Identification of a novel GPI‐anchored CRISP glycoprotein, MAK248, located on the posterior head and equatorial segment of cynomolgus macaque sperm

Yudin, Ashley I.; Li, M. W.; Robertson, Kathryn; Tollner, Theodore L.; Cherr, Gary N.; Overstreet, James W.

doi:10.1002/mrd.10193

Cited by 19 publications

(24 citation statements)

References 87 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In contrast, our results suggest that HrUrabin plays a pivotal role in the primary binding of sperm to HrVC70, a sperm receptor on the VC, rather than gamete fusion, during fertilization. In macaque, it is reported that an antibody raised against sperm surface protein, which is released by treatment with PI-PLC, revealed the existence of GPI-anchored CRISP on the sperm membrane, possibly participating in fertilization (25). This protein exists in two isoforms with molecular masses of 24 and 48 kDa, similarly to HrUrabin, although they assumed that the 48-kDa isoform is a dimer of the 24-kDa isoform (25).…”

Section: Difference In the Results By Far Western Analysis And Yeastmentioning

confidence: 99%

“…In macaque, it is reported that an antibody raised against sperm surface protein, which is released by treatment with PI-PLC, revealed the existence of GPI-anchored CRISP on the sperm membrane, possibly participating in fertilization (25). This protein exists in two isoforms with molecular masses of 24 and 48 kDa, similarly to HrUrabin, although they assumed that the 48-kDa isoform is a dimer of the 24-kDa isoform (25). As mentioned above, CRISP members on the sperm surface seem to play diverse roles in fertilization in different species.…”

Section: Difference In the Results By Far Western Analysis And Yeastmentioning

confidence: 99%

See 1 more Smart Citation

Ascidian Sperm Glycosylphosphatidylinositol-anchored CRISP-like Protein as a Binding Partner for an Allorecognizable Sperm Receptor on the Vitelline Coat

Urayama

Harada

Nakagawa

et al. 2008

Journal of Biological Chemistry

View full text Add to dashboard Cite

Although ascidians are hermaphroditic, many species including Halocynthia roretzi are self-sterile. We previously reported that a vitelline coat polymorphic protein HrVC70, consisting of 12 EGF (epidermal growth factor)-like repeats, is a candidate allorecognition protein in H. roretzi, because the isolated HrVC70 shows higher affinity to nonself-sperm than to self-sperm. Here, we show that a sperm 35-kDa glycosylphosphatidylinositol-anchored CRISP (cysteine-rich secretory protein)-like protein HrUrabin in a low density detergentinsoluble membrane fraction is a physiological binding partner for HrVC70. We found that HrVC70 specifically interacts with HrUrabin, which had been separated by SDS-PAGE and transferred onto a nitrocellulose membrane. HrUrabin has an N-linked sugar chain, essential for binding to HrVC70. HrUrabin mRNA is expressed in the testis but not in the ovary, and the protein appears to be localized on the surface of sperm head and tail. Anti-HrUrabin antibody, which neutralizes the interaction between HrUrabin and HrVC70, potently inhibited fertilization and allorecognizable sperm-binding to HrVC70-agarose. However, no significant difference in the binding ability of HrUrabin to HrVC70 was observed in autologous and allogeneic combinations by Far Western analyses. These results indicate that sperm-egg binding in H. roretzi is mediated by the molecular interaction between HrUrabin on the sperm surface and HrVC70 on the vitelline coat, but that HrUrabin per se is unlikely to be a direct allorecognition protein.Ascidians, the invertebrate chordates, are hermaphroditic animals releasing gametes nearly simultaneously during the spawning season. Most ascidians show self-sterility or preference for "non-autologous" (allogeneic) fertilization (1, 2), which appears to be beneficial for the achievement of genetic diversity in the next generation. However, the mechanism of self-sterility during ascidian fertilization is a long-standing enigma. In the early part of the 20th century, Morgan (3-6) studied this problem using the solitary ascidian Ciona intestinalis, and found that a barrier against self-fertilization is abolished by the treatment of eggs with weak acid (citrus juice) or protease (pancreatic extract) (3). Because the vitelline coat (VC) 3 -free naked eggs are self-fertile, he proposed that a self/nonself-recognition molecule must reside on the VC or test cells. Later, it was found that only nonself-sperm tightly and specifically bound to the VC of glycerinated eggs in C. intestinalis (7). From these results, it is currently believed that a certain allorecognition molecule responsible for self-sterility must reside on the VC.We have been studying the mechanism of self-sterility using another solitary ascidian, Halocynthia roretzi, because a large quantity of readily fertilizable gametes can be easily obtained from this species, which is aqua-cultured in Japan for human consumption (8). Although H. roretzi exhibits much more strict self-sterility than C. intestinalis, the mode of self-sterility in...

show abstract

Section: Difference In the Results By Far Western Analysis And Yeastmentioning

confidence: 99%

Section: Difference In the Results By Far Western Analysis And Yeastmentioning

confidence: 99%

Ascidian Sperm Glycosylphosphatidylinositol-anchored CRISP-like Protein as a Binding Partner for an Allorecognizable Sperm Receptor on the Vitelline Coat

Urayama

Harada

Nakagawa

et al. 2008

Journal of Biological Chemistry

View full text Add to dashboard Cite

show abstract

“…Cynomolgus macaque sperm have a constituent population of GPI-anchored (glyco)proteins that are released after exposure to phosphatidylinositol-specific phospholipase C (PI-PLC) [18]. Because this group of membrane proteins is completely exposed to the external environment, they have been used to elicit an isoimmune response in female macaques [18].…”

Section: Introductionmentioning

confidence: 99%

“…Because this group of membrane proteins is completely exposed to the external environment, they have been used to elicit an isoimmune response in female macaques [18]. Following immunization with these PI-PLC-released proteins, together with five different adjuvants, only two glycoproteins (24 and 53 kDa) were consistently recognized as potent isoantigens [18]. The 24-kDa protein was found to be a GPI-anchored CRISP glycoprotein called MAK248, and it has been described in detail previously [18].…”

Section: Introductionmentioning

confidence: 99%

ESP13.2, a Member of the -Defensin Family, Is a Macaque Sperm Surface-Coating Protein Involved in the Capacitation Process

Yudin

Tollner

et al. 2003

Biology of Reproduction

View full text Add to dashboard Cite

Female macaques produced isoantibodies to a limited number of sperm surface proteins following immunization with sperm components released by phosphatidylinositol-specific phospholipase C (PI-PLC). Washed, acrosome-intact, fixed sperm injected into rabbits elicited a major immune response to one of the same PI-PLC-released proteins, which was shown to be a sperm surface-coating protein. After purification and digestion of the glycoprotein, four peptides were analyzed for amino acid sequence, and all had 100% homology with an epididymal secretory protein, ESP13.2, reported previously to be a small, cationic-rich peptide and a member of the beta-defensin family. Antibodies to purified ESP13.2 recognized a number of protein bands on Western blots of nonreduced PI-PLC-released sperm components and nonreduced whole-sperm extracts. After chemical disulfide reduction, only a single, broad band from 31 to 35 kDa was recognized by anti-ESP13.2 antibodies. Indirect immunofluorescence showed ESP13.2 over the entire surface of ejaculated macaque sperm. Fluorescence was only slightly reduced after sperm were washed through 80% Percoll. A 24-h incubation in capacitating medium significantly reduced the amount of ESP13.2 over the head and midpiece, whereas exposure of the incubated sperm to dbcAMP and caffeine (capacitation activators) resulted in almost complete loss of ESP13.2 from the sperm surface. After activation, ESP13.2 was the primary component released into the medium as judged electrophoretically. Lignosulfonic acid, a potent inhibitor of macaque fertilization in vitro, completely blocked release of ESP13.2 from the sperm surface, even following treatment with activators. These findings suggest that the beta-defensin, ESP13.2, has a function in the capacitation of macaque spermatozoa and may modulate sperm surface-receptor presentation at the time of fertilization.

show abstract

“…This 35-kDa GPI-anchored glycoprotein, referred to as HrUrabin (Halocynthia roretzi unique lipid rafts-derived binding partner), showed a sequence homology to a CRISP (Cys-rich secretory protein) family, some members of which are known to play roles in fertilization (Yudin et al, 2002;Ellerman et al, 2006;Roberts et al, 2006). We showed that HrUrabin also has a function in fertilization, since an antibody against HrUrabin specifically inhibited fertilization.…”

Section: Hrurabin a Sperm Binding Partner Of Hrvc70mentioning

confidence: 85%

Allorecognition mechanisms during ascidian fertilization

Harada¹,

Sawada²

2008

Int. J. Dev. Biol.

View full text Add to dashboard Cite

Ascidians (primitive chordates) are hermaphroditic animals, releasing sperm and eggs nearly simultaneously. But, many ascidians, including Ciona intestinalis and Halocynthia roretzi, show self-sterility or preference for cross-fertilization rather than self-fertilization. The molecular mechanisms underlying this allorecognition process are only poorly understood. We recently identified the genes responsible for self-incompatibility in C. intestinalis by a positional cloning: sperm-borne polycystin 1-like receptor, referred to as s-Themis, and its fibrinogen-like ligand called v-Themis on the vitelline coat (VC) are highly polymorphic and appear to be responsible for allorecognition in the fertilization of C. intestinalis. In H. roretzi, on the other hand, we revealed that HrVC70, a 70-kDa main component of the VC consisting of 12 epidermal-growthfactor (EGF)-like repeats, is a candidate allorecognition protein, since the attachment of this protein to the VC during oocyte maturation and its detachment by weak acid are closely linked to the gain and the loss of self-sterility, respectively, and also since nonself-sperm rather than selfsperm efficiently bound to HrVC70-agarose. As a binding partner of HrVC70, a 35-kDa GPIanchored glycoprotein in sperm lipid rafts, referred to as HrUrabin, was identified: HrUrabin appears to play a key role in allorecognizable sperm binding to HrVC70 during fertilization. In the present review, we describe the current progress on the molecular bases of allorecognition, or self-incompatibility, during ascidian fertilization, by considering the SI systems in another organisms including fungies and flowering plants.

show abstract

Identification of a novel GPI‐anchored CRISP glycoprotein, MAK248, located on the posterior head and equatorial segment of cynomolgus macaque sperm

Cited by 19 publications

References 87 publications

Ascidian Sperm Glycosylphosphatidylinositol-anchored CRISP-like Protein as a Binding Partner for an Allorecognizable Sperm Receptor on the Vitelline Coat

Ascidian Sperm Glycosylphosphatidylinositol-anchored CRISP-like Protein as a Binding Partner for an Allorecognizable Sperm Receptor on the Vitelline Coat

ESP13.2, a Member of the -Defensin Family, Is a Macaque Sperm Surface-Coating Protein Involved in the Capacitation Process

Allorecognition mechanisms during ascidian fertilization

Contact Info

Product

Resources

About