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Literature DB >> 57957

Electron microscopic autoradiography of 35SO4-labelled material closely associated with collagen fibrils in mammalian synovium and ear cartilage.

Abstract

Electron microscopic autoradiography of connective tissue obtained from mice and rabbits previously injected with 35SO4 indicated that sulphated proteoglycans are localized on collagen fibrils. Ruthenium Red-positive transverse belts surrounding fibrils near the a-bands were heavily labelled, but fine lateral filaments of Ruthenium Red-positive material were not. These filaments, which interconnect collagen fibrils in a variety of connective tissues may represent linear aggregations of hyaluronic acid, glycoproteins and non-sulphated or long-lived sulphated proteoglycans.

Entities: Chemical Disease Species

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Year: 1976 PMID： 57957 DOI： 10.1007/bf01007168

Source DB: PubMed Journal: Histochem J ISSN： 0018-2214

18 in total

1. Alcian Blue staining of cartilage for electron microscopy. Application of the critical electrolyte concentation principle.

Authors: B H Schofield; B R Williams; S B Doty
Journal: Histochem J Date: 1975-03

4. Collagen metabolism in the liver. An annotated and supplemented report of a workshop at the National Institutes of Health on February 28 and March 1, 1977.

Authors:
Journal: Am J Dig Dis Date: 1978-07

5. An ultrastructural study of glycosaminoglycans associated with collagen and other constituents of the cat anulus fibrosus.

Authors: W F Butler; P Heap
Journal: Histochem J Date: 1982-01

6. An electron microscopical study of the influence of different glycosaminoglycans on the fibrillogenesis of collagen type I and II in vitro.

Authors: S Lilja; H J Barrach
Journal: Virchows Arch A Pathol Anat Histol Date: 1981

7. Ultrastructure of transport pathways in stressed synovium of the knee in anaesthetized rabbits.

Authors: J R Levick; J N McDonald
Journal: J Physiol Date: 1989-12 Impact factor: 5.182

8. Cartilage ultrastructure after high pressure freezing, freeze substitution, and low temperature embedding. II. Intercellular matrix ultrastructure - preservation of proteoglycans in their native state.

Authors: E B Hunziker; R K Schenk
Journal: J Cell Biol Date: 1984-01 Impact factor: 10.539

8 in total

Electron microscopic autoradiography of 35SO4-labelled material closely associated with collagen fibrils in mammalian synovium and ear cartilage.

1. Alcian Blue staining of cartilage for electron microscopy. Application of the critical electrolyte concentation principle.

2. The relationship of hyaluronate and collagen in the bovine vitreous body.

3. Dermatan sulfate-protein: isolation from and interaction with collagen.

4. Digestion with chondroitinases of acid mucosaccharides in rabbit cartilages as revealed by electron microscopy.

5. Electron microscopic demonstration of proteoglycans in guinea pig epiphyseal cartilage.

6. Ruthenium red-positive filaments interconnecting collagen fibrils.

7. Interaction of cartilage proteoglycans with collagen-substituted agarose gels.

8. High-resolution autoradiography. I. Methods.

9. Hyaluronic acid in cartilage and proteoglycan aggregation.

10. The interaction of collagen and acid mucopolysaccharides. A model for connective tissue.

Review 1. Proteoglycan-fibrillar collagen interactions.

2. Microfibrillar meshwork of the synovial lining and associated broad banded collagen: a clue to identity.

3. Electron microscopic observations on pulmonary connective tissue stained by Ruthenium Red.

4. Collagen metabolism in the liver. An annotated and supplemented report of a workshop at the National Institutes of Health on February 28 and March 1, 1977.

5. An ultrastructural study of glycosaminoglycans associated with collagen and other constituents of the cat anulus fibrosus.

6. An electron microscopical study of the influence of different glycosaminoglycans on the fibrillogenesis of collagen type I and II in vitro.

7. Ultrastructure of transport pathways in stressed synovium of the knee in anaesthetized rabbits.

8. Cartilage ultrastructure after high pressure freezing, freeze substitution, and low temperature embedding. II. Intercellular matrix ultrastructure - preservation of proteoglycans in their native state.