Abstract: The present invention relates to muscle repair promoters for local application that contain a colony-stimulating factor (CSF) as an active ingredient. The muscle repair promoters of the present invention exhibit their effect at low doses, particularly when they are administered intramuscularly.

Abstract: Disclosed are a method, a composition, a microarray, an antibody and a kit for diagnosis and prognosis of cancer, based on detection of deletion of the exon 3 region of G-CSF gene or levels of a mutated G-CSF protein having a deletion of an amino acid sequence corresponding to the exon 3 region, wherein the deletion of the exon 3 region of the G-CSF gene is used as a cancer biomarker.

Abstract: Provided are methods for inducing an increase in the number of CD4+ T-lymphocytes in HIV-infected patients by administering human GM-CSF. The GM-CSF may be administered concurrently with at least one antiretroviral agent.

Abstract: Provided are methods for inducing an increase in the number of CD4+ T-lymphocytes in HIV-infected patients by administering human GM-CSF. The GM-CSF may be administered concurrently with at least one antiretroviral agent.

Abstract: The present invention is directed to an isolated and purified, recombinant, unglycosylated and dimeric CSF-1, the dimeric CSF-1 being biologically active and essentially endotoxin and pyrogen-free, the dimeric CSF-1 consisting essentially of two monomeric human CSF-1 subunits. The present invention is further directed to pharmaceutical compositions comprising the same.

Abstract: A method for purifying CSF protein is described. The method comprises: precipitating the protein with ammonium sulfate at 80% saturation to form a pellet containing the CSF protein; resuspending the pellet in a buffered solution at a pH in the range of about 6 to about 8; applying the buffered solution containing CSF to a chromatographic column, eluting with the buffered solution containing sodium chloride and collecting the fractions having CSF activity; pooling the active fractions, applying them to a C4 reverse phase column and eluting with a 0 to 90% acetonitrile gradient to collect the active fractions. The purified CSF protein has a specific activity of at least about 1.times.10.sup.7 units per mg of protein and preferably at least about 4.times.10.sup.7 units per mg of protein when assayed using the human bone marrow assay.

Abstract: The invention relates to stable compositions of proteins and related methods wherein a protein capable of transitioning into the molten globular state is contacted with a negatively charged lipid vesicle, thereby stabilizing the protein against thermally-induced aggregation, denaturation, and loss of activity. The protein:phospholipid complex directly stabilizes the secondary and tertiary structure of the protein, and the compositions are useful in high temperature formulations and in novel delivery vehicles.

Abstract: The present invention is directed to a biologically active CSF-1 dimer comprising a first CSF-1 monomer and a second CSF-1 monomer, wherein at least one of the monomers is truncated at the C-terminus after residue position 223. The dimers also include point mutations in one or both of the CSF-1 monomer. The invention also includes pharmaceutical compositions that comprise the CSF-1 dimer in a pharmaceutical excipient.

Abstract: The present invention provides a chemically-modified protein prepared by binding polyethylene glycol to a polypeptide characterized by being the product of expression by a host cell of an exogenous DNA sequence and substantially having the following amino acid sequence: ##STR1## The chemically-modified protein according to the present invention has a much longer lasting neutrophil-increasing activity than that of the intact human G-CSF, enabling fewer numbers of administration with a lower dose.

Abstract: The present invention relates to the purification of proteins, to the products of such purification, and to DNA probes constructed therefrom. More specifically, the invention relates to the purification and sequencing of murine and human colony stimulating factor-1 (CSF-1).

Abstract: DNA for new forms of CSF-1 are provided which relate to N-terminal and C-terminal truncations. Specifically, N-.gradient.3 terminal truncations of the short and long forms of CSF-1 have been found to be particularly advantageous. These forms may have a C-terminal truncation at a variety of different amino acids beyond position 149.

Abstract: The present invention relates to the production of CSF-1 heterodimers and pharmaceutical formulations of the heterodimers. The heterodimers can be formed using CSF-1 monomers that have variations in sequence, N or C-terminal processing. For example, CSF/C.gradient.150 can be dimerized with LCSF/C.gradient. 190 to form a heterodimer. Dimerization may occur by separately preparing homodimers and mixing them together under the appropriate conditions. Thereafter, homodimers may be separated from the heterodimers by various chromatographic techniques. Once the heterodimers are isolated, pharmaceutical preparations can be prepared.

Abstract: Biologically active deletion and substitution mutants of hIL-3 are provided. Preferred mutants are those having one or more deletions at the N-terminus (amino acids 1-14) and/or the C-terminus (amino acids 116-133, 120-130 and/or 130-133). Preferred substitution mutants include Cys.sup.16 .fwdarw.Ala.sup.16 and/or Cys.sup.84 .fwdarw.Ala.sup.84, Glu.sup.50 .fwdarw.Lys.sup.50 and Lys.sup.79 .fwdarw.Glu.sup.79. These mutants can be used to formulate pharmaceutical compositions. Also disclosed are antibodies directed against specific epitopes localized between amino acids 29 and 54.

Abstract: Derivatives of naturally occurring G-CSF having at least one of the biological properties of naturally occurring G-CSF, and a solution stability of at least 35% at 5 mg/ml are disclosed in which the derivative has at least Cys.sup.17 of the native sequence replaced by a Ser.sup.17 residue and Asp.sup.27 of the native sequence replaced by a Ser.sup.17 residue. Nucleotide sequences coding for part or all of the amino acid sequence of the derivatives of the invention may be incorporated into autonomously replicating plasmid or viral vectors employed to transform or transfect suitable procaryotic or eucaryotic host cells such as bacteria, yeast or vertebrate cells in culture.

Abstract: A granulocyte stimulating factor (G-CSF) or a G-CSF variant differs from natural G-CSF in that one or several amino acids of the sequence ##STR1## at position 50 to 56 of the mature G-CSF with 174 amino acids or at position 53 to 59 of the mature G-CSF with 117 amino acids or/and at least one of the 4 His residues at position 43, 79, 156 or 170 of the mature G-CSF with 174 amino acids position 46, 82, 159 or 173 of the mature G-CSF with 177 amino acids are mutagenized. It is suitable for immunotherapy.

Abstract: Amplified expression of recombinant DNA products is achieved in hosts expressing proteases that cleave at multi-basic amino acid residues. To this end, cDNAs encoding granulocyte-macrophage colony stimulating factor (GM-CSF) are mutated such that one or both of the arginine residues at positions 23 and 24 of the protein product are deleted or replaced by non-basic amino acid residues. The GM-CSF analogs thus obtained maintain the activity of the wild-type protein.

Abstract: Novel hG-CSF polypeptide derivatives having an amino acid sequence derived from the amino acid sequence of the human granulocyte colony stimulating factor polypeptide by substitution of at least one amino acid by a different amino acid and/or deletion of at least one amino acid, recombinant plasmids containing a DNA fragment insert coding for any of these hG-CSF polypeptide derivatives, microorganisms carrying one of such plasmids, methods of producing the hG-CSF polypeptide derivatives using the microorganisms, a monoclonal antibody binding to the hG-CSF polypeptide derivative, and chemically modified hG-CSF or derivatives thereof are disclosed.

Abstract: A novel human megakaryocytopoietic factor capable of stimulating the growth and development of colonies of megakaryocytes is provided, including procedures for its purification and use as a pharmaceutical agent.

Abstract: Expression of a gene coding for human granulocyte macrophage colony-stimulating factor (CSF) in bacteria results in CSF proteins which are biologically active. Modification of the natural or of a synthetic gene structure results in biologically active derivatives with a modified amino acid sequence.

Abstract: Amplified expression of recombinant DNA products is achieved in hosts expressing protease that cleave at multi-basic amino acid residues. To this end, wild-type genes encoding the desired protein products are mutated by substituting codons or eliminating codons encoding multi-basic amino acid residues while maintaining the activity of the expressed protein product. Mutation of the desired gene can be conveniently carried out by site-specific in vitro mutagenisis.

Abstract: A polypeptide or glycosylated polypeptide with at least one new carbohydrate chain produced by means of recombinant DNA technique, which has protease resistance and thermal stability and is expected to have longer lifetime in blood than those of a naturally-occurring form.

Abstract: Novel hG-CSF polypeptide derivatives having an amino acid sequence derived from the amino acid sequence of the human granulocyte colony stimulating factor polypeptide by substitution of at least one amino acid by a different amino acid and/or deletion of at least one amino acid, recombinant plasmids containing a DNA fragment insert coding for any of these hG-CSF polypeptide derivatives, microorganisms carrying one of such plasmids, methods of producing the hG-CSF polypeptide derivatives using the microorganisms, a monoclonal antibody binding to the hG-CSF polypeptide derivative, and chemically modified hG-CSF or derivatives thereof are disclosed.

Abstract: Subjects suffering from infectious diseases are treated by direct administration of therapeutically-effective quantities of granulocyte-macrophage colony stimulating factor employed by itself or in conjunction with an antibiotic or a sulfonamide or other immunologically effective therapeutic agents. Homogeneous granulocyte-macrophage colony stimulating factor for use in treatment in bacterial diseases is prepared by recombinant DNA techniques and then purified to homogeneity by reverse phase high-performance liquid chromatography so that it may be safely administered to subject's suffering from infectious diseases.

Abstract: This invention provides a crystalline form of recombinant human granulocyte-macrophage colony-stimulating factor (r-h-GM-CSF) and methods for making such crystals.