Abstract: Growth differentiation factor-10 (GDF-10) polypeptide is disclosed as well as polynucleotides encoding GDF-10, vectors and host cells.

Abstract: This invention relates to the glycoprotein v gene. Specifically, this invention discloses the sequence and structure of the glycoprotein v gene and the amino acid sequence of the glycoprotein v polypeptide. In addition, the evolutionary relationship of the glycoprotein v gene with other glycoproteins is described and several uses of the isolated glycoprotein v gene are shown.

Abstract: Dimeric proteins having substantially the same biological activity as PDGF are disclosed. More specifically, the protein may have two substantially identical polypeptide chains, each of the chains being substantially homologous to the A-chain of PDGF. Alternatively, the protein may have two polypeptide chains that are substantially identical to the A-chain of PDGF. In addition, proteins comprising polypeptides that are variants or derivatives of the A-chain of PDGF are also disclosed. Therapeutic compositions containing these proteins and methods for enhancing the wound-healing process in warm-blooded animals are also disclosed.

Abstract: A novel family of growth regulatory proteins termed "epithelins" are described. The epithelins comprise several distinct members sharing significant structural homology. Two members of the epithelin family, epithelin 1 and epithelin 2, have been purified from natural sources. In addition, cDNA and PCR clones encoding mature and precursor epithelins from various chordate sources have been obtained and sequenced, including the complete human, mouse and rat epithelin precursors. The recombinant expression of rat epithelin precursor and mature forms is described. Purified epithelin 1 is a bifunctional growth regulator, capable of stimulating the growth of some cell types while inhibiting the growth of others. Purified epithelin 2 is functionally similar to epithelin 1 with respect to growth inhibitory bioactivity. In contrast, however, epithelin 2 is apparently not capable of eliciting the growth stimulatory activity characteristic of epithelin 1 and, in fact, antagonizes this epithelin 1 activity.

Abstract: The invention provides methods for the systematic analysis of the structure and function of polypeptides by identifying active domains which influence the activity of the polypeptide with a target substance. Such active domains are determined by substituting selected amino acid segments of the polypeptide with an analogous polypeptide segment from an analog to the polypeptide. The analog has a different activity with the target substance as compared to the parent polypeptide. The activities of the segment-substituted polypeptides are compared to the same activity for the parent polypeptide for the target. A comparison of such activities provides an indication of the location of the active domain in the parent polypeptide. The invention also provides methods for identifying the active amino acid residues within the active domain of the parent polypeptide.

Abstract: The survival and proliferation of Schwann cells can be promoted by culturing such cells in the presence of peptides derived from the EGF-like domain of proteins from the NDF/heregulin family. Colon epithelial cells can be stimulated to multiply and differentiate by culturing such cells in the presence of the same peptides.

Abstract: A novel family of growth regulatory proteins termed "epithelins" are described. The epithelins comprise several distinct members sharing significant structural homology. Two members of the epithelin family, epithelin 1 and epithelin 2, have been purified from natural sources. In addition, cDNA and PCR clones encoding mature and precursor epithelins from various chordate sources have been obtained and sequenced, including the complete human, mouse and rat epithelin precursors. The recombinant expression of rat epithelin precursor and mature forms is described. Purified epithelin 1 s a bifunctional growth regulator, capable of stimulating the growth of some cell types while inhibiting the growth of others. Purified epithelin 2 is functionally similar to epithelin 1 with respect to growth inhibitory bioactivity. In contrast, however, epithelin 2 is apparently not capable of eliciting the growth stimulatory activity characteristic of epithelin 1 and, in fact, antagonizes this epithelin 1 activity.

Abstract: The invention features human CD11 recombinant or synthetic peptide capable of inhibiting a CD11/CD18-mediated immune response, a purified DNA encoding a human CD11b peptide, soluble heterodimeric molecules composed of a CD11 peptide and a CD18 peptide, and a method of controlling any phagocyte-mediated tissue damage such as that associated with reduced perfusion of heart tissue during acute cardiac insufficiency.

Abstract: The present invention relates to novel complexes of major histocompatibility complex (MHC) molecules and uses of such complexes. In one aspect, the invention relates to loaded MHC complexes that include at least one MHC molecule with a peptide-binding groove and a presenting peptide non-covalently linked to the MHC protein. In another aspect, the invention features single chain MHC class II peptide fusion complexes with a presenting peptide covalently linked to the peptide binding grove of the complex. MHC complexes of the invention are useful for a variety of applications including: 1) in vitro screens for identification and isolation of peptides that modulate activity of selected T cells, including peptides that are T cell receptor antagonists and partial agonists, and 2) methods for suppressing or inducing an immune response in a mammal.

Abstract: The present invention relates to new recombinant DNA-molecules comprising nucleotide sequences of S. dysgalactiae encoding for at least one protein or polypeptide having fibronectin binding property.

Abstract: Chimeric proteins containing sequences from MCP and DAF and further containing peptide sequences capable of binding glycosaminoglycans. Nucleotide sequences encoding the chimeric proteins, expression vectors containing the nucleotide sequences, as well as transformed host cells capable of producing the chimeric proteins are claimed.

Abstract: Disclosed are (1) a human parathyroid hormone mutein which comprises at least one modification selected from the group consisting of (i) deletion of 3 to 6 amino acid residues on the N-terminal side in the amino acid sequence of human parathyroid hormones, (ii) substitution of another lipophilic amino acid residue for at least one methionine residue in the amino acid sequence, and (iii) substitution of a cysteine residue for one amino acid residue within the region of amino acid residue Nos. 34 to 47 in the amino acid sequence; (2) a recombinant DNA having a nucleotide sequence coding for the human parathyroid hormone mutein described in (1); (3) a vector containing the recombinant DNA described in (2); (4) a vector in which the recombinant DNA described in (2) is inserted into a region controlled by an E.

Abstract: The invention identifies the CTLA4 receptor as a ligand for the B7 antigen. The complete amino acid sequence encoding human CTLA4 receptor gene is provided. Methods are provided for expressing CTLA4 as an immunoglobulin fusion protein, for preparing hybrid CTLA4 fusion proteins, and for using the soluble fusion proteins, fragments and derivatives thereof, including monoclonal antibodies reactive with B7 and CTLA4, to regulate T cell interactions and immune responses mediated by such interactions.

Abstract: An acid-labile protein is described that, when incubated with the 53-Kd acid-stable protein occupied by IGF, converts it to a high molecular weight complex, corresponding to the in vivo form of IGF. This protein is called the acid-labile subunit (ALS) of IGF binding protein complex and is provided in biologically pure form. ALS is useful in treating wounds and promoting cellular growth. The nucleic acid encoding ALS, antibodies binding thereto, and fragments thereof are also disclosed.

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.

Abstract: Schwann cells can be treated in vivo to survive longer and to proliferate by contacting them with peptides derived from the EGF-like domain of proteins of the NDF/heregulin family.

Abstract: Methods are provided for the preparation in recombinant host cells of biologically active soluble variants of discretely encoded, heteromultimer polypeptide receptors. Such variants are synthesized by the secretion from recombinant transformants of transmembrane-modified heteromultimer receptors. Preferred receptors are extracellular matrix, cell surface, or plasma protein-binding receptors such as GPIIb-IIIa.

Abstract: Polypeptides comprising a first domain, which comprises a binding region of an immunoglobulin heavy chain variable region, and a second domain, which comprises a binding region of an immunoglobulin light chain variable region, the domains being linked but incapable of associating with each other to form an antigen binding site, associate to form antigen binding multimers, such as dimers, which may be multivalent or have multispecificity. The domains may be linked by a short peptide linker or may be joined directly together. Bispecific dimers may have longer linkers. Methods of preparation of the polypeptides and multimers and diverse repertoires thereof, and their display on the surface of bacteriophage for easy selection of binders of interest, are disclosed, along with many utilities.

Abstract: Chimeric peptides or polypeptides that combine ligand binding portions from within the lectin and EGF domains of two different selectins are disclosed. The peptides or polypeptides can be constructed solely of the indicated portions of lectin or EGF domains or they can include portions of any of the remaining domains (SCR, transmembrane or cytoplasmic), or the entire extracellular portion, of a generic selectin molecule. The peptides or polypeptides also can be joined to a carrier protein (e.g., a soluble portion of an immunoglobulin molecule) to increase the serum half-life of the therapeutic agent. The chimeric polypeptides can be used as therapeutic agents to antagonize selectin function. They are also useful for screening for agents that are simultaneously antagonists of the function of lectin and EGF domains of different selectins.

Abstract: An isolated antibody that specifically binds a peptide coded by a nucleotide sequence coding for a variable region of .beta.-chain of an human T lymphocyte receptor, said nucleotide sequence having a nucleotide sequence selected from any of:the nucleotide sequences of SEQ ID Nos. 2 to 19.