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Identification and function of beta-...

Shi, Xudong.

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Identification and function of beta-1,4-galactosyltransferase associated proteins.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	Identification and function of beta-1,4-galactosyltransferase associated proteins./
作者:	Shi, Xudong.
面頁冊數:	164 p.
附註:	Source: Dissertation Abstracts International, Volume: 64-03, Section: B, page: 1102.
Contained By:	Dissertation Abstracts International64-03B.
標題:	Biology, Molecular. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3086177

Identification and function of beta-1,4-galactosyltransferase associated proteins.
Shi, Xudong.

Identification and function of beta-1,4-galactosyltransferase associated proteins. - 164 p.

Source: Dissertation Abstracts International, Volume: 64-03, Section: B, page: 1102.

Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2003.

Studies in several laboratories demonstrated that sperm surface beta 1,4-galactosyltransferase (GalTase-I) binds to ZP3 and stimulates the acrosome reaction. To study the signaling events activated by GalTase-I, the cytoplasmic domain of GalTase-I was expressed as fusion proteins with maltose binding protein. These expressed fusion proteins and synthetic GalTase-I peptide were used to screen a pig testis phage display cDNA library. Several phage clones that possess high affinity with GalTase-I fusion proteins and synthetic peptide were identified. The identified proteins include a kinase anchor protein 9; rho-associated, coiled-coil containing protein kinase I; actin; sarcolemmal associated protein-3 and a protein has high homology to rhodopsin receptor. The interaction between phage clone and GalTase-I cytoplasmic domain was further tested and confirmed with GalTase-I binding assay and Far-Western assay.Subjects--Topical Terms:

1017719
Biology, Molecular.

Identification and function of beta-1,4-galactosyltransferase associated proteins.
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100 1 $a Shi, Xudong. $3 1637859
245 1 0 $a Identification and function of beta-1,4-galactosyltransferase associated proteins.
300 $a 164 p.
500 $a Source: Dissertation Abstracts International, Volume: 64-03, Section: B, page: 1102.
500 $a Adviser: David J. Miller.
502 $a Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2003.
520 $a Studies in several laboratories demonstrated that sperm surface beta 1,4-galactosyltransferase (GalTase-I) binds to ZP3 and stimulates the acrosome reaction. To study the signaling events activated by GalTase-I, the cytoplasmic domain of GalTase-I was expressed as fusion proteins with maltose binding protein. These expressed fusion proteins and synthetic GalTase-I peptide were used to screen a pig testis phage display cDNA library. Several phage clones that possess high affinity with GalTase-I fusion proteins and synthetic peptide were identified. The identified proteins include a kinase anchor protein 9; rho-associated, coiled-coil containing protein kinase I; actin; sarcolemmal associated protein-3 and a protein has high homology to rhodopsin receptor. The interaction between phage clone and GalTase-I cytoplasmic domain was further tested and confirmed with GalTase-I binding assay and Far-Western assay.
520 $a Dot-blot and GalTase-I binding assay confirmed that actin is associated with GalTase-I <italic>in vitro</italic> in mouse sperm lysate; synthetic GalTase-I cytoplasmic peptide affinity precipitated actin in mouse sperm; furthermore, the affinity precipitation results demonstrated that actin form dimmers after acrosomal reaction; cytochalasin B inhibits actin polymerization also prevent ionphore A 23187 induced mouse sperm acrosomal reaction.
520 $a As an alternative method, synthetic GalTase-I peptide was immobilized to affinity isolate GalTase-I associated proteins in pig sperm lysate. Several proteins were found specifically associated with GalTase-I cytoplasmic domain as demonstrated in SDS-PAGE. Mass spectrometric sequencing determined that one of the proteins identified is homologous to human squamous cell carcinoma antigen.
520 $a In summary, a pig testis phage display cDNA library screening and protein affinity chromatography were applied to identify GalTase-I associated proteins. Several proteins were identified as candidates that interact with GalTase-I and potentially play important roles during fertilization. Deciphering proteins that interact with GalTase-I cytoplasmic domain will greatly enhance our ability to understand the signaling events activated by GalTase-I during the process of fertilization.
590 $a School code: 0090.
650 4 $a Biology, Molecular. $3 1017719
650 4 $a Biology, Cell. $3 1017686
650 4 $a Biology, Microbiology. $3 1017734
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690 $a 0379
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710 2 0 $a University of Illinois at Urbana-Champaign. $3 626646
773 0 $t Dissertation Abstracts International $g 64-03B.
790 1 0 $a Miller, David J., $e advisor
790 $a 0090
791 $a Ph.D.
792 $a 2003
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3086177