Molecules Involved in Mammalian Sperm-Egg Interaction

Mcleskey, S. B.; Dowds, C. Marie; Carballada, Rosa; White, Rebekah R.; Saling, Patricia M.

doi:10.1016/s0074-7696(08)62231-7

Cited by 181 publications

(132 citation statements)

References 260 publications

Supporting

Mentioning

125

Contrasting

Unclassified

Order By: Relevance

“…Although a large number of potential candidate binding partners for sperm-egg interaction have been described, including galactyltransferase, Sp56, zona receptor kinase, spermadhesins, PH20, proacrosin, Sp38, and Sp17, the precise roles of these molecules have not been firmly established (43). Hence, the identification of additional molecules that participate in gamete interactions, particularly those retained after the remodeling events of acrosomal exocytosis, could greatly enhance the understanding of this process.…”

Section: Discussionmentioning

confidence: 99%

SAMP14, a Novel, Acrosomal Membrane-associated, Glycosylphosphatidylinositol-anchored Member of the Ly-6/Urokinase-type Plasminogen Activator Receptor Superfamily with a Role in Sperm-Egg Interaction

Shetty

Wolkowicz

Digilio

et al. 2003

Journal of Biological Chemistry

100

View full text Add to dashboard Cite

We report a new member of the Ly-6/urokinase-type plasminogen activator receptor (uPAR) superfamily of receptors, SAMP14, which is retained on the inner acrosomal membrane of the human spermatozoan following the acrosome reaction and may play a role in fertilization. The SAMP14 sequence predicted a glycosylphosphatidylinositol (GPI)-anchored protein with a signal peptide, a transmembrane domain near the carboxyl terminus, and a putative transamidase cleavage site in the proprotein. Attachment of SAMP14 to the membrane by a lipid anchor was confirmed by its sensitivity to phosphatidylinositol phospholipase C. SAMP14 has a single functional domain similar to the Ly-6 and urokinase plasminogen activator receptor superfamily of proteins, and the gene mapped to 19q13.33, near the PLAUR locus for uPAR at 19q13.2. Northern and dot blotting showed that SAMP14 expression was testis-specific. Indirect immunofluorescence and immunoelectron microscopy with antisera to purified recombinant SAMP14 localized the protein to outer and inner acrosomal membranes as well as the acrosomal matrix of ejaculated human sperm. Acrosome-reacted sperm demonstrated SAMP14 immunofluorescence, indicating its retention on the inner acrosomal membrane following the acrosome reaction. However, SAMP14 localized to the entire sperm when unwashed swim-up sperm from the ejaculate were stained, indicating that some SAMP14 is loosely associated with the plasma membrane. Antibodies against recombinant SAMP14 inhibited both the binding and the fusion of human sperm to zona free hamster eggs, suggesting that SAMP14 may have a role in sperm-egg interaction. SAMP14 represents a GPI-anchored putative receptor in the Ly-6/uPAR family that is exposed on the inner acrosomal membrane after the acrosome reaction.

show abstract

Section: Discussionmentioning

confidence: 99%

SAMP14, a Novel, Acrosomal Membrane-associated, Glycosylphosphatidylinositol-anchored Member of the Ly-6/Urokinase-type Plasminogen Activator Receptor Superfamily with a Role in Sperm-Egg Interaction

Shetty

Wolkowicz

Digilio

et al. 2003

Journal of Biological Chemistry

100

View full text Add to dashboard Cite

show abstract

“…PL is a homolog of the egg envelope in other vertebrates, the zona pellucida (ZP) in mammals, the vitelline membrane in amphibians and the chorion in teleosts. The vertebrate's egg envelope serves several functions in the process of fertilization, including species-specific sperm-egg binding, induction of the acrosome reaction, and prevention of polyspermy (McLeskey et al 1998). Although the penetration of the PL by supernumerary spermatozoa is found regularly in birds, the PL behaves in a manner analogous to the ZP in mammalian species (Howarth 1990).…”

Section: Introductionmentioning

confidence: 99%

Molecular characterization of egg envelope glycoprotein ZPD in the ovary of Japanese quail (Coturnix japonica)

Sato

Kinoshita²,

Kansaku³

et al. 2009

Reproduction

View full text Add to dashboard Cite

The egg envelope surrounding avian oocytes exhibits a three-dimensional network of coarse fibers between the granulosa cells and the oocyte. Our previous studies have demonstrated that one of the matrix's components, ZP3, is synthesized in the ovarian granulosa cells. Another component, ZP1, which is critically involved in triggering the sperm acrosome reaction, is synthesized in the liver. We have previously isolated cDNAs encoding quail ZP3 and ZP1, and we now report the isolation of cDNA encoding quail ZPD. By RNase protection assay and in situ hybridization, we have demonstrated that ZPD transcripts are restricted to the granulosa cells of preovulatory follicles. The expression level of ZPD increased progressively during follicular development, and the highest expression was observed in the largest follicles. Western blot analyses using the specific antibody against ZPD indicate that the 40 kDa protein is the authentic ZPD, and the contents of ZPD protein also increased during follicular development. Moreover, we found that the addition of FSH to the culture media enhances the ZPD secretion in the cultured granulosa cells. Two-dimensional gel electrophoresis revealed the presence of several ZPD isoforms with different pI values ranging from 5.5 to 7. Immunohistochemical analyses indicate that the materials recognized with anti-quail ZPD antibody were accumulated in the egg envelope of large yellow follicles. These results demonstrate the presence of ZPD protein in the egg envelope, and that the amount of ZPD in the egg envelope as well as the mRNA in the cells increases at the latter stages of folliculogenesis.

show abstract

“…Cytosolic calcium signaling is involved in the regulation of intracellular pH, which appears to play an important role in secretory processes in response to hormones [9,11]. In addition, an acidic microenvironment is crucial for male fertility since sperm cannot fertilize an egg without proper acidification of the acrosome [12]. Sertoli cells secrete lactate in the presence of glucose [13].…”

Section: Introductionmentioning

confidence: 99%

Pharmacological profile of inhibition of the chloride channels activated by extracellular acid in cultured rat Sertoli cells

et al. 2006

View full text Add to dashboard Cite

-Sertoli cells from mammalian testis are key cells involved in the development and maintenance of stem cell spermatogonia as well as in the secretion of a Cl − and K + -rich fluid into the lumen of seminiferous tubules. The pharmacology and contribution of Cl − channels to the physiology of Sertoli cells were investigated using whole-cell patch clamp and iodide efflux experiments applied to cultured rat Sertoli cells. We characterized an outwardly rectifying Cl − current stimulated by various acid species including the physiologically relevant lactic acid. Using the iodide efflux technique, the pharmacological properties of this Cl − current, noted ICl acid , revealed Ca 2+ -independent inhibition by DIDS (IC 50 = 27 µM), glibenclamide (IC 50 = 31 µM) and DPC (IC 50 = 86 µM). ICl acid was neither affected by calix[4]arene nor by 9-AC. The order of potency for inhibition of ICl acid is DIDS ≈ glibenclamide > DPC >> calix[4]arene, 9-AC. For comparison, the inhibitory profile of the swelling-and ATP-activated Cl − currents in Sertoli cells is DPC = DIDS >> glibenclamide = 9-AC for ICl swell and DPC = 9-AC = DIDS >> glibenclamide for ICl ATP . This description provides new insights into the physiology and pharmacology of the endogenous Cl − channels expressed and potentially involved in fluid secretion in Sertoli cells.Cl − channels / pharmacology / proton-activation / ATP / cell volume / glibenclamide

show abstract

Molecules Involved in Mammalian Sperm-Egg Interaction

Cited by 181 publications

References 260 publications

SAMP14, a Novel, Acrosomal Membrane-associated, Glycosylphosphatidylinositol-anchored Member of the Ly-6/Urokinase-type Plasminogen Activator Receptor Superfamily with a Role in Sperm-Egg Interaction

SAMP14, a Novel, Acrosomal Membrane-associated, Glycosylphosphatidylinositol-anchored Member of the Ly-6/Urokinase-type Plasminogen Activator Receptor Superfamily with a Role in Sperm-Egg Interaction

Molecular characterization of egg envelope glycoprotein ZPD in the ovary of Japanese quail (Coturnix japonica)

Pharmacological profile of inhibition of the chloride channels activated by extracellular acid in cultured rat Sertoli cells

Contact Info

Product

Resources

About