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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1980-2-28
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pubmed:abstractText |
Mild acid hydrolysis of phosphomannan secreted by the yeast hansenula holstii (NRRL Y- 2448) produces two phosphomannyl fragments which differ strikingly in their potency as inhibitors of pinocytosis of human beta-glucuronidase by human fibroblasts. The larger molecular weight polyphosphomonoester fragment is 100,000-fold more potent an inhibitor of enzyme uptake than the smaller penta-mannosyl-monophosphate fragment. Binding to attached fibroblasts at 3 degrees C was much greater with the polyphosphomonoester fragment than with the pentamannosyl-monophosphate. The larger molecular weight fragment was also subject to adsorptive pinocytosis and was taken up by fibroblasts at a rate 30- fold greater than the rate of uptake of pentamannosyl-monophosphate. Evidence that the polyphosphomonoester fragment is taken up by the phosphomannosyl-recognition system that mediates uptake of lysosomal enzymes includes: (a) its pinocytosis is inhibited by the same compounds that competitively inhibit enzyme pinocytosis (mannose-6-phosphate and phosphomannan from saccharomyces cerevisiae mutant mnn-1); (b) alkaline phosphatase treatment greatly reduces its susceptibility to pinocytosis; (c) its pinocytosis is competitively inhibited by high-uptake human beta-glucuronidase; and (d) this inhibition by high-uptake enzyme is dramatically reduced by prior treatment of the enzyme with alkaline phosphatase or endoglycosidase-H. Endoglycosidase-H treatment human beta-glucuronidase dramatically reduced its susceptibility to pinocytosis by fibroblasts. The phosphomannosyl components of high- uptake enzyme released by endoglycosidase-H treatment were much less effective inhibitors of polyphosphomonoester pinocytosis than when present on the phosphomannyl-enzyme. These results suggest that high-uptake acid hydrolases may be polyvalent ligands analogous to the polyphosphomonoester mannan fragment whose pinocytosis depends on interaction of more than one phospho-mannosyl recognition marker with pinocytosis receptors on fibroblasts.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/7350171-1070007,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7350171-1119807,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7350171-13793161,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7350171-14907713,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7350171-266721,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7350171-291966,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7350171-340454,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7350171-413568,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7350171-4202279,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7350171-4255108,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7350171-4257494,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7350171-4271574,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7350171-4345092,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7350171-4351076,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7350171-4364008,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7350171-4572357,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7350171-4599414,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7350171-4700198,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7350171-646806,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7350171-806251,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7350171-827294,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7350171-908752,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7350171-922886
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0021-9525
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
84
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
77-86
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pubmed:dateRevised |
2010-6-22
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pubmed:meshHeading |
pubmed-meshheading:7350171-Alkaline Phosphatase,
pubmed-meshheading:7350171-Fibroblasts,
pubmed-meshheading:7350171-Glucuronidase,
pubmed-meshheading:7350171-Hexosephosphates,
pubmed-meshheading:7350171-Humans,
pubmed-meshheading:7350171-Mannans,
pubmed-meshheading:7350171-Mannosephosphates,
pubmed-meshheading:7350171-Pinocytosis,
pubmed-meshheading:7350171-Polysaccharides,
pubmed-meshheading:7350171-Receptors, Drug
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pubmed:year |
1980
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pubmed:articleTitle |
Fibroblast receptor for lysosomal enzymes mediates pinocytosis of multivalent phosphomannan fragment.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.
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