Dergiler / Caucasian Journal of Science / 2015 / Cilt: 2 Sayı: 1

GLİKOPROTEİNLERİN YAPISAL ÖZELLİKLERİ VE FETAL FİBRONEKTİNLER

Sevda Eliş Yıldız(Kafkas Üniversitesi, Sağlık Yüksekokulu, Kars)
Mümtaz Nazlı(MEHMET AKİF ERSOY ÜNİVERSİTESİ, VETERİNER FAKÜLTESİ)
Sayfa
44–50
Yayın Tarihi
2015-12-31
DOI
—
🏛️Bu makalenin bibliyografik verileri ve tam metin bağlantısı DergiPark üzerinden sağlanmıştır.
DergiPark Kaydı ↗
✨

Yapay Zeka Hızlı Bakış & Çıkarımlar

AI Insight
⚡ TL;DR(1 Cümlede Hızlı Çıkarım)

In this review, we have given information about structure, function and the fetal fibronectins of the glycoproteins.

📌 3 Maddede Bu Makale

🎯
Amaç & Hipotez:Glycoproteins exist in various organism and they have many different functions.
📊
Temel Bulgular & Veri:These proteinsler in which have short oligosaccharides and serve in so many cellular events as cell surface recognition by hormones, viruses and other substances.
💡
Sonuç & Katkı:In this review, we have given information about structure, function and the fetal fibronectins of the glycoproteins.
🔬Tür:Literatür & Derleme Çalışması
📍Kapsam:Genişletilmiş Akademik Örneklem
⚙️Değişkenler:Fetal Fibronectin · Glycoproteins · Laminin

Abstract

Glycoproteins exist in various organism and they have many different functions. These proteinsler in which have short oligosaccharides and serve in so many cellular events as cell surface recognition by hormones, viruses and other substances. There are two distinct types of sugar containing proteins that occur cells: glycoproteins and proteoglycans. Most of the proteins that are integral components of the plasma membrane and that function as receptors for hormones or other molecules in the circulation, or that mediate interactions between cells, are glycoproteins. In addition, many of the proteins of the endoplasmic reticulum and Golgi apparatus, and those that are secreted by cells, including serum and mucous proteins, are glycoproteins. İndeed, glycosylation is the major postsynthetic modification of proteins; it occurs either during the course of protein synthesis in the endoplasmic reticulum or once the protein has been synthesized and transported to the golgi apparatus. Fibronectin is a multifunctional extracellular matrix and plasma protein that plays a central role in cell adhesion. Intensive research on fibronectin has made it a prototype cell adhesion protein.  Fetal Fibronectin is a glycoprotein produced by the chorionic membranes and is localized to the deciduas basalis adjacent to the intervillous space. Its primary purpose appears to be that of an adhesion molecule  which helps bind the chorionic membranes to the underlying maternal decidua. In this review, we have given information about structure, function and the fetal fibronectins of the glycoproteins.

🔖

Bu Makaleye Atıf Yap

Yıldız, S. E., Nazlı, M. (2015). GLİKOPROTEİNLERİN YAPISAL ÖZELLİKLERİ VE FETAL FİBRONEKTİNLER. Caucasian Journal of Science, Cilt: 2 Sayı: 1, 44–50. https://ajindex.com/articles/1468956

📄 Tam Metin PDF Okuyucu

📄

PDF görüntüleyici hazırlanıyor...

Kaynakça (28)

  1. Ergüler, G., Demir N., Demir, R., Türkiye Klinikleri Tıp Bilimleri Dergisi, 2002, 22, 3, 313-327.
  2. Sağlam, M., Aştı, RN., Özer A., Genel Histoloji. 6. Baskı. Yorum Matbaacılık. 2001, Ankara.
  3. Yavuz, Ö., Türkiye Klinikleri Tıp Bilimleri Dergisi, 2001, 21, 517-522.
  4. Başaran, A., Tıbbı Biyoloji Ders Kitabı. 7. Baskı. 2005, Güneş ve Nobel Tıp Kitapevleri.
  5. Rao, VSR., Qasaba, PK., Balaji, PV., Confirmation of Carbonhyrates. 1st Edition, Australia: Harwood Academic Publishers, 1998.
  6. Ünübol, Aybak., Uysal, H., F.Ü Sağ. Bil. Vet. Derg., 2010, 24, 2, 107-114.
  7. Nelson, DL., Michael, MC., Carbohydrates and Glycobiology. In Ryan M. Ed. Lehninger principles of biochemistry. United States of America: Wort Publishers. 2000, 293–324.
  8. Uysal, H., Temel ve Uygulamalı Alanlarda Uluslararası Katılımlı Prof. Dr. Semahat GELDİAY Anısına. İzmir Kongre Kitabı, 2003.
  9. Johansson, S., Svineng, G., Wennerberg, K., Front Biosci., 1997, (2) 126-46.
  10. Huppertz, B., Kertschanska, S., Demir, AY., Cell Tissue Res., 1998, 291, 133-48.
  11. Demir AY., Türkiye Klinikleri Tıp Bilimleri Dergisi, 2002, 22, 5, 449-460.
  12. Zardi, L., Carnemolla, B., Siri, A., EMBO J., 1987, 6, 2337-42.
  13. Siironen, J., Sandberg, M., Vuorinen, V., J. Neurochem., 1992, 59, 2184-2192.
  14. Wallquist, W., Patarroyo, M., Thams, S., The Journal of Comparative Neurology, 2002, 454, 284-293.
  15. Nacar, AA., Ömeroğlu, S., Düzce Tıp Fakültesi Dergisi, 2004, 1, 42-47.
  16. Erickson, AC., Couchman, JR., J Histochem Cytochem., 2000, 48, 1291-306.
  17. Öner, H., Öner, J., Türkiye Klinikleri Tıp Bilimler Dergisi, 2005, 25, 5, 688-692.
  18. Mayer, U., Nischt, R., Poschl, E., EMBO J. 1993, 12, 1879-85.
  19. Colognato, H., Yurchenco, PD., Dev. Dyn. 2000, 218-213-34.
  20. Smyth, N., Vatansever, HS., Murray, P.,. J. Cell Biol., 1999, 144, 151-60.
  21. Benirschke, K., Kaufmann, P.,. Pathology of the Human Placenta, 3 rd ed. New York: Springer, 1995.
  22. Nanaev, AK., Kohnen, G., Milovanov, AP.,. Placenta, 1997, 18, 53-64.
  23. Frank, HG., Malekzadeh, F., Kertschanska, S., Acta Anat., 1994, 150, 55-68.
  24. Zhao, Y., Luck, M.R., J Reprod Fertil., 1995, 104, 1, 115–23.
  25. Kruk, P.A., Auersperg, N., In Vitro Cell Dev Biol Anim., 1994, 30, 4, 217–225.
  26. Akkoyunlu, G., Üstünel, İ., Demir, R., Türk J. Biol., 2000, 24, 467-481.
  27. Woodruff, TK., Battaglia, J., Bowdidge, Biol Reprod., 1993, 48, 1, 68–76.
  28. Aten, RF., Kolodecik, TR., Behrman, HR.,. Endocrinology, 1995, 136, 4, 1753–1758.