Epididymal secreted protein Crisp-1 and sperm function

Roberts, Kenneth P.; Ensrud, Kathy M.; Wooters, Joseph; Nolan, Michael A.; Johnston, Daniel St; Hamilton, David W.

doi:10.1016/j.mce.2005.12.034

Cited by 63 publications

(38 citation statements)

References 37 publications

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“…1). Examples identified through biochemical investigation include GPIanchored proteins (bull: SPAM1 (Morin et al 2010); mouse: PH20 (Thaler & Cardullo 1995) and rat: 2B1 glycoprotein (Seaton et al 2000)), proteins showing carbonyl reductase activity (hamster: P26h (Montfort et al 2002) and pig ), cysteinerich secretory proteins (mouse and rat: CRISP1 (Roberts et al 2006, Busso et al 2007, Da Ros et al 2008) as well as the secreted protein containing N-terminal Notch-like type II EGF repeats and C-terminal discoidin/F5/8 C domains type 1 (SED1 in human and rodents (Ensslin & Shur 2003, Shur et al 2006, Copland et al 2009) and its porcine and bovine homologues, p47 and lactadherin, respectively (Ensslin et al 1998, and in the pig the spermadhesin AQN3, which is secreted in part from the cauda epididymis and mainly from the seminal vesicles . Integral membrane proteins of testicular origin such as proteins of a disintegrin and metalloprotease (ADAM) family have also been described to function in spermoocyte interaction and fertilisation (Evans 2001).…”

Section: Physiological Alterations Of the Sperm Surfacementioning

confidence: 99%

Sperm surface changes and physiological consequences induced by sperm handling and storage

2011

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Spermatozoa interact with their immediate environment and this contact remodels the sperm surface in preparation for fertilisation. These fundamental membrane changes will be critically covered in this review with special emphasis on the very specific surface destabilisation event, capacitation. This process involves very subtle and intricate modifications of the sperm membrane including removal of suppression (decapacitation) factors and changes in the lateral organisation of the proteins and lipids of the sperm surface. Processing of sperm for assisted reproduction (storage, sex-sorting, etc.) subjects spermatozoa to numerous stressors, and it is possible that this processing overrides such delicate processes resulting in sperm instability and cell damage. To improve sperm quality, novel mechanisms must be used to stabilise the sperm surface during handling. In this review, different types of membrane stress are considered, as well as novel surface manipulation methods to improve sperm stability.

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Section: Physiological Alterations Of the Sperm Surfacementioning

confidence: 99%

Sperm surface changes and physiological consequences induced by sperm handling and storage

2011

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“…Cysteine-rich secretory proteins (CRISPs) are single-chain secreted proteins with molecular weights of 20-30 kDa which are characterized by a high cysteine content, especially in their C-terminal third (Yamazaki & Morita, 2004;Roberts et al, 2006). The first described CRISP was protein D/E (also known as acidic epididymal glycoprotein, sperm coating protein and CRISP-1) from rat epididymis (Cameo & Blaquier, 1976;Brooks et al, 1986).…”

Section: Introductionmentioning

confidence: 99%

Structures of pseudechetoxin and pseudecin, two snake-venom cysteine-rich secretory proteins that target cyclic nucleotide-gated ion channels: implications for movement of the C-terminal cysteine-rich domain

Suzuki

Yamazaki

Brown

et al. 2008

Acta Crystallogr D Biol Crystallogr

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Cyclic nucleotide-gated (CNG) ion channels play pivotal roles in sensory transduction by retinal photoreceptors and olfactory neurons. The elapid snake toxins pseudechetoxin (PsTx) and pseudecin (Pdc) are the only known protein blockers of CNG channels. These toxins belong to a cysteinerich secretory protein (CRISP) family containing an N-terminal pathogenesis-related proteins of group 1 (PR-1) domain and a C-terminal cysteine-rich domain (CRD). PsTx and Pdc are highly homologous proteins, but their blocking affinities on CNG channels are different: PsTx blocks both the olfactory and retinal channels with $15-30-fold higher affinity than Pdc. To gain further insights into their structure and function, the crystal structures of PsTx, Pdc and Zn 2+-bound Pdc were determined. The structures revealed that most of the amino-acid-residue differences between PsTx and Pdc are located around the concave surface formed between the PR-1 domain and the CRD, suggesting that the concave surface is functionally important for CNG-channel binding and inhibition. A structural comparison in the presence and absence of Zn 2+ ion demonstrated that the concave surface can open and close owing to movement of the CRD upon Zn 2+ binding. The data suggest that PsTx and Pdc occlude the pore entrance and that the dynamic motion of the concave surface facilitates interaction with the CNG channels.

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“…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.

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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.

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Epididymal secreted protein Crisp-1 and sperm function

Cited by 63 publications

References 37 publications

Sperm surface changes and physiological consequences induced by sperm handling and storage

Sperm surface changes and physiological consequences induced by sperm handling and storage

Structures of pseudechetoxin and pseudecin, two snake-venom cysteine-rich secretory proteins that target cyclic nucleotide-gated ion channels: implications for movement of the C-terminal cysteine-rich domain

Allorecognition mechanisms during ascidian fertilization

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