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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
12
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pubmed:dateCreated |
1990-5-24
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pubmed:abstractText |
The mannose 6-phosphate (Man-6-P)/insulin-like growth factor (IGF) II receptor has separate binding sites for Man-6-P and IGF II. It targets newly synthesized lysosomal enzymes from the Golgi to acidic pre-lysosomal organelles and mediates endocytosis of Man-6-P-containing ligands and IGF II. The two classes of ligands, Man-6-P and IGF II, as well as IGF I and the epidermal growth factor, induce in fibroblasts a transient redistribution of the receptor from internal membranes to the cell surface (Braulke, T., Tippmer, S., Neher, E., and von Figura, K. (1989) EMBO J. 8, 681-686). Here we show that the redistribution induced by IGF I and IGF II is accomplished without affecting the internalization rate of cell surface receptors. The redistribution results in an increased binding of ligands to the Man-6-P- and IGF II-binding sites of the receptor. Furthermore, the uptake of the lysosomal enzyme arylsulfatase A and of a Man-6-P neoglycoprotein is stimulated 2-3-fold by IGF I and IGF II, and this effect persists for at least 6 h. The IGF I- and IGF II-induced receptor redistribution does not affect the targeting of newly synthesized lysosomal enzymes. These results show that important functions of the Man-6-P/IGF II receptor such as binding and internalization of ligands can be up-regulated by the ligands of this receptor and other growth factors such as IGF I through redistribution of the receptor.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cerebroside-Sulfatase,
http://linkedlifedata.com/resource/pubmed/chemical/Insulin-Like Growth Factor I,
http://linkedlifedata.com/resource/pubmed/chemical/Insulin-Like Growth Factor II,
http://linkedlifedata.com/resource/pubmed/chemical/Mannosephosphates,
http://linkedlifedata.com/resource/pubmed/chemical/Somatomedins,
http://linkedlifedata.com/resource/pubmed/chemical/mannose-6-phosphate
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
25
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pubmed:volume |
265
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
6650-5
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:1969863-Cells, Cultured,
pubmed-meshheading:1969863-Cerebroside-Sulfatase,
pubmed-meshheading:1969863-Endocytosis,
pubmed-meshheading:1969863-Fibroblasts,
pubmed-meshheading:1969863-Humans,
pubmed-meshheading:1969863-Insulin-Like Growth Factor I,
pubmed-meshheading:1969863-Insulin-Like Growth Factor II,
pubmed-meshheading:1969863-Kinetics,
pubmed-meshheading:1969863-Lysosomes,
pubmed-meshheading:1969863-Male,
pubmed-meshheading:1969863-Mannosephosphates,
pubmed-meshheading:1969863-Skin,
pubmed-meshheading:1969863-Somatomedins,
pubmed-meshheading:1969863-Temperature
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pubmed:year |
1990
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pubmed:articleTitle |
Insulin-like growth factors I and II stimulate endocytosis but do not affect sorting of lysosomal enzymes in human fibroblasts.
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pubmed:affiliation |
University of Göttingen, Biochemie II, Federal Republic of Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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