title: The role of proteoglycans in maintaining collagen fibril morphology.
abstract: The aortic wall contains various heterogenous proteoglycan populations which interact in different ways with other components of extracellular matrix. Proteoglycans (PGs) are known to provide structural support to the vessel wall as well as to influence specific physiological functions of the tissues. The aim of the present study was to investigate the effects of Chondroitinase AC (Chase), Streptococcal Hyaluronidase (Hyase) and Heparanase on human aortic wall collagen which had been treated previously with 4M GuHCl, in order to verify the effects of selective glycanolytic treatment on type I collagen fibril ultrastructure. Following 4M GuHCl treatment, collagen fibrils are seen to have a clearly visible period. Subsequent to GuHCl and Streptococcal Hyase treatment all collagen fibrils appear to be completely swollen in thin aperiodic filaments; the typical 64 nm collagen period is completely undetectable. After GuHCl and Chase treatment a small number of collagen fibrils are seen to be swollen in thin fibrils which are mainly localized at some distance from elastic fibres. Following GuHCl and Heparanase/Heparitinase III treatment a considerable number of collagen fibrils appear to be swollen in thin fibrils; the majority of which are situated in the vicinity of elastic fibrils. The swelling of collagen fibrils underlines the fundamental role of proteoglycans in maintaining collagen fibril integrity and periodicity. It is as yet impossible to precisely map interactions between these proteoglycans and collagen fibres. The role of Hyaluronic acid requires further investigation, although the nature of this interaction is undoubtedly a matter of considerable interest.
authors.affiliation: Laboratory of Human Morphology, Varese, Italy.
authors.forename: C
authors.initials: C
authors.lastname: Dell'Orbo
authors.forename: G
authors.initials: G
authors.lastname: De Luca
authors.forename: L
authors.initials: L
authors.lastname: Gioglio
authors.forename: D
authors.initials: D
authors.lastname: Quacci
authors.forename: C
authors.initials: C
authors.lastname: Soldi
mesh_terms: D000328:Adult; D000368:Aged; D000369:Aged, 80 and over; D001013:Aorta, Thoracic / Q000378:metabolism / Q000502:physiology / Q000648:ultrastructure*; D002808:Chondroitin Lyases; D003094:Collagen / Q000502:physiology / Q000648:ultrastructure*; D004396:Coloring Agents; D004730:Endothelium, Vascular / Q000648:ultrastructure; D005260:Female; D005966:Glucuronidase; D006026:Glycoside Hydrolases; D006801:Humans; D006821:Hyaluronoglucosaminidase; D006868:Hydrolysis; D008297:Male; D008854:Microscopy, Electron; D008875:Middle Aged; D018485:Muscle Fibers, Skeletal / Q000648:ultrastructure; D011134:Polysaccharides / Q000737:chemistry; D011509:Proteoglycans / Q000502:physiology*; D000099175:Heparanase
chemical_list: D002808:Chondroitin Lyases; D003094:Collagen; D004396:Coloring Agents; D005966:Glucuronidase; D006026:Glycoside Hydrolases; D006821:Hyaluronoglucosaminidase; D011134:Polysaccharides; D011509:Proteoglycans; D000099175:Heparanase