Intracellular proteoglycans

Abstract

Proteoglycans (PGs) are proteins with glycosaminoglycan chains, are ubiquitously expressed and have a wide range of functions. PGs in the extracellular matrix and on the cell surface have been the subject of extensive structural and functional studies. Less attention has so far been given to PGs located in intracellular compartments, although several reports suggest that these have biological functions in storage granules, the nucleus and other intracellular organelles. The purpose of this review is, therefore, to present some of these studies and to discuss possible functions linked to PGs located in different intracellular compartments. Reference will be made to publications relevant for the topics we present. It is beyond the scope of this review to cover all publications on PGs in intracellular locations.

Serglycin inhibits the classical and lectin pathways of complement via its glycosaminoglycan chains: Implications for multiple myeloma

“…SG is mainly expressed by cells of hematopoietic origin and is a key intracellular proteoglycan [2,3]. SG can carry eight GAG chains, which depending on cell-type, can be either chondroitin sulfate (CS), dermatan sulfate (DS), heparan sulfate (HS), and heparin [3,4]. SG is constitutively secreted from monocytes [5] and macrophages [6] into the extracellular matrix and the secretion increases upon activation of these cells.…”

“…Serglycin Introduction Serglycin (SG) is a proteoglycan with a 17 kDa protein moiety containing a characteristic domain rich in serine/glycine repeats, which serves as the attachment site for glycosaminoglycan (GAG) chains [1]. SG is mainly expressed by cells of hematopoietic origin and is a key intracellular proteoglycan [2,3]. SG can carry eight GAG chains, which depending on cell-type, can be either chondroitin sulfate (CS), dermatan sulfate (DS), heparan sulfate (HS), and heparin [3,4].…”

Immunohistochemical expression of heparan sulfate correlates with stromal cell proliferation in breast phyllodes tumors

“…[1][2][3] Its primary structure is characterized by repeats of disaccharide units of a uronic acid and a derivative of glucosamine. The biosynthetic process of heparan sulfate is highly complicated whereby it can undergo modifications such as sulfation, epimerization, and acetylation to generate a great structural diversity of heparan sulfate chains.…”

Critical Role of Dendritic Cells in T Cell Retention in the Interfollicular Region of Peyer’s Patches

“…molecules. Subset-specific expression of heparan sulfate was reported in mast cells (30). Indeed, highly differentiated connective tissue-type mast cells, but not mucosal mast cells, express high levels of heparin (30).…”

“…Subset-specific expression of heparan sulfate was reported in mast cells (30). Indeed, highly differentiated connective tissue-type mast cells, but not mucosal mast cells, express high levels of heparin (30). Heparin biosynthesis is mediated by multiple complex steps involving many enzymes such as N-deacetylase/Nsulfotransferase and exostoses-1 (31,32).…”