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Inhaled Corticosteroid Replacement Study - Efficacy and Safety of Ro 27-2441 (Test Drug) in Moderate Persistent Asthma

2014-08-27 03:55:41 | BioPortfolio

Summary

The primary objective of the study is to evaluate the anti-inflammatory action and safety of Ro 27-2441 (study drug) in asthmatic patients currently taking inhaled corticosteroids. The research is being conducted at up to 40 clinical research sites in the US. Study participants will have a number of visits to a research site over a 4-month period.

Study Design

Primary Purpose: Treatment

Conditions

Asthma

Intervention

Dual Integrin Antagonist

Location

Huntington Beach
California
United States
92647

Status

Completed

Source

Hoffmann-La Roche

Results (where available)

View Results

Links

Published on BioPortfolio: 2014-08-27T03:55:41-0400

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Medical and Biotech [MESH] Definitions

An integrin alpha subunit that primarily associates with INTEGRIN BETA1 or INTEGRIN BETA4 to form laminin-binding heterodimers. Integrin alpha6 has two alternatively spliced isoforms: integrin alpha6A and integrin alpha6B, which differ in their cytoplasmic domains and are regulated in a tissue-specific and developmental stage-specific manner.

An integrin beta subunit of approximately 85-kDa in size which has been found in INTEGRIN ALPHAIIB-containing and INTEGRIN ALPHAV-containing heterodimers. Integrin beta3 occurs as three alternatively spliced isoforms, designated beta3A-C.

An integrin alpha subunit that binds COLLAGEN and LAMININ though its I domain. It combines with INTEGRIN BETA1 to form the heterodimer INTEGRIN ALPHA1BETA1.

An integrin alpha subunit that primarily combines with INTEGRIN BETA1 to form the INTEGRIN ALPHA2BETA1 heterodimer. It contains a domain which has homology to collagen-binding domains found in von Willebrand factor.

This integrin alpha subunit combines with INTEGRIN BETA1 to form a receptor (INTEGRIN ALPHA5BETA1) that binds FIBRONECTIN and LAMININ. It undergoes posttranslational cleavage into a heavy and a light chain that are connected by disulfide bonds.

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