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  • 1
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    Soluble lectins: a new class of extracellular proteins (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-03-23
    Description: Soluble lectins of cellular slime molds and vertebrates are present at extracellular sites in the developing or adult tissues that make them. Some lectins are concentrated around cell groups, as in extracellular matrix or elastic fibers. Others are at the interface between cells and the external environment, as in mucin or slime. Specific glycoproteins, proteoglycans, or polysaccharides that bind these endogenous lectins may also be present at these sites. Interactions between the lectins and glycoconjugates appear to play a role in shaping extracellular environments.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barondes, S H -- New York, N.Y. -- Science. 1984 Mar 23;223(4642):1259-64.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6367039" target="_blank"〉PubMed〈/a〉
    Keywords: Adhesiveness ; Animals ; Dictyostelium/physiology ; Embryo, Nonmammalian/metabolism ; Extracellular Matrix/metabolism ; Fungal Proteins/analysis/metabolism/*physiology ; Galactosides/metabolism ; Glycoproteins/metabolism ; Intestines/metabolism ; *Lectins/analysis ; Ligands ; Liver/metabolism ; Macromolecular Substances ; Muscles/metabolism ; Polysaccharides/metabolism ; Proteoglycans/metabolism ; *Protozoan Proteins ; Receptors, Mitogen/metabolism ; Solubility
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
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    The elastin receptor: a galactoside-binding protein (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-03-25
    Description: The elastin receptor complex contains a component of 67 kilodaltons that binds to a glycoconjugate affinity column containing beta-galactoside residues and is eluted from this column with lactose. This protein component is also released from the surface of cultured chondroblasts by incubation with lactose, and its association with immobilized elastin is inhibited by lactose. Since lactose also blocks elastic fiber formation by cultured chondroblasts, the galactoside-binding property of the elastin receptor is implicated in this process.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hinek, A -- Wrenn, D S -- Mecham, R P -- Barondes, S H -- HL-26499/HL/NHLBI NIH HHS/ -- HL-29594/HL/NHLBI NIH HHS/ -- HL-38627/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1988 Mar 25;239(4847):1539-41.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology and Physiology, Jewish Hospital, Washington University Medical Center, St. Louis, MO 63110.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2832941" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cartilage/analysis ; Cattle ; Cells, Cultured ; Chromatography, Affinity ; Elastin/metabolism ; Extracellular Matrix/drug effects/metabolism ; Galactosides/*metabolism ; Glycoconjugates/metabolism ; Glycosides/*metabolism ; Immunoassay ; Immunohistochemistry ; Lactose/pharmacology ; Lung/*analysis ; Microscopy, Electron ; Receptors, Cell Surface/drug effects/isolation & purification/*metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
    Location Call Number Expected Availability
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