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Molecular and developmental characterization of a mammalian sperm postacrosomal sheath WW domain-binding protein (PAWP) involved in pronuclear formation during fertilization.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	Molecular and developmental characterization of a mammalian sperm postacrosomal sheath WW domain-binding protein (PAWP) involved in pronuclear formation during fertilization./
作者:	Wu, Alexander Tsang-Hsien.
出版者:	Ann Arbor : ProQuest Dissertations & Theses, : 2005,
面頁冊數:	212 p.
附註:	Source: Dissertations Abstracts International, Volume: 66-12, Section: B.
Contained By:	Dissertations Abstracts International66-12B.
標題:	Cellular biology. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=NQ99831
ISBN:	9780612998315

Molecular and developmental characterization of a mammalian sperm postacrosomal sheath WW domain-binding protein (PAWP) involved in pronuclear formation during fertilization.
Wu, Alexander Tsang-Hsien.

Molecular and developmental characterization of a mammalian sperm postacrosomal sheath WW domain-binding protein (PAWP) involved in pronuclear formation during fertilization. - Ann Arbor : ProQuest Dissertations & Theses, 2005 - 212 p.

Source: Dissertations Abstracts International, Volume: 66-12, Section: B.

Thesis (Ph.D.)--Queen's University (Canada), 2005.

This item must not be sold to any third party vendors.

This study details the cloning, molecular characterization and functional analysis of a non-structural component of the bovine perinuclear theca protein, PAWP (postacrosomal sheath WWI domain binding protein). PAWP is a signalling protein found exclusively in the postacrosomal sheath of the mature spermatozoa. Its N-terminal half region shares a sequence similarity to the N-terminal region of WW domain binding protein 2 (WBP2) which is found in the c-Yes tyrosine kinase pathway. The proline-rich C-terminal region of PAWP contains 2 PY motifs, a conserved binding sequence to group I WW domains and 12 unique self-repeating motifs, YGXPPXG whose function is yet to be elucidated. The PY motif of PAWP was demonstrated to interact with WWI domain in vitro by Far-Western technique. Microinjection of recombinant PAWP protein into metaphase II arrested oocytes caused pronuclear formation. PAWP-mediated pronuclear formation is promoted by the interaction between its PY motif and an oocyte WWI domain containing protein, as dominant negative inhibition of PAWP by its synthetic PY peptide was shown to abolish this interaction. Preliminary PAWP mRNA microinjection data demonstrated that PAWP induced higher rates of oocyte activation and oocyte cleavage compared to its recombinant protein form. In these activated oocytes, PAWP was localized to the nucleolus precursor bodies, leading to the hypothesis that PAWP could function in nucleologenesis during early embryonic development. During spermiogenesis, PAWP was synthesized de novo in the distal cytoplasm and transported rostrally by the manchette and stored on it before manchette descent. The deposition of PAWP and formation of the postacrosomal sheath were observed in the wake of the manchette. The hypothesis of the independent assembly of the postacrosomal sheath and subacrosomal layer was tested by examining the expression patterns of PAWP and tubulin in acrosome-less mouse spermatids caused by the feeding of imino sugar, NB-DNJ. The hypothesis was supported by the observation that PAWP deposition/PAS formation was still mediated by the distal migration of the manchette in the acrosome-less mouse spermatids. This investigation has led to the identification and characterization of a novel sperm postacrosomal-specific protein, PAWP which promotes pronuclear development during mammalian fertilization via an unprecedented interaction between the sperm PY motif to an oocyte WWI domain.

ISBN: 9780612998315Subjects--Topical Terms:

3172791
Cellular biology.
Subjects--Index Terms:

Fertilization

Molecular and developmental characterization of a mammalian sperm postacrosomal sheath WW domain-binding protein (PAWP) involved in pronuclear formation during fertilization.
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500 $a Source: Dissertations Abstracts International, Volume: 66-12, Section: B.
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506 $a This item must not be sold to any third party vendors.
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520 $a This study details the cloning, molecular characterization and functional analysis of a non-structural component of the bovine perinuclear theca protein, PAWP (postacrosomal sheath WWI domain binding protein). PAWP is a signalling protein found exclusively in the postacrosomal sheath of the mature spermatozoa. Its N-terminal half region shares a sequence similarity to the N-terminal region of WW domain binding protein 2 (WBP2) which is found in the c-Yes tyrosine kinase pathway. The proline-rich C-terminal region of PAWP contains 2 PY motifs, a conserved binding sequence to group I WW domains and 12 unique self-repeating motifs, YGXPPXG whose function is yet to be elucidated. The PY motif of PAWP was demonstrated to interact with WWI domain in vitro by Far-Western technique. Microinjection of recombinant PAWP protein into metaphase II arrested oocytes caused pronuclear formation. PAWP-mediated pronuclear formation is promoted by the interaction between its PY motif and an oocyte WWI domain containing protein, as dominant negative inhibition of PAWP by its synthetic PY peptide was shown to abolish this interaction. Preliminary PAWP mRNA microinjection data demonstrated that PAWP induced higher rates of oocyte activation and oocyte cleavage compared to its recombinant protein form. In these activated oocytes, PAWP was localized to the nucleolus precursor bodies, leading to the hypothesis that PAWP could function in nucleologenesis during early embryonic development. During spermiogenesis, PAWP was synthesized de novo in the distal cytoplasm and transported rostrally by the manchette and stored on it before manchette descent. The deposition of PAWP and formation of the postacrosomal sheath were observed in the wake of the manchette. The hypothesis of the independent assembly of the postacrosomal sheath and subacrosomal layer was tested by examining the expression patterns of PAWP and tubulin in acrosome-less mouse spermatids caused by the feeding of imino sugar, NB-DNJ. The hypothesis was supported by the observation that PAWP deposition/PAS formation was still mediated by the distal migration of the manchette in the acrosome-less mouse spermatids. This investigation has led to the identification and characterization of a novel sperm postacrosomal-specific protein, PAWP which promotes pronuclear development during mammalian fertilization via an unprecedented interaction between the sperm PY motif to an oocyte WWI domain.
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