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Proteasome (multicatalytic proteinase) of sea urchin sperm and its possible participation in the acrosome reaction.
Mol Reprod Dev. 1991 Jun; 29(2):189-99.MR

Abstract

The egg jelly-induced acrosome reaction of the sea urchin, Strongylocentrotus intermedius, was inhibited by succinyl-Leu-Leu-Val-Tyr-4-methyl-coumaryl-7-amide (Suc-Leu-Leu-Val-Tyr-MCA), but not by Suc-Ala-Ala-Pro-Phe-MCA. The proteases with hydrolytic activity toward the former were purified from sperm extract by DEAE-Sephacel and hydroxylapatite chromatographies, Sephacryl S-300 gel filtration, and heparin-Sepharose CL-6B chromatography. Two types of protease were separated, and the molecular weights were estimated to be 65 and 700 kDa, respectively, by gel filtration. The former was accompanied by hydrolytic activity toward Suc-Ala-Ala-Pro-Phe-MCA, which was not hydrolyzed by the latter. Polyacrylamide gel electrophoresis of 700 kDa protease gave a single protein band under nondenaturing conditions and at least eight bands in the range of 22-33 kDa in the presence of sodium dodecyl sulfate (SDS). The substrate specificity and the inhibitor sensitivity of 700 kDa protease indicate that it contains two types of the activity, one is chymotrypsin-type and the other trypsin-type. The former activity was enhanced by poly-L-lysine or SDS. These properties of 700 kDa protease are similar to those of proteasomes (multicatalytic proteinases) isolated from various eukaryotic sources. We had previously shown that inhibitors of chymotrypsin-like proteases inhibit the increase of intracellular Ca2+ concentration by egg jelly, resulting in the inhibition of the acrosome reaction of St. intermedius (Matsumura and Aketa, Gamete Res 23:255-266, 1989). Bringing these findings together, we suggest that the chymotrypsin-like activity of sperm proteasome participates in the onset of the acrosome reaction of St. intermedius.

Authors+Show Affiliations

Matsumura K
Akkeshi Marine Biological Station, Faculty of Science, Hokkaido University, Japan.
Aketa K
No affiliation info available

MeSH

AcrosomeAmino Acid SequenceAnimalsChymotrypsinCysteine EndopeptidasesElectrophoresis, Polyacrylamide GelMaleMolecular Sequence DataMultienzyme ComplexesOligopeptidesProtease InhibitorsProteasome Endopeptidase ComplexSea UrchinsSpermatozoaSubstrate SpecificityTrypsin

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

1878226

Citation

Matsumura, K, and K Aketa. "Proteasome (multicatalytic Proteinase) of Sea Urchin Sperm and Its Possible Participation in the Acrosome Reaction." Molecular Reproduction and Development, vol. 29, no. 2, 1991, pp. 189-99.
Matsumura K, Aketa K. Proteasome (multicatalytic proteinase) of sea urchin sperm and its possible participation in the acrosome reaction. Mol Reprod Dev. 1991;29(2):189-99.
Matsumura, K., & Aketa, K. (1991). Proteasome (multicatalytic proteinase) of sea urchin sperm and its possible participation in the acrosome reaction. Molecular Reproduction and Development, 29(2), 189-99.
Matsumura K, Aketa K. Proteasome (multicatalytic Proteinase) of Sea Urchin Sperm and Its Possible Participation in the Acrosome Reaction. Mol Reprod Dev. 1991;29(2):189-99. PubMed PMID: 1878226.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Proteasome (multicatalytic proteinase) of sea urchin sperm and its possible participation in the acrosome reaction. AU - Matsumura,K, AU - Aketa,K, PY - 1991/6/1/pubmed PY - 2000/6/1/medline PY - 1991/6/1/entrez SP - 189 EP - 99 JF - Molecular reproduction and development JO - Mol Reprod Dev VL - 29 IS - 2 N2 - The egg jelly-induced acrosome reaction of the sea urchin, Strongylocentrotus intermedius, was inhibited by succinyl-Leu-Leu-Val-Tyr-4-methyl-coumaryl-7-amide (Suc-Leu-Leu-Val-Tyr-MCA), but not by Suc-Ala-Ala-Pro-Phe-MCA. The proteases with hydrolytic activity toward the former were purified from sperm extract by DEAE-Sephacel and hydroxylapatite chromatographies, Sephacryl S-300 gel filtration, and heparin-Sepharose CL-6B chromatography. Two types of protease were separated, and the molecular weights were estimated to be 65 and 700 kDa, respectively, by gel filtration. The former was accompanied by hydrolytic activity toward Suc-Ala-Ala-Pro-Phe-MCA, which was not hydrolyzed by the latter. Polyacrylamide gel electrophoresis of 700 kDa protease gave a single protein band under nondenaturing conditions and at least eight bands in the range of 22-33 kDa in the presence of sodium dodecyl sulfate (SDS). The substrate specificity and the inhibitor sensitivity of 700 kDa protease indicate that it contains two types of the activity, one is chymotrypsin-type and the other trypsin-type. The former activity was enhanced by poly-L-lysine or SDS. These properties of 700 kDa protease are similar to those of proteasomes (multicatalytic proteinases) isolated from various eukaryotic sources. We had previously shown that inhibitors of chymotrypsin-like proteases inhibit the increase of intracellular Ca2+ concentration by egg jelly, resulting in the inhibition of the acrosome reaction of St. intermedius (Matsumura and Aketa, Gamete Res 23:255-266, 1989). Bringing these findings together, we suggest that the chymotrypsin-like activity of sperm proteasome participates in the onset of the acrosome reaction of St. intermedius. SN - 1040-452X UR - https://www.unboundmedicine.com/medline/citation/1878226/Proteasome__multicatalytic_proteinase__of_sea_urchin_sperm_and_its_possible_participation_in_the_acrosome_reaction_ DB - PRIME DP - Unbound Medicine ER -