GLİKOPROTEİNLERİN YAPISAL ÖZELLİKLERİ VE FETAL FİBRONEKTİNLER

Year 2015, Volume: 2 Issue: 1, 44 - 50, 31.12.2015

Sevda Eliş Yıldız , Mümtaz Nazlı

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.

Keywords

Fetal Fibronectin, Glycoproteins, Laminin

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