PMID- 10373300
OWN - NLM
STAT- MEDLINE
DCOM- 19990729
LR  - 20061115
IS  - 0012-1606 (Print)
IS  - 0012-1606 (Linking)
VI  - 211
IP  - 1
DP  - 1999 Jul 1
TI  - The cortical granule serine protease CGSP1 of the sea urchin, Strongylocentrotus 
      purpuratus, is autocatalytic and contains a low-density lipoprotein receptor-like
      domain.
PG  - 1-10
AB  - Trypsin-like activity is secreted from eggs of many species at fertilization, and
      this activity is believed to be critical for the block to polyspermy. Here we
      show that a cortical granule serine protease of sea urchins is the major and
      perhaps only protease family member important for fertilization. Zymography
      assays suggest that the cortical granules contain a single serine protease that
      can undergo autocatalysis and is secreted upon egg activation. We used this
      finding to identify a cDNA clone from a Strongylocentrotus purpuratus ovary cDNA 
      library that encodes a 581-amino-acid-residue protein that we refer to as
      cortical granule serine protease 1 (CGSP1). The catalytic domain of the protein
      contains the essential residues of the catalytic triad characteristic of a member
      of the trypsin-like family of serine proteases and the N-terminus of CGSP1
      resembles the ligand-binding domain of the low-density lipoprotein (LDL)
      receptor. Antibodies raised separately to both the protease and LDL receptor-like
      domains each localize to the cortical granules of unfertilized eggs. Furthermore,
      the full-length form of CGSP1, as well as intermediate and active forms of the
      protease, is detected in cortical granules by immunoblot analysis. Our evidence
      suggests that CGSP1 is activated at fertilization and is responsible for the
      protease-mediated reactions that follow cortical granule exocytosis and
      contribute to the block to polyspermy.
CI  - Copyright 1999 Academic Press.
FAU - Haley, S A
AU  - Haley SA
AD  - Department of Molecular and Cell Biology & Biochemistry, Brown University,
      Providence, Rhode Island, 02912, USA.
FAU - Wessel, G M
AU  - Wessel GM
LA  - eng
SI  - GENBANK/AF149789
PT  - Journal Article
PT  - Research Support, U.S. Gov't, Non-P.H.S.
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Dev Biol
JT  - Developmental biology
JID - 0372762
RN  - 0 (Receptors, Lipoprotein)
RN  - EC 3.4.21.- (Serine Endopeptidases)
RN  - EC 3.4.21.4 (Trypsin)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Base Sequence
MH  - Binding Sites
MH  - Cloning, Molecular
MH  - Cytoplasmic Granules/enzymology
MH  - Enzyme Activation
MH  - Immunohistochemistry
MH  - Molecular Sequence Data
MH  - Ovum/enzymology
MH  - Receptors, Lipoprotein/chemistry/*genetics
MH  - Reproduction
MH  - Sea Urchins/*enzymology/genetics
MH  - Sequence Homology, Amino Acid
MH  - Serine Endopeptidases/chemistry/*genetics
MH  - Trypsin/chemistry
EDAT- 1999/06/22 00:00
MHDA- 1999/06/22 00:01
CRDT- 1999/06/22 00:00
PHST- 1999/06/22 00:00 [pubmed]
PHST- 1999/06/22 00:01 [medline]
PHST- 1999/06/22 00:00 [entrez]
AID - 10.1006/dbio.1999.9299 [doi]
AID - S0012-1606(99)99299-0 [pii]
PST - ppublish
SO  - Dev Biol. 1999 Jul 1;211(1):1-10. doi: 10.1006/dbio.1999.9299.