GLİKOPROTEİNLERİN YAPISAL ÖZELLİKLERİ VE FETAL FİBRONEKTİNLER
GLİKOPROTEİNLERİN YAPISAL ÖZELLİKLERİ VE FETAL FİBRONEKTİNLER S. Eliş Yıldız, M. Nazlı Volume : 1 Issue : 1 Pages : 44-50 Year : 2015
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.