Leukocyte homing modulation

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

Reexamination Certificate

Rate now

  [ 0.00 ] – not rated yet Voters 0   Comments 0

Details

C514S008100, C514S023000, C514S053000, C514S054000, C514S061000, C514S062000, C530S395000, C536S001110, C536S004100, C536S017200, C536S018700

Reexamination Certificate

active

06387884

ABSTRACT:

INTRODUCTION
1. Technical Field
The field of this invention is the modulation of lymphocyte homing to provide therapies for inflammation and other pathogenic conditions associated with lymphocyte infiltration into tissue.
2. Background
The bloodstream is the pathway for numerous cells which migrate throughout the body, monitoring conditions. Cells of the lymphoid and myelomonocytic lineages act to identify foreign substances, such as pathogens, aberrant cells, and some compounds, and remove them from the system. These cells have available a large variety of mechanisms for protecting the host from the foreign substance. Many of these mechanisms are highly destructive and result in cytotoxicity of native tissue, inflammation, degradation, and the like. Mechanisms may involve the production of superoxide, secretion of various degradative compounds, such as perforans, endocytosis, etc.
While in many situations these protective mechanisms are salutary, in many other situations, they are found to have detrimental effects, involving inflammatory lesions, such as myocarditis, inflammatory bowel disease, psoriasis, allergic contact dermatitis, lichen planus, lymphoid hyperplasia in the skin, inflamed synovia, etc. There is, therefore, an interest in being able to modulate the effects of these various monitoring cells.
In recent years, it has been shown that the migrating cells have specific surface membrane proteins associated with their homing or being directed to a particular site. High endothelial venules serve as beacons for these cells, expressing proteins referred to as addressing, which bind to the “homing receptor” surface membrane proteins of the migrating cells. After binding to the high endothelial venules, the cells migrate by diapedesis, by mechanisms unknown, to the site of inflammation or injury. Therefore, by interfering with the binding between the addressin and the homing receptor, one may hope to reduce the infiltration of migrating cells into the inflamed site to prevent further aggravation of the site.
Relevant Literature
References associated with the characteristics of HECA-452 include Picker et al.,
J. Immunol.
(1990) 145:3247-3255; Raine et al.,
Clin. Immunol. Immunopathol.
(1990) 57:173-187; Jalkanen et al.,
J. Invest. Dermatol.
(1990) 94:786-792; Picker et al.,
Am. J. Pathol.
(1990) 136:1053-1068; VanDinther-Janssen et al.,
J. Rheumatol.
17:11-17; Jalkanen et al.,
Int. J. Cancer
(1989) 44:777-782; Facchetti et al.,
Immunol. Lett.
(1989) 20:277-281; Seldenrijk et al.,
Gut
(1989) 30:46-491; Kabl et al.,
J. Clin. Endocrinol. Metab.
(1989) 62:744-751; van der Valk et al.,
Am. J. Surg. Pathol.
(1989) 13:97-106; Duijvestijn et al.,
Am. J. Pathol.
(1988) 130:147-155; and Graber et al.,
J. Immunol.
(1990) 145:819-830.
Lowe et al.,
Cell
(1990) 63:475-484; Phillips et al.,
Science
(1990) 250:1130-1132; Walz et al.,
Science
(1990) 250:1132-1135; and Goelz et al.,
Cell
(1990) 63:1349-1356, report a neutrophil carbohydrate ligand for ELAM-1 as NeUAc&agr;2,3-gal&bgr;1-4 [Fuc&agr;1,3]GlcNac, the sialylated-Lewis X antigen, or sialylated lacto-N-fucopentaose III (sLNFIII).


REFERENCES:
patent: 4471057 (1984-09-01), Koprowski et al.
patent: 4851511 (1989-07-01), Hakomori et al.
patent: 4859769 (1989-08-01), Karlsson et al.
patent: 4876199 (1989-10-01), Hakomori
patent: 5143712 (1992-09-01), Brandley et al.
patent: 5211937 (1993-05-01), Brandley et al.
patent: 5538724 (1996-07-01), Butcher et al.
patent: 5723583 (1998-03-01), Seed et al.
patent: 408 859 (1991-01-01), None
patent: WO 90/13300 (1990-11-01), None
patent: WO 91/19502 (1991-12-01), None
patent: WO 92/01718 (1992-02-01), None
patent: WO 92/07572 (1992-05-01), None
Edgington, Biotechnology, 10: 383-389, May 1992.*
Ward et al., Therapeutic Immunology, 1: 165-171, Jan. 1994.*
Baeckström et al., “Purification and Characterization of a Membrane-bound and a Secreted Mucin-type Glycoprotein Carrying the Carcinoma-associated Sialyl-LeaEpitope on Distinct Core Proteins,”J. Biol. Chem. 266(32):21537-21547, 1991.
Berg et al., “The Cutaneous Lymphocyte Antigen Is a Skin Lymphocyte Homing Receptor for the Vascular Lectin Endothelial Cell-Leukocyte Adhesion Molecule 1,”J. Exp. Med. 174:1461-1466, 1991.
Berg et al., “A Carbohydrate Domain Common to Both Sialyl Leaand Sialyl LexIs Recognized by the Endothelial Cell Leukocyte Adhesion Molecule ELAM-1,”J. Biol. Chem. 266(23): 14869-14872, 1991.
Bird and Kimber, “Oligosaccharides Containing Fucose Linked &agr;(1-3) and &agr;(1-4) to N-Acetylglucosamine Cause Decompaction of Mouse Morulae,”Devel. Biol. 104:449-460, 1984.
Bowen et al., “Characterization of a Human Homologue of the Murine Peripheral Lymph Node Homing Receptor,”Journal of Cell Biology 109:421-427, 1989.
Brandley et al., “Carbohydrate Ligands of LEC Cell Adhesion Molecules,”Cell 63:861-863, 1990.
Broquet et al., “Effect of Desipramine on a Glycoprotein Sialyltransferase Activity in C6 Cultured Glioma Cells,”J. Neurochem. 54:388-394, 1990.
Childs et al., “High-molecular-weight glycoproteins are the major carriers of the carbohydrate differentiation antigens I, i and SSEA-1 of mouse teratocarcinoma cells,”Biochem. J. 215:491-503, 1983.
Ching and Rhodes, “Purification and Characterization of a Peanut-Agglutinin-Binding Pancreatic-Cancer-Related Serum Mucus Glycoprotein,”Int. J. Cancer 45:1022-1027, 1990.
Corral et al., “Requirement for Sialic Acid on Neutrophils in a GMP-140 (PADGEM) Mediated Adhesive Interaction with Activated Platelets,”Biochem. Biophys. Res. Commun. 172:1349-1356, 1990.
Duijvestijn et al., “High Endothelial Differentiation in Human Lymphoid and Inflammatory Tissues Defined by Monoclonal Antibody HECA-452,”Am. J. Path. 130:147-155, 1988.
Eggens et al., “A Role of Carbohydrate-Carbohydrate Interaction in the Process of Specific Cell Recognition During Embryogenesis and Organogenesis: A Preliminary Note,”Biochem. Biophys. Res. Commun. 158(3):913-920, 1989.
Eggens et al., “Specific Interaction between Lexand LexDeterminants. A Possible Basis for Cell Recognition in Preimplantation Embryos and in Embryonal Carcinoma Cells,”J. Biol. Chem. 264(16):9476-9484, 1989.
Fenderson et al., “The blood group I antigen defined by monolconal antibody C6 is a marker of early mesoderm during murine embryogenesis,”Differentiation 38:124-133, 1988.
Fenderson et al., “A Multivalent Lacto-N-Fucopenatose III-Lysyllysine Conjugate Decompacts Preimplantation Mouse Embryos, While the Free Oligosaccharide is Ineffective,”J. Exp. Med. 106:1591-1596, 1984.
Fenderson et al., “Coordinate Expression of X and Y Haptens during Murine Embryogenesis,”Devel. Biol. 114:12-21, 1986.
Fukushi et al., “Novel Fucolipids Accumulating in Human Adenocarcinoma. II. Selective Isolation of Hybridoma Antibodies That Differentially Recognize Mono-, Di, and Trifucosylated Type 2 Chain,”J. Biol. Chem. 259(7):4681-4685, 1984.
Fukushi et al., “Novel Fucolipids Accumulating in Human Adenocarcinoma. III. A Hybridoma Antibody (FH6) Defining a Human Cancer-Associated Difucoganglioside (VI3NeuAcV3Fuc2nLc6),”J. Biol. Chem. 259(16):10511-10517, 1984.
Gabius et al., “Endogenous Tumor Lectins: Overview and Perspective,”Anticancer Res. 6:573-578, 1986.
Gallatin et al., “A cell-surface molecule involved in organ-specific homing of lymphocytes,”Nature 304:30-34, 1983.
Gooi et al., “Stage-specific embryonic antigen involves &agr; 1 →3 fucosylated type 2 blood group chains,”Nature 292:156-158, 1981.
Hakamori et al., “Novel Fucolipids Accumulating in Human Adenocarcinoma. I. Glycolipids With Di- or Trifucosylated Type 2 Chain,”J. Biol. Chem. 259(7):4672-4680, 1984.
Hakomori et al., “The Hapten Structure of a Developmentally Regulated Glycolipid Antigen (SSEA-1) Isolated From Human Erythrocytes and Adenocarcinoma: A Preliminary Note,”Biochem. Biophys. Res. Comm. 100(4):1578-1586, 1981.
Hakomori S., “Aberrant Glycosylation in Cancer Cell Membrane as Focused on Glycolipids: Overview and Perspectives,”Cancer Res. 45:2405-2414, 1985.
Handa et al., “Selectin GMP-140 (CD62; PADGEM) Binds to Sialosyl-Leaand Sialosyl-Lex, and Sulfated Gly

LandOfFree

Say what you really think

Search LandOfFree.com for the USA inventors and patents. Rate them and share your experience with other people.

Rating

Leukocyte homing modulation does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with Leukocyte homing modulation, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Leukocyte homing modulation will most certainly appreciate the feedback.

Rate now

     

Profile ID: LFUS-PAI-O-2817939

  Search
All data on this website is collected from public sources. Our data reflects the most accurate information available at the time of publication.