title: Glioma pathogenesis-related 1-like 1 is testis enriched, dynamically modified, and redistributed during male germ cell maturation and has a potential role in sperm-oocyte binding.
abstract: The glioma pathogenesis-related 1 (GLIPR1) family consists of three genes [GLIPR1, GLIPR1-like 1 (GLIPR1L1), and GLIPR1-like 2 (GLIPR1L2)] and forms a distinct subgroup within the cysteine-rich secretory protein (CRISP), antigen 5, and pathogenesis-related 1 (CAP) superfamily. CAP superfamily proteins are found in phyla ranging from plants to humans and, based largely on expression and limited functional studies, are hypothesized to have roles in carcinogenesis, immunity, cell adhesion, and male fertility. Specifically data from a number of systems suggests that sequences within the C-terminal CAP domain of CAP proteins have the ability to promote cell-cell adhesion. Herein we cloned mouse Glipr1l1 and have shown it has a testis-enriched expression profile. GLIPR1L1 is posttranslationally modified by N-linked glycosylation during spermatogenesis and ultimately becomes localized to the connecting piece of elongated spermatids and sperm. After sperm capacitation, however, GLIPR1L1 is also localized to the anterior regions of the sperm head. Zona pellucida binding assays indicate that GLIPR1L1 has a role in the binding of sperm to the zona pellucida surrounding the oocyte. These data suggest that, along with other members of the CAP superfamily and several other proteins, GLIPR1L1 is involved in the binding of sperm to the oocyte complex. Collectively these data further strengthen the role of CAP domain-containing proteins in cellular adhesion and propose a mechanism whereby CAP proteins show overlapping functional significance during fertilization.
authors.affiliation: Department of Anatomy and Developmental Biology, School of Biomedical Sciences, Monash University, Victoria 3800, Australia.
authors.forename: Gerard M
authors.initials: GM
authors.lastname: Gibbs
authors.forename: Jennifer Chi Yi
authors.initials: JC
authors.lastname: Lo
authors.forename: Brett
authors.initials: B
authors.lastname: Nixon
authors.forename: Duangporn
authors.initials: D
authors.lastname: Jamsai
authors.forename: Anne E
authors.initials: AE
authors.lastname: O'Connor
authors.forename: Sewa
authors.initials: S
authors.lastname: Rijal
authors.forename: L Gabriel
authors.initials: LG
authors.lastname: Sanchez-Partida
authors.forename: Milton T W
authors.initials: MT
authors.lastname: Hearn
authors.forename: Deborah M
authors.initials: DM
authors.lastname: Bianco
authors.forename: Moira K
authors.initials: MK
authors.lastname: O'Bryan
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D015152:Blotting, Northern; D015153:Blotting, Western; D003001:Cloning, Molecular; D018076:DNA, Complementary / Q000737:chemistry / Q000235:genetics; D005260:Female; D005307:Fertilization in Vitro; D020869:Gene Expression Profiling; D006023:Glycoproteins / Q000235:genetics / Q000378:metabolism* / Q000502:physiology; D006031:Glycosylation; D008297:Male; D051379:Mice; D008810:Mice, Inbred C57BL; D008808:Mice, Inbred CBA; D008969:Molecular Sequence Data; D009865:Oocytes / Q000166:cytology / Q000378:metabolism*; D010802:Phylogeny; D017422:Sequence Analysis, DNA; D017386:Sequence Homology, Amino Acid; D013079:Sperm Maturation / Q000502:physiology; D013084:Sperm-Ovum Interactions / Q000502:physiology; D013094:Spermatozoa / Q000166:cytology / Q000254:growth & development / Q000378:metabolism*; D013737:Testis / Q000166:cytology / Q000378:metabolism*; D015044:Zona Pellucida / Q000378:metabolism
chemical_list: D018076:DNA, Complementary; C549825:Glipr1l1 protein, mouse; D006023:Glycoproteins