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词条 Zona pellucida
释义

  1. Structure

  2. Function

  3. Immunocontraception

  4. Additional images

  5. References

  6. Further reading

  7. External links

{{Infobox anatomy
| Name = Zona pellucida
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| Image2 = Gray3.png
| Caption2 = Human ovum: The zona pellucida is seen as a thick clear girdle surrounded by the cells of the corona radiata.
| Precursor =
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| Artery =
| Vein =
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The zona pellucida (plural zonae pellucidae, also egg coat or pellucid zone) is a glycoprotein layer surrounding the plasma membrane of mammalian oocytes. It is a vital constitutive part of the oocyte. The zona pellucida first appears in unilaminar primary oocytes. It is secreted by both the oocyte and the ovarian follicles. The zona pellucida is surrounded by the cumulus oophorus. The cumulus is composed of cells that care for the egg when it is emitted from the ovary.[1]

This structure binds spermatozoa, and is required to initiate the acrosome reaction.

In the mouse (the best characterised mammalian system), the zona glycoprotein, ZP3, is responsible for sperm binding, adhering to proteins on the sperm plasma membrane. ZP3 is then involved in the induction of the acrosome reaction, whereby a spermatozoon releases the contents of the acrosomal vesicle. The exact characterisation of what occurs in other species has become more complicated as further zona proteins have been identified.[2][3]

In humans, five days after the fertilization, the blastocyst performs zona hatching; the zona pellucida degenerates and decomposes, to be replaced by the underlying layer of trophoblastic cells.

The zona pellucida is essential for oocyte growth and fertilization.

Structure

The zona pellucida is a translucent matrix of glycoproteins that surrounds the mammalian oocyte, and its formation is critical to successful fertilization.[4] In non-mammals it is called the vitelline membrane or vitelline envelope.[5]

Function

The thick membrane of the zona pellucida functions to only allow species-specific fertilizaton; to prevent polyspermy, and enable the acrosome reaction for the successful adhesion and penetration of the sperm cell. The major glycoproteins of the egg coat responsible, are known as sperm-binding proteins.[6]

The four major sperm-binding proteins, or sperm-receptors, are ZP1, ZP2, ZP3, and ZP4. They bind to capacitated spermatozoa and induce the acrosome reaction. Successful fertilization depends on the ability of sperm to penetrate the extracellular matrix of the zona pellucida that surrounds the egg.

In the mouse:

  • ZP3 allows species-specific sperm binding
  • ZP2 mediates subsequent sperm binding
  • ZP1 cross-links ZP2 and ZP3.

Data with native human protein are not currently available.

Immunocontraception

{{Main|Immunocontraception}}

ZP module-containing glycoproteins ZP1, ZP2, ZP3 and ZP4 are targets for immunocontraception in mammals.

In non-mammals, the zona pellucida is called the vitelline membrane or envelope, and the vitelline envelope in insects, and plays an important role in preventing cross-breeding of different species, especially in species such as fish that fertilize outside of the body.

The zona pellucida is commonly used to control wildlife population problems by immunocontraception. When the zona pellucida of one animal species is injected into the bloodstream of another, it results in sterility of the second species due to immune response. This effect can be temporary or permanent, depending on the method used. In New Jersey, immunocontraception using porcine zona pellucida has been trialled for the control of deer.[7]

Additional images

References

1. ^{{cite book|last=Gilbert|first=Scott|title=Developmental Biology|date=2013|publisher=Sinauer Associates Inc|isbn=9781605351926|pages=123}}
2. ^{{cite journal |pmid=12968942 |year=2003 |last1=Conner |first1=SJ |last2=Hughes |first2=DC |title=Analysis of fish ZP1/ZPB homologous genes--evidence for both genome duplication and species-specific amplification models of evolution |volume=126 |issue=3 |pages=347–52 |journal=Reproduction |doi=10.1530/rep.0.1260347}}
3. ^{{cite journal |pages=1148–52 |doi=10.1093/humrep/deh835 |title=Cracking the egg: Increased complexity in the zona pellucida |year=2005 |last1=Conner |first1=S.J. |journal=Human Reproduction |volume=20 |issue=5 |pmid=15760956 |last2=Lefièvre |first2=L |last3=Hughes |first3=DC |last4=Barratt |first4=CL}}
4. ^{{cite journal |last1=Gupta |display-authors=et al |first1=SK |title=Mammalian zona pellucida glycoproteins: structure and function during fertilization |journal=Cell and Tissue Research |date=September 2012 |volume=349 |issue=3 |pages=665–78 |doi=10.1007/s00441-011-1319-y |pmid=22298023}}
5. ^{{cite journal |last1=Monné |first1=M |last2=Jovine |first2=L |title=A structural view of egg coat architecture and function in fertilization. |journal=Biology of Reproduction |date=October 2011 |volume=85 |issue=4 |pages=661–9 |doi=10.1095/biolreprod.111.092098 |pmid=21715714}}
6. ^{{cite journal |last1=Gupta |first1=SK |last2=Bansal |first2=P |last3=Ganguly |first3=A |last4=Bhandari |first4=B |last5=Chakrabarti |first5=K |title=Human zona pellucida glycoproteins: functional relevance during fertilization. |journal=Journal of Reproductive Immunology |date=December 2009 |volume=83 |issue=1–2 |pages=50–5 |doi=10.1016/j.jri.2009.07.008 |pmid=19850354}}
7. ^{{cite web|title=Community-Based Deer Management|url=http://www.state.nj.us/dep/fgw/cbdmp.htm|publisher=New Jersey Department of Environmental Protection|accessdate=8 July 2015|date=24 September 2014}}

Further reading

  • {{cite journal |doi=10.1016/0014-5793(92)80853-9 |title=A large domain common to sperm receptors (Zp2 and Zp3) and TGF-β type III receptor |year=1992 |last1=Bork |first1=Peer |last2=Sander |first2=Chris |journal=FEBS Letters |volume=300 |issue=3 |pages=237–40 |pmid=1313375}}
  • {{cite journal |doi=10.1016/S1472-6483(10)62086-X |title=Biochemical and functional characterization of the human zona pellucida |year=2003 |last1=Oehninger |first1=Sergio |journal=Reproductive BioMedicine Online |volume=7 |issue=6 |pages=641–8 |pmid=14748962}}
  • {{cite journal |doi=10.1074/jbc.M304026200 |title=Structural Characterization of Native Mouse Zona Pellucida Proteins Using Mass Spectrometry |year=2003 |last1=Boja |first1=E. S. |journal=Journal of Biological Chemistry |volume=278 |issue=36 |pages=34189–202 |pmid=12799386 |last2=Hoodbhoy |first2=T |last3=Fales |first3=HM |last4=Dean |first4=J}}
  • Bagnell C (2005). "Animal Reproduction". Rutgers University Department of Animal Sciences.{{Verify source|what is this? is it a book? a journal article? i only see a university course by that name http://animalsciences.rutgers.edu/faculty/bagnell/carol-a-bagnell.html|date=August 2011}}
  • {{cite journal |doi=10.1146/annurev.biochem.74.082803.133039 |title=Zona Pellucida Domain Proteins |year=2005 |last1=Jovine |first1=Luca |last2=Darie |first2=Costel C. |last3=Litscher |first3=Eveline S. |last4=Wassarman |first4=Paul M. |journal=Annual Review of Biochemistry |volume=74 |pages=83–114 |pmid=15952882}}
  • {{cite journal |doi=10.1055/s-2006-948550 |title=Tracking Down the ZP Domain: From the Mammalian Zona Pellucida to the Molluscan Vitelline Envelope |year=2006 |last1=Monné |first1=Magnus |last2=Han |first2=Ling |last3=Jovine |first3=Luca |journal=Seminars in Reproductive Medicine |volume=24 |issue=4 |pages=204–16 |pmid=16944418}}
  • {{cite journal |doi=10.1074/jbc.R800027200 |pmc=2528931 |title=Zona Pellucida Glycoproteins |year=2008 |last1=Wassarman |first1=P. M. |journal=Journal of Biological Chemistry |volume=283 |issue=36 |pages=24285–9 |pmid=18539589}}
  • {{cite journal |doi=10.1387/ijdb.072524pw |title=Mammalian fertilization:the eggs multifunctional zona pellucida |year=2008 |last1=Wassarman |first1=Paul M. |last2=Litscher |first2=Eveline S. |journal=The International Journal of Developmental Biology |volume=52 |issue=5–6 |pages=665–76 |pmid=18649280}}
  • {{cite journal |doi=10.1038/nature07599 |title=Crystal structure of the ZP-N domain of ZP3 reveals the core fold of animal egg coats |year=2008 |last1=Monné |first1=Magnus |last2=Han |first2=Ling |last3=Schwend |first3=Thomas |last4=Burendahl |first4=Sofia |last5=Jovine |first5=Luca |journal=Nature |volume=456 |issue=7222 |pages=653–7 |pmid=19052627|bibcode=2008Natur.456..653M }}
  • {{cite journal |doi=10.1016/j.cell.2010.09.041 |title=Insights into Egg Coat Assembly and Egg-Sperm Interaction from the X-Ray Structure of Full-Length ZP3 |year=2010 |last1=Han |first1=Ling |last2=Monné |first2=Magnus |last3=Okumura |first3=Hiroki |last4=Schwend |first4=Thomas |last5=Cherry |first5=Amy L. |last6=Flot |first6=David |last7=Matsuda |first7=Tsukasa |last8=Jovine |first8=Luca |journal=Cell |volume=143 |issue=3 |pages=404–15 |pmid=20970175}}

External links

  • {{BUHistology|18404loa}} - "Female Reproductive System: ovary, cumulus oophorus "
  • {{BUHistology|14805loa}} - "Female Reproductive System: ovary, multilaminar primary follicle"
  • {{UCDavisOrganology|Reproductive/mammal/ovary2/ovary7}} - "Mammal, canine ovary (LM, High)"
  • Image at um.edu.mt
  • Image at um.edu.mt
{{Female reproductive system}}{{DEFAULTSORT:Zona Pellucida}}

3 : Germ cell structures|Reproductive system|Vertebrate developmental biology

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