Human SP-10: Acrosomal Distribution, Processing, and Fate after the Acrosome Reaction1

Foster, James A.; Klotz, Kenneth L.; Flickinger, Charles J.; Thomas, Ted S.; Wright, Richard M.; Castillo, James R.; Herr, John C.

doi:10.1095/biolreprod51.6.1222

Cited by 64 publications

(49 citation statements)

References 16 publications

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“…The general lysis and extraction procedure used has the advantage that it provides a general idea of the types of proteins that constitute the sperm proteome. Therefore, this approach should be complementary to other proteomic approaches focusing on specific compartments or organelles such as the cytoplasm, membrane, cytoskeleton, tail, acrosome or sperm head [8][9][10][11][24][25][26][27][28].…”

Section: Resultsmentioning

confidence: 99%

See 1 more Smart Citation

Proteomic identification of human sperm proteins

Martínez-Heredia¹,

Estanyol²,

Ballescà³

et al. 2006

Proteomics

233

177

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Conventional 1-DE has in the past provided a wealth of information concerning the major sperm proteins. However, so far there are relatively few reports exploiting the potential of the present proteomic tools to identify and to study additional yet-unidentified important proteins present in human spermatozoa. In the present work, 2-DE of proteins extracted from human normozoospermic spermatozoa led to the resolution of over 1000 spots. Subsequent excision from the gels of 145 spots and MALDI-TOF MS analysis allowed the identification of 98 different proteins. The function of these proteins turned out to be energy production (23%), transcription, protein synthesis, transport, folding and turnover (23%), cell cycle, apoptosis and oxidative stress (10%), signal transduction (8%), cytoskeleton, flagella and cell movement (10%), cell recognition (7%), metabolism (6%) and unknown function (11%). As many as 23% of the proteins identified have not been previously described as being expressed in human spermatozoa. The present data provide an important clue towards determining the function of these proteins and opens up the possibility to perform additional experiments.

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Section: Resultsmentioning

confidence: 99%

“…In man, specific approaches to target subcellular organelles or compartments have been successfully used [11,[24][25][26][27][28]. A 2-D protein map of the human sperm head has been described, but without MS identification [29].…”

Section: Introductionmentioning

confidence: 99%

Proteomic identification of human sperm proteins

Martínez-Heredia¹,

Estanyol²,

Ballescà³

et al. 2006

Proteomics

233

177

View full text Add to dashboard Cite

show abstract

“…A BLASTP run (9) against the National Center for Biotechnology Information's nr database (http:͞͞www.ncbi.nlm.nih.gov͞ blast͞) by using the PATE putative protein sequence resulted in hits to the acrosomal vesicle proteins, SP-10, with e-scores between 0.003 and 0.07. The acrosomal vesicle protein SP-10 may be involved in sperm-zona binding and penetration (10). The aligned part of the SP-10 protein belongs to a snake toxin family of proteins according to the sequence-based protein classification database Pfam (11).…”

Section: Discussionmentioning

confidence: 99%

PATE,a gene expressed in prostate cancer, normal prostate, and testis, identified by a functional genomic approach

Bera

Maitra

Iavarone

et al. 2002

Proc. Natl. Acad. Sci. U.S.A.

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To identify target antigens for prostate cancer therapy, we have combined computer-based screening of the human expressed sequence tag database and experimental expression analysis to identify genes that are expressed in normal prostate and prostate cancer but not in essential human tissues. Using this approach, we identified a gene that is expressed specifically in prostate cancer, normal prostate, and testis. The gene has a 1.5-kb transcript that encodes a protein of 14 kDa. We named this gene PATE (expressed in prostate and testis). In situ hybridization shows that PATE mRNA is expressed in the epithelial cells of prostate cancers and in normal prostate. Transfection of the PATE cDNA with a Myc epitope tag into NIH 3T3 cells and subsequent cell fractionation analysis shows that the PATE protein is localized in the membrane fraction of the cell. Analysis of the amino acid sequence of PATE shows that it has structural similarities to a group of proteins known as three-finger toxins, which includes the extracellular domain of the type ␤ transforming growth factor receptor. Restricted expression of PATE makes it a potential candidate for the immunotherapy of prostate cancer.immunotherapy ͉ cancer vaccine ͉ snake toxin ͉ membrane protein P rostate cancer is the most frequently diagnosed noncutaneous cancer and the second leading cause of cancer deaths in men. It has been estimated that about one in five men in the United States will develop prostate cancer during their lifetime, and, to date, there are no curative therapies available for this disease after it has metastasized from its site of origin.

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“…By immunoelectron microscopy, zonadhesin localizes to the perimeter of the acrosome in intact ejaculated boar spermatozoa or cauda epididymal hamster sperm, and to the leading edge of acrosomal matrix overlying cells with disrupted acrosomal membranes (Bi et al, 2003, Olson et al, 2004. On the other hand, SP-10 is most abundant within the principal segment and posterior bulb of the equatorial segment of the human sperm acrosome (Foster et al, 1994).…”

Section: Compartmentalization Within the Acrosomal Matrixmentioning

confidence: 99%

“…In humans a 45,000 M r precursor is proteolytically processed to polymorphic forms ranging from 18,000-34,000 M r in mature sperm (Foster et al, 1994, Herr et al, 1990. SP-10 antibodies interfere with sperm binding to the zona pellucida in bovine in vitro fertilization, suggesting that SP-10 functions in sperm-zona pellucida interactions (Coonrod et al, 1996).…”

Section: Sp10mentioning

confidence: 99%

The role of the acrosomal matrix in fertilization

Buffone

Foster²,

Gerton³

2008

Int. J. Dev. Biol.

Self Cite

112

107

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Mammalian sperm must have properly formed acrosomes to be fully functional in the process of binding and penetrating the zona pellucida (ZP), the extracellular matrix surrounding the egg. There is much evidence to raise doubts about the old "bag of enzymes" paradigm of acrosomal function, although this is the model that seems to prevail. We concur with other scientists that acrosomal exocytosis is not an all or none event where the acrosome is either "intact" or "reacted". As determined by transmission electron microscopy of human sperm undergoing acrosomal exocytosis, six stages can be identified, with the intermediate ones involving loss of acrosomal matrix material. In the mouse, there is a temporal relationship among four stages of acrosomal exocytosis. Numerous evidences suggest a more complex role for the acrosome in fertilization in which the acrosomal matrix is a scaffold for sperm-ZP interactions that self-regulates by a controlled disassembly mechanism.

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Human SP-10: Acrosomal Distribution, Processing, and Fate after the Acrosome Reaction1

Cited by 64 publications

References 16 publications

Proteomic identification of human sperm proteins

Proteomic identification of human sperm proteins

PATE,a gene expressed in prostate cancer, normal prostate, and testis, identified by a functional genomic approach

The role of the acrosomal matrix in fertilization

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