The Small Proteoglycan Fibromodulin Is Expressed in Mitotic, but Not in Postmitotic Fibroblasts

1999 ◽  
Vol 1 (1) ◽  
pp. 59-65 ◽  
Author(s):  
Jean Bernhard Petri ◽  
Olaf Rott ◽  
Tino Wetzig ◽  
Konrad Herrmann ◽  
Uwe-Frithjof Haustein
Keyword(s):  
Small Proteoglycan

Stimulation of Small Proteoglycan Synthesis by the Hyaluronan Synthesis Inhibitor 4-Methylumbelliferone in Human Skin Fibroblasts

2009 ◽  
Vol 50 (3) ◽  
pp. 194-202 ◽  
Author(s):  
Masaru Funahashi ◽  
Toshiya Nakamura ◽  
Ikuko Kakizaki ◽  
Hideki Mizunuma ◽  
Masahiko Endo
Keyword(s):  
Human Skin ◽  
Skin Fibroblasts ◽  
Proteoglycan Synthesis ◽  
Human Skin Fibroblasts ◽  
Synthesis Inhibitor ◽  
Small Proteoglycan ◽  
Stimulation Of

scholarly journals Binding of heparin and of the small proteoglycan decorin to the same endocytosis receptor proteins leads to different metabolic consequences.

1991 ◽  
Vol 114 (1) ◽  
pp. 45-52 ◽  
Author(s):  
H Hausser ◽  
H Kresse
Keyword(s):  
Cultured Cells ◽  
Dermatan Sulfate ◽  
Core Protein ◽  
Affinity Binding ◽  
Dependent Manner ◽  
Concentration Dependent Manner ◽  
Receptor Proteins ◽  
High Affinity ◽  
Dermatan Sulfate Proteoglycan ◽  
Small Proteoglycan

Decorin, a small interstitial dermatan sulfate proteoglycan, is turned over in cultured cells of mesenchymal origin by receptor-mediated endocytosis followed by intralysosomal degradation. Two endosomal proteins of 51 and 26 kD have been implicated in the endocytotic process because of their interaction with decorin core protein. However, heparin and protein-free dermatan sulfate were able to inhibit endocytosis of decorin in a concentration-dependent manner. After Western blotting of endosomal proteins, there was competition for binding to the 51- and 26-kD proteins between heparin and decorin. In spite of its high-affinity binding, heparin was poorly cleared from the medium of cultured cells and then catabolized in lysosomes. In contrast to decorin, binding of heparin to the 51- and 26-kD proteins was insensitive to acidic pH, thus presumably preventing its dissociation from the receptor in the endosome. Recycling of heparin to the cell surface after internalization could indeed be demonstrated.

‘Small’-proteoglycan: collagen interactions: Keratan sulphate proteoglycan associates with rabbit corneal collagen fibrils at the ‘a’ and ‘c’ bands

1985 ◽  
Vol 5 (9) ◽  
pp. 765-774 ◽  
Author(s):  
J. E. Scott ◽  
M. Haigh
Keyword(s):  
Binding Sites ◽  
Type I Collagen ◽  
Specific Binding ◽  
Corneal Stroma ◽  
Collagen Fibrils ◽  
Type I ◽  
Keratan Sulphate ◽  
Protein Rich ◽  
Small Proteoglycan ◽  
Corneal Collagen

l. Proteoglycans (PGs) in rabbit corneal stroma and mouse sclera have been stained for electron microscopy with Cupromeronic blue in a critical electrolyte concentration (CEC) mode, with and without prior digestion of the tissue by keratanase or chondroitinase ABC to remove the keratan sulphate (KS) or chondroitin-dermatan sulphates (CS or DS) respectively.2. Two classes of PGs, located orthogonally to the corneal collagen fibrils at either the ‘step’ (band ‘a’ or ‘c’) or gap zone (band ‘d’ or ‘e’) are shown to be KS-PGs or DS-PGs respectively. Four separate and specific PG binding sites on Type I collagen fibrils have thus been identified.3. Rabbit corneal KS and DS PGs each contain two kinds of PG (Gregory JD, Coster L & Damle SP (1982) J. Biol. Chem.257, 6965–6970). We propose that each ‘small’ protein-rich PG is associated with a specific binding site on the collagen fibril.

Immunolocalization of the small proteoglycan decorin in human teeth

1996 ◽  
Vol 41 (4) ◽  
pp. 351-357 ◽  
Author(s):  
Nagako Yoshiba ◽  
Kunihiko Yoshiba ◽  
Masaaki Iwaku ◽  
Hidehiro Ozawa
Keyword(s):  
Human Teeth ◽  
Small Proteoglycan

Role of the small proteoglycan bikunin in human reproduction

HORMONES ◽  
2019 ◽  
Vol 19 (2) ◽  
pp. 123-133
Author(s):  
Antonio Junior Lepedda ◽  
Pierina De Muro ◽  
Giampiero Capobianco ◽  
Marilena Formato
Keyword(s):  
Human Reproduction ◽  
Small Proteoglycan

scholarly journals Interaction of the small proteoglycan decorin with fibronectin. Involvement of the sequence NKISK of the core protein

1991 ◽  
Vol 280 (2) ◽  
pp. 411-414 ◽  
Author(s):  
G Schmidt ◽  
H Hausser ◽  
H Kresse
Keyword(s):  
Core Protein ◽  
Solid Phase ◽  
Repetitive Sequences ◽  
Central Position ◽  
Independent Manner ◽  
High Affinity ◽  
Kd Values ◽  
Solid Phase Assay ◽  
20 Nm ◽  
Small Proteoglycan

Decorin, an interstitial small proteoglycan, was shown to interact with fibronectin via its core protein. In a solid-phase assay, both high-affinity (KD values between 10 and 20 nM) and low-affinity (KD values between 110 and 130 nM) binding sites were found. The central position of decorin core protein is made up of several repeats containing NKISK in positions 85-89 and similar sequences in other repeats. The pentapeptide inhibited, albeit not completely, the high-affinity interaction between decorin and fibronectin in a specific charge-independent manner. Half-maximal inhibition occurred at a peptide concentration of 10 microM. Core-protein-derived peptides that had been produced by endoproteinase Lys-C digestion were not inhibitory, but endoproteinase Arg-C-generated peptides served as inhibitors of binding. These results suggest that NKISK as a component of repetitive sequences of decorin is involved in the interaction between the proteoglycan and fibronectin.

scholarly journals The Cartilage-specific Fibronectin Isoform Has a High Affinity Binding Site for the Small Proteoglycan Decorin

2002 ◽  
Vol 278 (13) ◽  
pp. 11175-11181 ◽  
Author(s):  
Rina Gendelman ◽  
Nancy I. Burton-Wurster ◽  
James N. MacLeod ◽  
George Lust
Keyword(s):  
Binding Site ◽  
Affinity Binding ◽  
High Affinity Binding ◽  
High Affinity ◽  
High Affinity Binding Site ◽  
Small Proteoglycan

scholarly journals Presence of small proteoglycan fragments in normal and arthritic human cartilage

1992 ◽  
Vol 35 (9) ◽  
pp. 1042-1052 ◽  
Author(s):  
Petra Witsch-Prehm ◽  
Rolf Miehlke ◽  
Hans Kresse
Keyword(s):  
Human Cartilage ◽  
Small Proteoglycan
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