glycine, leucine, arginine, and proline. Synthesis of the decapeptide is accomplished by coupling, in appropriate combinations of appropriate protected forms of the amino acids, and finally deprotecting to yield the amide, L-pglutamyl-L-histidyl-L-tryptophanyl-L-seryl-L-tyrosyl-glycyl-L-leucyl-L- arginyl-L-prolyl-glycinamide.

Growing community of inventors

San Carlos, CA, United States of America

Jaw-Kang Chang