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  • Life Sciences (General)  (1)
  • Rye Chromosomal location  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Rye chromosome arm 3RS encodes a homodimeric inhibitor of insect α-amylase (1994)
    Springer
    Theoretical and applied genetics 89 (1994), S. 60-63 
    Details
    ISSN: 1432-2242
    Keywords: α-amylase inhibitor ; Rye Chromosomal location ; Homoeologous genes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A new inhibitor of insect α-amylase, designated RDAI-1, has been purified from rye (Secale cereale L.) endosperm. RDAI-1 is homologous to wheat homodimeric inhibitors. This homology is supported by their similar N-terminal amino-acid sequences, inhibitory activities towards amylases from Tenebrio molitor (Coleoptera) and human saliva, and aggregative properties in gel-filtration chromatography. The gene encoding RDAI-1, IdhaR1, is located on the short arm of chromosome 3R, which is homoeologous with wheat chromosome arms 3BS and 3DS, where the genes for homodimeric inhibitors have been previously mapped.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00226983
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    Paper (German National Licenses)
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  • 2
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    Collagenase-3 binds to a specific receptor and requires the low density lipoprotein receptor-related protein for internalization (1999)
    In:  Other Sources
    Details
    Publication Date: 2019-07-13
    Description: We have previously identified a specific receptor for collagenase-3 that mediates the binding, internalization, and degradation of this ligand in UMR 106-01 rat osteoblastic osteosarcoma cells. In the present study, we show that collagenase-3 binding is calcium-dependent and occurs in a variety of cell types, including osteoblastic and fibroblastic cells. We also present evidence supporting a two-step mechanism of collagenase-3 binding and internalization involving both a specific collagenase-3 receptor and the low density lipoprotein receptor-related protein. Ligand blot analysis shows that (125)I-collagenase-3 binds specifically to two proteins ( approximately 170 kDa and approximately 600 kDa) present in UMR 106-01 cells. Western blotting identified the 600-kDa protein as the low density lipoprotein receptor-related protein. Our data suggest that the 170-kDa protein is a specific collagenase-3 receptor. Low density lipoprotein receptor-related protein-null mouse embryo fibroblasts bind but fail to internalize collagenase-3, whereas UMR 106-01 and wild-type mouse embryo fibroblasts bind and internalize collagenase-3. Internalization, but not binding, is inhibited by the 39-kDa receptor-associated protein. We conclude that the internalization of collagenase-3 requires the participation of the low density lipoprotein receptor-related protein and propose a model in which the cell surface interaction of this ligand requires a sequential contribution from two receptors, with the collagenase-3 receptor acting as a high affinity primary binding site and the low density lipoprotein receptor-related protein mediating internalization.
    Keywords: Life Sciences (General)
    Type: The Journal of biological chemistry (ISSN 0021-9258); 274; 42; 30087-93
    Format: text
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    NASA TECHNICAL REPORTS
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