alpha-Mannosidase from rat epididymal fluid is a ligand for phosphomannosyl receptors on the sperm surface (Journal article)

Belmonte, S. A./ Challa, A./ Gutierrez, L. S./ Bertini, F./ Sosa, M. A.


This study demonstrates that alpha-mannosidase from rat epididymal fluid is a ligand for phosphomannosyl receptors on the sperm surface. This enzyme was bound to intact epididymal spermatozoa with high affinity and in saturable form, and the binding was inhibited by mannose-6-phosphate but not by phosphorylated derivatives of fructose. Treatment of the enzyme with sodium periodate inhibited the binding of alpha-mannosidase, confirming that a carbohydrate residue is involved in the interaction with spermatozoa. Evidence is also presented that the cation-independent phosphomannosyl receptors are responsible for the interaction with alpha-mannosidase. These findings suggest a new role for extracellular transport mediated by the mannose-6-phosphate receptor.
Institution and School/Department of submitter: Πανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών Υγείας. Τμήμα Ιατρικής
Keywords: Animals,Body Fluids/enzymology,Epididymis/enzymology,Hydrogen-Ion Concentration,Ligands,Male,Mannosidases/*metabolism,Rats,Receptors, Cytoplasmic and Nuclear/*metabolism,Spermatozoa/*metabolism,alpha-Mannosidase
URI: http://olympias.lib.uoi.gr/jspui/handle/123456789/23972
ISSN: 0105-6263
Item type: journalArticle
Link: http://www.ncbi.nlm.nih.gov/pubmed/9805243
Item language: en
Item access scheme: campus
Institution and School/Department of submitter: Πανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών Υγείας. Τμήμα Ιατρικής
Publication date: 1998
Abstract: This study demonstrates that alpha-mannosidase from rat epididymal fluid is a ligand for phosphomannosyl receptors on the sperm surface. This enzyme was bound to intact epididymal spermatozoa with high affinity and in saturable form, and the binding was inhibited by mannose-6-phosphate but not by phosphorylated derivatives of fructose. Treatment of the enzyme with sodium periodate inhibited the binding of alpha-mannosidase, confirming that a carbohydrate residue is involved in the interaction with spermatozoa. Evidence is also presented that the cation-independent phosphomannosyl receptors are responsible for the interaction with alpha-mannosidase. These findings suggest a new role for extracellular transport mediated by the mannose-6-phosphate receptor.
Journal name: Int J Androl
Journal type: peer-reviewed
Appears in Collections:Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά)

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