Soluble molecule related to but distinct from ICAM-1

Drug – bio-affecting and body treating compositions – Designated organic active ingredient containing – Peptide containing doai

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530350, A61K 3817, C07K 14705

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active

058496998

ABSTRACT:
The present invention relates to a soluble form of intercellular adhesion molecule (sICAM-1) and purified and isolated human sICAM-1. This invention also relates to a purified and isolated DNA sequence encoding sICAM-1. The extracellular domain of sICAM-1 and insoluble ICAM-1 are substantially the same. ICAM-1 is involved in the process through which lymphocytes attach to cellular substrates during inflammation and serves as the major human rhinovirus receptor (HRR). sICAM-1 therefore has both the property of reducing immune inflammation and inhibiting infection of rhinovirus and Coxsackie A virus.

REFERENCES:
Staunton et al 1989 Cell 56(5):849-853.
Cole et al. 1986. Topographic local of leparin binding domain of the NCAM. J. Cell Biol. 103 1739-1744.
Gussow & Pleogh, 1987, Soluble class/outigens: a conundrum with no solutions? Immunol Today 8:220.
Scopes, R.R. Protein Protein Purification: Principles and Practice.
Springer-Verlag, new york 1982, pp. 39-43.
Bothlein et al. 1986. A human ICAM-1 distinct from F7A-1 J. Immunol. 137:1270-1274.
Marlin & Springer, 1987. Purified ICAM-1 is a ligend for lymphocyte function associated antigen 1. Cell 51:813-819.
Gough. 1987. Putting a stop to an immunoglobulin message, Trends in Genet. 3:238.
Staunton et al. 1988. Primary structure of ICAM-1 demon. interact. betw. members of the Immunogl. & Integrin Supergene Families Cell 52:925-933.
Bock et al 1987. Characterization of soluble forms of NCAM FEBS letters 255:33.
Gower et al 1988. Alternative Splicing Generates a Secreted form of NCAM in muscle and brain. Cell 55:955.
Simmons et al 1988. ICAM, an adhesion ligand of LFA-1, is homol. to NCAM. Nature 331:624-627.
Cunningham et al. Neural Cell Adhesion Molecule: Structure, Immuno. like Domains, Cell surf. Mod., and Alt. RNA Spl. Science, 236:799.
Journal of Virology, vol. 58, No. 2, May 1986, pp. 290-295, J.E. Tomassini et al.; Isolation of a receptor protein involved in attachment of human rhinoviruses.

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