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  • 1
    Publication Date: 1987-09-18
    Description: The protein portion of the immunosuppressive glycoprotein uromodulin is identical to the Tamm-Horsfall urinary glycoprotein and is synthesized in the kidney. Evidence that the glycoproteins are the same is based on amino acid sequence identity, immunologic cross-reactivity, and tissue localization to the thick ascending limb of Henle's loop. Nucleic acid sequencing of clones for uromodulin isolated from a complementary DNA bank from human kidney predicts a protein 639 amino acids in length, including a 24--amino acid leader sequence and a cysteine-rich mature protein with eight potential glycosylation sites. Uromodulin and preparations of Tamm-Horsfall glycoprotein bind to recombinant murine interleukin-1 (rIL-1) and human rIL-1 alpha, rIL-1 beta, and recombinant tumor necrosis factor (rTNF). Uromodulin isolated from urine of pregnant women by lectin adherence is more immunosuppressive than material isolated by the original salt-precipitation protocol of Tamm and Horsfall. Immunohistologic studies demonstrate that rIL-1 and rTNF bind to the same area of the human kidney that binds to antiserum specific for uromodulin. Thus, uromodulin (Tamm-Horsfall glycoprotein) may function as a unique renal regulatory glycoprotein that specifically binds to and regulates the circulating activity of a number of potent cytokines, including IL-1 and TNF.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hession, C -- Decker, J M -- Sherblom, A P -- Kumar, S -- Yue, C C -- Mattaliano, R J -- Tizard, R -- Kawashima, E -- Schmeissner, U -- Heletky, S -- New York, N.Y. -- Science. 1987 Sep 18;237(4821):1479-84.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3498215" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Cloning, Molecular ; Enzyme-Linked Immunosorbent Assay ; Glycoproteins/metabolism ; Humans ; Interleukin-1/metabolism ; Kidney/*metabolism ; Ligands/metabolism ; Lymphokines/*metabolism ; Molecular Weight ; Mucoproteins/*analysis/genetics ; RNA, Messenger/analysis ; Recombinant Proteins/metabolism ; Tumor Necrosis Factor-alpha ; Uromodulin
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
    Publication Date: 1985-08-02
    Description: Crude fractions of urine from pregnant women are immunosuppressive in vitro. An 85-kilodalton immunosuppressive glycoprotein purified to homogeneity from such urine inhibited in vitro assays of human T-cell and monocyte activity at concentrations of 10(-9) to 10(-11) molar. This material was nontoxic and blocked early events required for normal T-cell proliferation in vitro. On the basis of its tissue source and its in vitro activity, the name "uromodulin" is proposed for this glycoprotein.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Muchmore, A V -- Decker, J M -- New York, N.Y. -- Science. 1985 Aug 2;229(4712):479-81.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2409603" target="_blank"〉PubMed〈/a〉
    Keywords: B-Lymphocytes/drug effects ; Chromatography/methods ; Collodion ; Cytotoxicity, Immunologic/drug effects ; Electrophoresis, Polyacrylamide Gel ; Epitopes ; Female ; Hemolytic Plaque Technique ; Humans ; Immunosuppressive Agents/isolation & purification/*urine ; In Vitro Techniques ; Isoelectric Focusing ; Lymphocyte Activation/drug effects ; Molecular Weight ; *Mucoproteins ; Pregnancy ; Pregnancy Proteins/isolation & purification/pharmacology/*urine ; T-Lymphocytes/drug effects ; Uromodulin
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Location Call Number Expected Availability
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