Identification of bovine sperm acrosomal proteins that interact with a 32-kDa acrosomal matrix protein

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• 作者：Subir K. Nagdas ; Linda Smith ; Ilza Medina-Ortiz…
• 关键词：Bovine sperm ; Acrosome ; acrosomal protein ; Lactadherin–SPACA3–IZUMO1
• 刊名：Molecular and Cellular Biochemistry
• 出版年：2016
• 出版时间：March 2016
• 年：2016
• 卷：414
• 期：1-2
• 页码：153-169
• 全文大小：2,122 KB
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• 作者单位：Subir K. Nagdas (1)
  Linda Smith (1)
  Ilza Medina-Ortiz (1)
  Luisa Hernandez-Encarnacion (1)
  Samir Raychoudhury (2)
  
  1. Department of Chemistry and Physics, Fayetteville State University, 1200 Murchison Road, Fayetteville, NC, 28301, USA
  2. Department of Biology, Chemistry and Environmental Health Science, Benedict College, Columbia, SC, 29204, USA
  
• 刊物类别：Biomedical and Life Sciences
• 刊物主题：Life Sciences
  Biochemistry
  Medical Biochemistry
  Oncology
  Cardiology
  
• 出版者：Springer Netherlands
• ISSN：1573-4919

文摘

Mammalian fertilization is accomplished by the interaction between sperm and egg. Previous studies from this laboratory have identified a stable acrosomal matrix assembly from the bovine sperm acrosome termed the outer acrosomal membrane–matrix complex (OMC). This stable matrix assembly exhibits precise binding activity for acrosin and N-acetylglucosaminidase. A highly purified OMC fraction comprises three major (54, 50, and 45 kDa) and several minor (38–19 kDa) polypeptides. The set of minor polypeptides (38–19 kDa) termed “OMCrpf polypeptides” is selectively solubilized by high-pH extraction (pH 10.5), while the three major polypeptides (55, 50, and 45 kDa) remain insoluble. Proteomic identification of the OMC32 polypeptide (32 kDa polypeptide isolated from high-pH soluble fraction of OMC) yielded two peptides that matched the NCBI database sequence of acrosin-binding protein. Anti-OMC32 recognized an antigenically related family of polypeptides (OMCrpf polypeptides) in the 38–19-kDa range with isoelectric points ranging between 4.0 and 5.1. Other than glycohydrolases, OMC32 may also be complexed to other acrosomal proteins. The present study was undertaken to identify and localize the OMC32 binding polypeptides and to elucidate the potential role of the acrosomal protein complex in sperm function. OMC32 affinity chromatography of a detergent-soluble fraction of bovine cauda sperm acrosome followed by mass spectrometry-based identification of bound proteins identified acrosin, lactadherin, SPACA3, and IZUMO1. Co-immunoprecipitation analysis also demonstrated the interaction of OMC32 with acrosin, lactadherin, SPACA3, and IZUMO1. Our immunofluorescence studies revealed the presence of SPACA3 and lactadherin over the apical segment, whereas IZUMO1 is localized over the equatorial segment of Triton X-100 permeabilized cauda sperm. Immunoblot analysis showed that a significant portion of SPACA3 was released after the lysophosphatidylcholine (LPC)-induced acrosome reaction, whereas the IZUMO1 and lactadherin polypeptides remain associated to the particulate fraction. Almost entire population of bovine sperm IZUMO1 relocates to the equatorial segment during the LPC-induced acrosome reaction. We propose that the interaction of OMC32 matrix polypeptide with detergent-soluble acrosomal proteins regulates the release of hydrolases/other acrosomal protein(s) during the acrosome reaction.