Analysis of loss of adhesive function in sperm lacking cyritestin or fertilin β

被引:211
作者
Nishimura, H
Cho, C
Branciforte, DR
Myles, DG
Primakoff, P
机构
[1] Univ Calif Davis, Sch Med, Dept Cell Biol & Human Anat, Davis, CA 95616 USA
[2] Univ Calif Davis, Sect Mol & Cellular Biol, Davis, CA 95616 USA
关键词
fertilization; sperm-egg fusion; sperm-zona binding; ADAM; microdomain;
D O I
10.1006/dbio.2001.0166
中图分类号
Q [生物科学];
学科分类号
07 ; 0710 ; 09 ;
摘要
We produced mice lacking the sperm surface protein cryitestin (ADAM 3) and found mutant males are infertile. Similar to fertilin beta (ADAM 2) null sperm (C. Cho ef al., 1998, Science 281, 1857-1859), cyritestin null sperm are drastically deficient in adhesion to the egg zona pellucida (0.3% of wild type) and to the egg plasma membrane (9% of wild type). Thus sperm from male mice with a gene deletion of either ADAM have a loss of adhesive function in at least two steps of fertilization. We found deletion of either ADAM gene resulted in the loss of multiple gene products. This loss of multiple gene products (sperm membrane proteins) appears to result from a novel, developmental mechanism during sperm differentiation. Because the altered sperm protein expression must be responsible for the fertilization defects, our data suggest new models for the molecular basis of the affected steps in fertilization. (C) 2001 Academic Press.
引用
收藏
页码:204 / 213
页数:10
相关论文
共 39 条
  • [1] MOUSE EGG INTEGRIN ALPHA-6-BETA-1 FUNCTIONS AS A SPERM RECEPTOR
    ALMEIDA, EAC
    HUOVILA, APJ
    SUTHERLAND, AE
    STEPHENS, LE
    CALARCO, PG
    SHAW, LM
    MERCURIO, AM
    SONNENBERG, A
    PRIMAKOFF, P
    MYLES, DG
    WHITE, JM
    [J]. CELL, 1995, 81 (07) : 1095 - 1104
  • [2] Endoplasmic reticulum quality control of oligomeric membrane proteins:: Topogenic determinants involved in the degradation of the unassembled Na,K-ATPase α subunit and in its stabilization by β subunit assembly
    Béguin, P
    Hasler, U
    Staub, O
    Geering, K
    [J]. MOLECULAR BIOLOGY OF THE CELL, 2000, 11 (05) : 1657 - 1672
  • [3] A model for sperm-egg binding and fusion based on ADAMs and integrins
    Bigler, D
    Chen, M
    Waters, S
    White, JM
    [J]. TRENDS IN CELL BIOLOGY, 1997, 7 (06) : 220 - 225
  • [4] ADAMs: focus on the protease domain
    Black, RA
    White, JM
    [J]. CURRENT OPINION IN CELL BIOLOGY, 1998, 10 (05) : 654 - 659
  • [5] MAMMALIAN SPERM-EGG INTERACTION - IDENTIFICATION OF A GLYCOPROTEIN IN MOUSE EGG ZONAE PELLUCIDAE POSSESSING RECEPTOR ACTIVITY FOR SPERM
    BLEIL, JD
    WASSARMAN, PM
    [J]. CELL, 1980, 20 (03) : 873 - 882
  • [6] PROTEOLYTIC PROCESSING OF A PROTEIN INVOLVED IN SPERM EGG FUSION CORRELATES WITH ACQUISITION OF FERTILIZATION COMPETENCE
    BLOBEL, CP
    MYLES, DG
    PRIMAKOFF, P
    WHITE, JM
    [J]. JOURNAL OF CELL BIOLOGY, 1990, 111 (01) : 69 - 78
  • [7] Metalloprotease-disintegrins: Links to cell adhesion and cleavage of TNF alpha and notch
    Blobel, CP
    [J]. CELL, 1997, 90 (04) : 589 - 592
  • [8] Evidence that a functional fertilin-like ADAM plays a role in human sperm-oolemmal interactions
    Bronson, RA
    Fusi, FM
    Calzi, F
    Doldi, N
    Ferrari, A
    [J]. MOLECULAR HUMAN REPRODUCTION, 1999, 5 (05) : 433 - 440
  • [9] Mediation of sperm-egg fusion:: evidence that mouse egg α6β1 integrin is the receptor for sperm fertilinβ
    Chen, H
    Sampson, NS
    [J]. CHEMISTRY & BIOLOGY, 1999, 6 (01): : 1 - 10
  • [10] Analysis of mouse fertilin in wild-type and fertilin β-/- sperm:: Evidence for C-terminal modification, α/β dimerization, and lack of essential role of fertilin α in sperm-egg fusion
    Cho, CH
    Ge, HY
    Branciforte, D
    Primakoff, P
    Myles, DG
    [J]. DEVELOPMENTAL BIOLOGY, 2000, 222 (02) : 289 - 295