Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P11684 (Uteroglobin)
 114 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Uteroglobin has been purified from hare lung by gel filtration and chromatography on carboxymethyl-cellulose. Hare uteroglobin appears homogeneous by electrophoresis under both denaturing and nondenaturing conditions. Its chemical and immunological properties as well as its ability to bind progesterone are compared to those of rabbit uteroglobin. The two proteins have the same N-terminal residue (glycine) and both lack tryptophan but differ in amino acid composition. Sodium dodecyl sulfate-gel electrophoresis shows that hare uteroglobin is composed of two subunits of identical Mr (about 7000) held together by disulfide bridges. The amino acid composition indicates a subunit composed of 65-67 residues, which is compatible with the apparent Mr observed. Thus, hare uteroglobin appears to be slightly smaller than the rabbit protein. Hare uteroglobin partially reacts with anti-rabbit uteroglobin in a radioimmunoassay and also binds progesterone, although this binding is relatively unaffected by dithiothreitol. The synthesis of hare uteroglobin in the uterus appears to be rather insensitive to ovarian steroid hormones.
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PMID:Isolation and characterization of uteroglobin from the lung of the hare (Lepus capensis). 663 70

1. Uteroglobin-like antigens were found in the lung and uterus of the hare (Lepus) and the pika (Ochotona). These antigens presented an immunoreactivity indistinguishable from that of rabbit uteroglobin, as determined by radioimmunoassay. 2. The molecular weight and the subunit composition of these antigens were similar to those of rabbit uteroglobin as analyzed by SDS gel-electrophoresis. 3. Similar amounts of uteroglobin-like immunoreactivity were found in the respective lungs and uteri of hare and rabbit whereas the concentration of immunoreactivity in the pika organs was several-fold lower.
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PMID:Uteroglobin-like antigens in species of Lagomorpha. 706 7

Uteroglobin (UG) is a steroid-inducible, multifunctional, secreted protein with antiinflammatory and antichemotactic properties. Recently, we have reported a high affinity UG-binding protein (putative receptor), on several cell types, with an apparent molecular mass of 190 kDa (Kundu, G. C., Mantile, G., Miele, L., Cordella-Miele, E., and Mukherjee, A. B. (1996) Proc. Natl. Acad. Sci. U. S. A. 93, 2915-2919). Since UG is a homodimer in which the 70 amino acid subunits are connected by two disulfide bonds, we sought to determine whether UG monomers also interact with the 190-kDa UG-binding protein and if so, whether it has the same biological activity as the dimer. Surprisingly, we discovered that in addition to the 190-kDa species, another protein, with an apparent molecular mass of 49 kDa, binds reduced UG with high affinity and specificity. Both 49- and 190-kDa proteins are readily detectable on nontransformed NIH 3T3 and some murine cancer cells (e. g. mastocytoma, sarcoma, and lymphoma), while lacking on others (e.g. fibrosarcoma). Most interestingly, pretreatment of the cells, which express the binding proteins, with reduced UG dramatically suppresses extracellular matrix (ECM) invasion, when such treatment had no effect on fibrosarcoma cells that lack the UG-binding proteins. Tissue-specific expression studies confirmed that while both 190- and 49-kDa UG-binding proteins are present in bovine heart, spleen, and the liver, only the 190-kDa protein is detectable in the trachea and in the lung. Neither the 190-kDa nor the 49-kDa protein was detectable in the aorta. Purification of these binding proteins from bovine spleen by UG-affinity chromatography and analysis by SDS-polyacrylamide gel electrophoresis followed by silver staining identified two protein bands with apparent molecular masses of 40 and 180 kDa, respectively. Treatment of the NIH 3T3 cells with specific cytokines (i.e. interleukin-6) and other agonists (i.e. lipopolysaccharide) caused a substantially increased level of 125I-UG binding but the same cells, when treated with platelet-derived growth factor, tumor necrosis factor-alpha, interferon-gamma, and phorbol 12-myristate 13-acetate, did not alter the UG binding. Taken together, these findings raise the possibility that UG, through its binding proteins, plays critical roles in the regulation of cellular motility and ECM invasion.
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PMID:Uteroglobin (UG) suppresses extracellular matrix invasion by normal and cancer cells that express the high affinity UG-binding proteins. 971 16