JEFFREY A WHITSETT, MD
Medical Practice at Medical Village Dr, Covington, KY

2006007, Apr 13, 2006

Feb 5, 2004

10/772716

Jeffrey Whitsett - Cincinnati OH, US

A61K 48/00, A61K 39/395

424143100, 514044000, 514002000

The present invention provides methods to protect a subject from a respiratory disorder involving an airway obstructive disease such as asthma or chronic obstructive pulmonary disease. Provided are methods to protect a subject from an airway obstructive disease using gene therapy. Methods are provided for supplying FoxA2 function to cells of the lung and airway, such as smooth muscle and epithelial cells, by FoxA2 gene therapy. The FoxA2 gene, a modified FoxA2 gene, or a part of the gene may be introduced into the cell in a vector such that the gene remains extrachromosomal or may be integrated into the subjects chromosomal DNA for expression. These methods provide for administering to a subject in need of such treatment a therapeutically effective amount of a FoxA2 gene, or pharmaceutically acceptable composition thereof, for overexpressing the FoxA2 gene. Such methods of expressing the administered FoxA2 gene in the lungs and airway provide for: (1) preventing or alleving bronchial hyperresponsiveness; (2) preventing or alleving of an airway obstructive disease, e.g., bronchial hyperreactivity, airway hyperresponsiveness, asthma or chronic obstructive pulmonary disorder (“COPD”); (3) reducing the airway resistance response to inhaled natural or synthetic bronchoconstrictors or allergens or to exercise; and (4) enhancing responsiveness (relaxation) of airway tissues to β-agonists.

5387746, Feb 7, 1995

Nov 12, 1992

7/975202

Jeffrey A. Whitsett - Cincinnati OH

Scios Nova Inc. - Mountain View CA

A61K 3702, C07K 710

514 12

A novel hydrophobic surfactant-associated protein mixture, i. e. , a SAP-6 proteins, has been isolated from pulmonary animal tissue. A small, novel pulmonary hydrophobic surfactant-associated SAP-6-Val protein having a molecular weight of about 6,000 daltons as determined by SDS-PAGE and about 3,500-4,000 daltons as determined by tricine-SDS-PAGE has been further isolated from the SAP-6 protein mixture. The amino acid residue compositions of the SAP-6-Val protein for human and bovine have been determined and disclosed. When a SAP-6-Val protein is combined with phospholipids, it enhances the surfactant-like activity of the phospholipids in lungs of animals and, therefore, uniquely imparts to the mixture significant pulmonary biophysical activity. Such a mixture results in enhanced adsorption of the phospholipids with properties similar to that of natural pulmonary surfactant material. SAP-6-Val proteins in combination with phospholipids is highly useful for replacing or supplementing natural pulmonary surfactant material for reducing or maintaining normal surface tension in lungs, and especially in lungs of patients suffering from hyaline membrane disease, HMD, or other syndromes associated with the lack or insufficient amounts of natural pulmonary surfactant material.

6838428, Jan 4, 2005

Apr 26, 2000

09/558576

Jeffrey A. Whitsett - Cincinnati OH, US

Children's Hospital Medical Center - Cincinnatti OH

A61K 3800, A61K 3542

514 2, 514 12, 514 14, 514 13, 514888, 424557, 435 691, 435 697

Surfactant protein D (SP-D) is a 43-kDa member of the collectin family of collagenous lectin domain-containing proteins that is expressed in epithelial cells of the lung. The SP-D gene was targeted by homologous recombination in embryonic stem cells that were used to produce SP-D (−/−) mice. The SP-D (−/−) deficiency caused inflammation, increased oxidant production by isolated alveolar macrophages, abnormal surfactant structure and levels, and decreased SP-A expression. Therefore, disclosed is the SP-D (−/−) mouse as an excellent model for emphysema. Also included are models for testing emphysema therapies in the mouse model, methods for using SP-D protein or DNA as a treatment for emphysema and pulmonary infections, and diagnosis.

5013720, May 7, 1991

Apr 4, 1990

7/504691

Jeffrey A. Whitsett - Cincinnati OH

Abbott Laboratories

C07K 1300, C07K 710, A61K 3700

514 12

A novel hydrophobic surfactant-associated protein mixture, i. e. , a SAP-6 proteins, has been isolated from pulmonary animal tissue. A small, novel pulmonary hydrophobic surfactant-associated SAP-6-Val protein having a molecular weight of about 6,000 daltons as determined by SDS-PAGE and about 3,500-4,000 daltons as determined by tricine-SDS-PAGE has been further isolated from the SAP-6 protein mixture. The amino acid residue compositions of the SAP-6-Val protein for human and bovine have been determined and disclosed. When a SAP-6-Val protein is combined with phospholipids, it enhances the surfactant-like activity of the phospholipids in lungs of animals and, therefore, uniquely imparts to the mixture significant pulmonary biophysical activity. Such a mixture results in enhanced adsorption of the phospholipids with properties similar to that of natural pulmonary surfactant material. SAP-6-Val proteins in combination with phospholipids is highly useful for replacing or supplementing natural pulmonary surfactant material for reducing or maintaining normal surface tension in lungs, and especially in lungs of patients suffering from hyaline membrane disease, HMD, or other syndromes associated with the lack or insufficient amounts of natural pulmonary surfactant material.

2008019, Aug 14, 2008

Mar 26, 2004

10/551105

Jeffrey Allen Whitsett - Cincinnati OH, US

A61K 38/16, C12N 15/66, C12N 5/00, A61P 11/00

514 12, 4353201, 435325

The use of fibroblast growth factor (FGF)- protein, certain of its downstream target genes and respective expressed proteins, in particular sonic hedgehog (Shh), Shh protein, β-catenin, β-catenin protein, and the Wnt family of proteins that stimulate β-catenin, and the respective nucleotide sequences encoding this protein, particularly for inducing cartilage formation, particularly for the purpose of generating, repairing, reconstructing, or de novo formation of, cartilaginous tissue. Therapies for which FGF- and the target proteins are useful include repair and reconstruction of various tissues in conducting airways such as the trachea, bronchi, lung and larynx caused by, for example, tracheal-bronchial abnormalities, tracheal-laryngo or bronchial malaria. Other therapies for which FGF- and the target proteins would be useful include other cartilaginous tissues, such as those of joint and skeletal tissue caused by, for example, arthritis and meniscus abnormalities in joints.

5976873, Nov 2, 1999

May 17, 1995

8/442809

Robert J. Bohinski - Cincinnati OH
Jeffrey A. Whitsett - Cincinnati OH

Children's Hospital Medical Center - Cincinnati OH

C12N 1563, C12N 1511, B32B 516

4353201

An oligonucleotide which includes at least one nucleic acid sequence which binds to at least one nuclear protein found in lung cells, such as TTF-1 protein. The oligonucleotide may be contained in a vector. The at least one nuclear protein provides for lung cell-specific expression of the vector upon binding of the at least one nucleic acid sequence to the at least one nuclear protein. Such vector may also include genes encoding therapeutic agents, and may be employed for delivering genes encoding therapeutic agents to lung cells.

2006019, Aug 31, 2006

Apr 28, 2006

11/413197

Wolfram Steinhilber - Stockach, DE
Jeffrey Whitsett - Cincinnati OH, US
Ann Levine - Cincinnati OH, US
Thomas Korfhagen - Cincinnati OH, US

A61K 38/17

514012000

Recombinant surfactant protein A and medicament compositions based thereon are useful for the prevention or treatment of pulmonary infection and inflammation.

7135452, Nov 14, 2006

Jan 18, 2000

09/889348

Wolfram Steinhilber - Stockach, DE
Jeffrey A. Whitsett - Cincinnati OH, US
Ann Marie Levine - Cincinnati OH, US
Thomas R. Korfhagen - Cincinnati OH, US

Altana Pharma AG - Constance

A61K 38/00, C12N 15/00

514 2, 435 691, 514 12, 514885

Recombinant surfactant protein A and pharmaceutical compositions based thereon are useful for the prevention or treatment of pulmonary infection and inflammation.