YWK-II protein/APLP2 in mouse gametes: Potential role in fertilization

Zhuang, Dazhong; Qiao, Yuan; Zhang, Xiaodong; Miao, Shiying; Koide, S. S.; Wang, Linfang

doi:10.1002/mrd.20380

Cited by 8 publications

(8 citation statements)

References 29 publications

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“…The N-terminus of the APLPs inherits a 22 amino acid high affinity binding site for glycosaminoglycans [66] and therefore might act as a cell adhesion molecule which probably involves binding to the extracellular matrix. This is consistent with APLP2's function in fertilization: APLP2 is found in sperm membranes (designated also as YWK-II, [67]) and a polypeptide from its ectodomain blocked sperm-egg membrane fusion [68]. Antibodies raised against the extracellular domain of APLP2 confirmed the importance of the N-terminus of APLP2 for fertility [69].…”

Section: Consequences Of Aplp Proteolytic Pro-cessing For Cellular Fusupporting

confidence: 74%

The Role of the Anti-Amyloidogenic Secretase ADAM10 in Shedding the APP-like Proteins

Fahrenholz¹

2012

CAR

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ADAM10 (A disintegrin and metalloproteinase 10) has been demonstrated as an enzyme with protective properties in Alzheimer's disease: in mouse models it not only lowered generation of toxic A-beta peptides and formation of senile plaques but also alleviated learning deficits and enhanced synaptic density. This is due to cleavage of the amyloid precursor protein (APP) within its A-beta stretch and to the release of the extracellular domain of APP with neuroprotective function. Aside from cleaving APP, ADAM10 has been linked to over 40 putative substrates at least in cell culture. These substrates are connected with important cellular functions such as cell migration, stress response and transport. For this contribution we focussed on ADAM10 acting on the APP-like proteins since for some of their representatives - in particular APLP2 and APP-L - a shedding by ADAM10 has been demonstrated in vivo. In addition, the importance of these proteins, especially of APLP2, has been repeatedly shown by intense analysis of double and triple transgenic mice which lack APP in combination with one or both APLPs: several phenotypes such as defects in migration of neuroblasts, in formation of synapses and synaptic transmission have been reported. However, the specific contribution of either the uncleaved full-length proteins or their extracellular domains secreted upon ADAM10 activity has not been elucidated. In this review, we report on recent findings concerning shedding of APP-like proteins and resulting functional consequences.

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Section: Consequences Of Aplp Proteolytic Pro-cessing For Cellular Fusupporting

confidence: 74%

The Role of the Anti-Amyloidogenic Secretase ADAM10 in Shedding the APP-like Proteins

Fahrenholz¹

2012

CAR

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“…Three different YWK-II transcripts are expressed in the testis at various stages of germ cell differentiation. In mature spermatozoa, the protein is found in the plasma membrane overlying the acrosome (Huang et al, 2000;Zhuang et al, 2006). Segment 22-308 of the extracellular region of YWK-II appears to participate in the binding and fusion of spermatozoa with the egg plasma membrane (Zhuang et al, 2006).…”

mentioning

confidence: 97%

“…In mature spermatozoa, the protein is found in the plasma membrane overlying the acrosome (Huang et al, 2000;Zhuang et al, 2006). Segment 22-308 of the extracellular region of YWK-II appears to participate in the binding and fusion of spermatozoa with the egg plasma membrane (Zhuang et al, 2006). Sperm b1,4-galactosyltransferase I (B4GALT1) [ID: T3-500] is a receptor for the zona pellucida (ZP) (Shur and Hall, 1982).…”

mentioning

confidence: 98%

Surfing the wave, cycle, life history, and genes/proteins expressed by testicular germ cells. Part 3: Developmental changes in spermatid flagellum and cytoplasmic droplet and interaction of sperm with the zona pellucida and egg plasma membrane

Hermo¹,

Pelletier²,

Cyr³

et al. 2009

Microscopy Res & Technique

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Spermiogenesis constitutes the steps involved in the metamorphosis of spermatids into spermatozoa. It involves modification of several organelles in addition to the formation of several structures including the flagellum and cytoplasmic droplet. The flagellum is composed of a neck region and middle, principal, and end pieces. The axoneme composed of nine outer microtubular doublets circularly arranged to form a cylinder around a central pair of microtubules is present throughout the flagellum. The middle and principal pieces each contain specific components such as the mitochondrial sheath and fibrous sheath, respectively, while outer dense fibers are common to both. A plethora of proteins are constituents of each of these structures, with each playing key roles in functions related to the fertility of spermatozoa. At the end of spermiogenesis, a portion of spermatid cytoplasm remains associated with the released spermatozoa, referred to as the cytoplasmic droplet. The latter has as its main feature Golgi saccules, which appear to modify the plasma membrane of spermatozoa as they move down the epididymal duct and hence may be partly involved in male gamete maturation. The end product of spermatogenesis is highly streamlined and motile spermatozoa having a condensed nucleus equipped with an acrosome. Spermatozoa move through the female reproductive tract and eventually penetrate the zona pellucida and bind to the egg plasma membrane. Many proteins have been implicated in the process of fertilization as well as a plethora of proteins involved in the development of spermatids and sperm, and these are high lighted in this review.

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“…Since YWK-II protein was located on spermatozoa and eggs (20), their relative importance in sperm-egg membrane fusion was examined. Capacitated spermatozoa and zona-free eggs were incubated separately with purified GST-Fa, GST-Fb or GST for 15 min.…”

Section: Ywk-ii Protein On the Plasma Membrane Of Oocytes Accounted Fmentioning

confidence: 99%

Delineation of the functional domains of the extracellular region of YWK-II Protein/APLP2 of sperm membrane

Zhuang

Wang²,

Yang³

et al. 2006

Front Biosci

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The sperm membrane protein, designated as YWK-II protein/APLP2, is a member of the amyloid precursor protein (APP) superfamily and is a type I transmembrane protein involved in fertilization. Here, the structure-function of the domains of YWK-II protein was examined. Five segments with overlapping ends encompassing the entire extracellular region of mouse YWK-II gene were prepared, cloned and separately expressed in E. coli. The recombinant YWK-II segments were fused with glutathione S-transferase (GST), purified and evaluated for their antifertility activities by measuring their capacity to block in vitro mouse sperm-egg interaction. The structural domain(s) involved in the fertilization process was identified. The polypeptide segment corresponding to position 22-207 of YWK-II-763 inhibited the early stage of fertilization when the spermatozoa interacted with zona-free eggs; whereas the polypeptide segment 201-395 (lacking 309-364) of YWK-II-763 blocked sperm-egg membrane fusion. The remaining three segments, 201-395, 389-574 and 517-704 (lacking 613-624) of YWK-II-763, did not influence the in vitro fertilization process. The present results suggest that segment 22-308 of YWK-II-763 participates in the binding and fusion of sperm and egg plasma membranes thereby promoting fertilization.

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YWK-II protein/APLP2 in mouse gametes: Potential role in fertilization

Cited by 8 publications

References 29 publications

The Role of the Anti-Amyloidogenic Secretase ADAM10 in Shedding the APP-like Proteins

The Role of the Anti-Amyloidogenic Secretase ADAM10 in Shedding the APP-like Proteins

Surfing the wave, cycle, life history, and genes/proteins expressed by testicular germ cells. Part 3: Developmental changes in spermatid flagellum and cytoplasmic droplet and interaction of sperm with the zona pellucida and egg plasma membrane

Delineation of the functional domains of the extracellular region of YWK-II Protein/APLP2 of sperm membrane

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