Incyte Pharmaceuticals, Inc.

Mayo Foundation for Medical Education and Research

University of Kansas

Invitron Limited

Randy W Scott

Joffre B Baker

Craig G Wilde

Gerald J Gleich

Michael P McGrogan

Richard A Berg

Fred Golini

Christian C Simonsen, Sr

Several natural polypeptides (basophil granule proteins, 'BGP') derived from the cytoplasmic granules of human basophils, and modified forms thereof, are described. These polypeptides, the DNA which encodes them and antibodies which recognize them, are useful as diagnostics for, and treatments for, pathologies involving inflammatory and IgE-mediated responses, parasitic and helminthic infections, hypersensitivity reactions and certain types of leukocytic leukemias.

Basophil granule proteins

DNA segments encoding two slightly different protease nexin I forms (PN-I.alpha. and PN-I.beta.) are cloned and expressed to provide practical quantities of PN-I for diagnostic and therapeutic use. PN-I is a serine protease inhibitor useful in controlling conditions mediated by proteolytic activity.

Recombinant purified protease nexin

One or more amino acid residues within the reactive site region of protease nexin-I are altered in order to create analogs or variants of protease nexin-I. These analogs have substantially different protease specificities as well as different effects on regulating the activity of proteolytic enzymes which enzymes have substantial effects on a number of different physiological functions. Formulations containing the protease nexin-I variants and methods for administering these formulations to obtain desirable therapeutic results are disclosed.

Protease nexin-I variants

Recombinant molecule encoding human protease nexin

A method of treating wound healing with a composition containing protease nexin-I (PN-I) is disclosed. Compositions comprised of PN-I uniformly dispersed throughout a pharmaceutically acceptable carrier are disclosed as are such compositions further comprising antibiotics. Wound dressings are taught which are comprised of a support base having an absorbent area thereon which has PN-I absorbed thereon and which absorbent area is surrounded by a pressure sensitive adhesive strip for adhering the dressing to a surface surrounding the wound to be treated.

Use of protease nexin-I in wound dressings

One or more amino acid residues within the reactive site region of protease nexin-I are altered in order to create analogs or variants or protease nexin-I. These analogs have substantially different protease specificities as well as different effects on regulating the activity of proteolytic enzymes which enzymes have substantial effects on a number of different physiological functions. Formulations containing the protease nexin-I variants and methods for administering these formulations to obtain desirable therapeutic results are disclosed.

Protease nexin-I variants which inhibit elastase

A method of treating wound healing with a composition containing protease nexin-I (PN-I) is disclosed. Compositions comprised of PN-I uniformly dispersed throughout a pharmaceutically acceptable carrier are disclosed as are such compositions further comprising antibiotics. Occlusive wound dressings are taught which are comprised of a support surface having an absorbent area thereon which has PN-I absorbed thereon and which absorbent area is surrounded by a pressure sensitive adhesive strip for adhering the dressing to a surface surrounding the wound to be treated.

Use of protease nexin-I to mediate wound healing

The gene encoding protease nexin I (PN-I) is cloned and expressed to provide practical quantities of PN-I for diagnostic and therapeutic use. PN-I is a serine protease inhibitor useful in controlling conditions mediated by proteolytic activity.

Purified protease nexin

The gene encoding protease nexin I (PN-I) is cloned and expressed to provide practical quantities of PN-1 for diagnostic and therapeutic use. PN-I is a serine protease inhibitor useful in controlling conditions mediated by proteolytic activity.

Growing community of inventors

Sunnyvale, CA, United States of America

Randy W Scott