Abstract: Method for treatment of inflammatory and fibrotic conditions in vivo using pure rhUG is disclosed. Method for treating or preventing inflammatory or fibrotic conditions characterized by a deficiency of endogenous functional UG is also disclosed. Compositions containing pure rhUG, optionally also containing lung surfactant, and assay procedures for detection of UG-fibronectin complexes, are also provided.

Abstract: The invention provides two human phospholipid binding proteins (PLBP) and polynucleotides which identify and encode PLBP. The invention also provides expression vectors, host cells, agonists, antibodies and antagonists. The invention also provides methods for treating and preventing disorders associated with expression of PLBP.

Abstract: The subject invention provides a pharmaceutical composition, which comprises an amount of calreticulin effective for blocking or preventing thrombosis in a subject, causing substantially no defect or no defect in normal hemostasis, and a pharmaceutically effective carrier. The subject invention provides a method for blocking or preventing thrombosis in a subject, causing substantially no defect or no defect in normal hemostasis, which method comprises administering calreticulin to the subject in an amount effective for blocking or preventing thrombosis. The subject invention provides a pharmaceutical composition, which comprises calreticulin in combination with an other antithrombotic agent, in an amount and proportion effective for enhancing the action of the other antithrombotic agent, to prevent clotting or dissolve clots which have already formed.

Abstract: Methods are provided for the isolation and purification of recombinant lung surfactant protein. The methods involve a multistep procedure including extraction with a C.sub.1 -C.sub.4 aliphatic alcohol and chromatographic purification steps which employ a C.sub.1 -C.sub.4 aliphatic alcohol as eluant. Purified proteins obtained using the disclosed isolation and purification steps are provided as well.

Abstract: 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.

Abstract: Methods are provided for the isolation and purification of recombinant lung surfactant protein. The methods involve a multistep procedure including extraction with a C.sub.1 -C.sub.4 aliphatic alcohol and chromatographic purification steps which employ a C.sub.1 -C.sub.4 aliphatic alcohol as eluant. Purified proteins obtained using the disclosed isolation and purification steps are provided as well.

Abstract: A composition comprising nerve growth factor and 2-amino-1,1,3-tricyano-1-propene useful for the induction, stimulation, and maintenance of nerve growth, and methods of potentiating choline O-acetyltransferase and tyrosine hydroxylase by 2-amino-1,1,3-tricyano-1-propene are disclosed.

Abstract: Novel neutrotrophic factor compositions are provided, obtained from lung tissue. The factors are found to be active on parasympathetic ganglion neutrons enhancing acetylcholine activity. The compositions find use in the treatment of a number of eye disorders.

Abstract: A formulation is described for systemic delivery and controlled release of a trophic factor. The formulation comprises a glycolipid carrier component which delivers trophic factor, such as nerve growth factor, to a target organ. The glycolipid carrier protects the trophic factor from degradation by enzymes typically endogenous to the human body.

Abstract: A composition comprising nerve growth factor and 2-amino-1,1,3-tricyano-1-propene useful for the induction, stimulation, and maintenance of nerve growth, and methods of potentiating choline O-acetyltransferase and tyrosine hydroxylase by 2-amino-1,1,3-tricyano-1-propene are disclosed.

Abstract: Methods and compositions are provided for detecting antigens having a specific epitope associated with squamous lung carcinoma. The antigen may be found at lesion sites or in the blood as indicative of the squamous lung carcinoma.Specific antibodies may be used for the detection of the antigen and in therapy.The mouse hybridoma 43-9F producing IgM monoclonal antibody 43-9F and SLC cell RH-SLC-L11 were deposited at The PHLS Centre for Applied Microbiology and Research, Porton Down, Salisbury, U.K. on Jan. 31, 1985 and given Accession Nos. 85013101 and 85061403, respectively.

Abstract: 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.

Abstract: Protein having a phospholipase A.sub.2 inhibitory activity which has the nature to be induced from cells upon administration of glucocorticoid and has a phospholipase A.sub.2 inhibitory activity.

Abstract: The present invention provides human characterized by a molecular weight of about 170,000 Dalton, a hexameric structure with monomeric subunits with a molecular weight of about 28,000 Dalton and a carbohydrate content of about 2%.The present invention provides a process for obtaining and purifying globular domain NC1 of basal membrane collagen, wherein human or animal tissue is subjected to a first limiting treatment with bacterial collagenase, the degradation products obtained are separated from non-collagen proteins by chromatography on a weakly basic anion exchanger, the collagen degradation products are then subjected to a second collagenase digestion at an elevated temperature and the globular domain NC1 is purified by molecular sieve fractionation.Furthermore, the present invention is concerned with the use of this for the determination in body fluids in the case of the use of their antibodies, as well as far the detection of antibodies directed thereagainst in body fluids.