Assembly of cartilage proteoglycan with hyaluronate and structure of the central filament in proteoglycan aggregate

1990 ◽  
Vol 18 (2) ◽  
pp. 204-207 ◽  
Author(s):  
MATTHIAS MÖRGELIN ◽  
MATS PAULSSON ◽  
JÜRGEN ENGEL
Keyword(s):  
Cartilage Proteoglycan ◽  
Central Filament

scholarly journals Cartilage proteoglycan aggregates. Electronmicroscopic studies of native and fragmented molecules

1978 ◽  
Vol 175 (3) ◽  
pp. 913-919 ◽  
Author(s):  
Dick Heinegård ◽  
Stefan Lohmander ◽  
Johan Thyberg
Keyword(s):  
Electron Microscopy ◽  
Hyaluronic Acid ◽  
Electron Micrographs ◽  
Chondroitin Sulphate ◽  
Average Length ◽  
Side Chain ◽  
Nasal Cartilage ◽  
Cartilage Proteoglycan ◽  
Central Filament ◽  
Proteoglycan Aggregates

1. Proteoglycan aggregates from bovine nasal cartilage were studied by using electron microscopy of proteoglycan/cytochrome c monolayers. 2. The aggregates contained a variably long central filament of hyaluronic acid with an average length of 1037nm. The proteoglycan monomers attached to the hyaluronic acid appeared as side chain filaments varying in length (averaging 249nm). They were distributed along the central filament at an average distance of about 36nm. 3. Chondroitin sulphate side chains were removed from the proteoglycan monomers of the aggregates by partial chondroitinase digestion. The molecules obtained had the same general appearance as intact aggregates. 4. Proteoglycan aggregates were treated with trypsin and the largest fragment, which contains the hyaluronic acid, link protein and hyaluronic acid-binding region, was recovered and studied with electron microscopy. Filaments that lacked the side chain extensions and had the same length as the central filament in the intact aggregate were observed. 5. Hyaluronic acid isolated after papain digestion of cartilage extracts gave filaments with similar length and size distribution as observed for the central filament both in the intact aggregate and in the trypsin digests. 6. Umbilical-cord hyaluronic acid was also studied and gave electron micrographs similar to those described for hyaluronic acid from cartilage. However, the length of the filament was somewhat shorter. 7. The electron micrographs of both intact and selectively degraded proteoglycans corroborate the current model of cartilage proteoglycan structure.

scholarly journals Complete primary structure of the rat cartilage proteoglycan core protein deduced from cDNA clones.

1987 ◽  
Vol 262 (36) ◽  
pp. 17757-17767 ◽  
Author(s):  
K Doege ◽  
M Sasaki ◽  
E Horigan ◽  
J R Hassell ◽  
Y Yamada
Keyword(s):  
Primary Structure ◽  
Core Protein ◽  
Cdna Clones ◽  
Cartilage Proteoglycan ◽  
Complete Primary Structure

scholarly journals Monoclonal antibodies as probes for determining the microheterogeneity of the link proteins of cartilage proteoglycan.

1985 ◽  
Vol 260 (20) ◽  
pp. 11348-11356 ◽  
Author(s):  
B Caterson ◽  
J R Baker ◽  
J E Christner ◽  
Y Lee ◽  
M Lentz
Keyword(s):  
Monoclonal Antibodies ◽  
Cartilage Proteoglycan

scholarly journals Treatment of Bovine Nasal Cartilage Proteoglycan with Chondroitinases from Flavobacterium heparinum and Proteus vulgaris

1972 ◽  
Vol 247 (14) ◽  
pp. 4521-4528 ◽  
Author(s):  
Vincent C. Hascall ◽  
Rick L. Riolo ◽  
James Hayward ◽  
Clifford C. Reynolds
Keyword(s):  
Proteus Vulgaris ◽  
Nasal Cartilage ◽  
Cartilage Proteoglycan ◽  
Flavobacterium Heparinum

Small-angle x-ray scattering of bovine nasal cartilage proteoglycan in solution

Biopolymers ◽  
1987 ◽  
Vol 26 (5) ◽  
pp. 633-650 ◽  
Author(s):  
S. S. Stivala ◽  
A. Patel ◽  
B. Khorramian ◽  
J. D. Gregory ◽  
S. Damle
Keyword(s):  
Small Angle ◽  
X Ray ◽  
Nasal Cartilage ◽  
X Ray Scattering ◽  
Cartilage Proteoglycan ◽  
Ray Scattering
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