scholarly journals The periphery of the developing collagen fibril Quantitative relationships with dermatan sulphate and other surface-associated species

1984 ◽  
Vol 220 (3) ◽  
pp. 869-869
Keyword(s):  
Collagen Fibril ◽  
Dermatan Sulphate ◽  
Associated Species

scholarly journals The periphery of the developing collagen fibril. Quantitative relationships with dermatan sulphate and other surface-associated species

1984 ◽  
Vol 218 (1) ◽  
pp. 229-233 ◽  
Author(s):  
J E Scott
Keyword(s):  
Embryonic Development ◽  
Data Base ◽  
Collagen Fibril ◽  
Developmental Period ◽  
Dermatan Sulphate ◽  
Tissue Concentrations ◽  
Sulphate Content ◽  
Electron Histochemistry ◽  
Associated Species ◽  
The Relationship

Dermatan sulphate, hydroxyproline and collagen fibril diameters were measured in flexor tendons from chick and calf limbs, from early in embryonic development to maturity. The collagen fibril is viewed as a long thin cylinder. A species X present at the periphery of the cylinder, regularly and specifically arrayed along the fibril, should then satisfy the relationship [X]/[collagen]r = k where [X] and [collagen] are tissue concentrations of X and collagen, and r is the fibril radius. Throughout the developmental period studied, dermatan sulphate (i.e.X) in chick, calf and rat tendons fits the relationship, implying that it is specifically, regularly and entirely associated with collagen fibrils, thus confirming and extended previous electron histochemistry [Scott & Orford (1981) Biochem. J. 197, 213-216]. This approach explains the pattern of change of dermatan sulphate content during development of the tendon. The findings imply that the dermatan sulphate proteoglycan-collagen interaction is evolutionarily highly conserved. The relationship [X]/[collagen]r = k is used to show that surface concentrations of covalently bound species, such as extension propeptides, can be easily assessed, given the data base described in paragraph 1 above.

Isolation and characterization of a collagen fibril-associated dermatan sulphate proteoglycan from bovine lung

1987 ◽  
Vol 926 (3) ◽  
pp. 296-309 ◽  
Author(s):  
Toin H.M.S.M. van Kuppevelt ◽  
Henriet M.J. Janssen ◽  
Henk M. van Beuningen ◽  
Kin-Sun Cheung ◽  
Martin M.A. Schijen ◽  
...  
Keyword(s):  
Collagen Fibril ◽  
Dermatan Sulphate ◽  
Sulphate Proteoglycan ◽  
Isolation And Characterization

scholarly journals Proteoglycan-collagen arrangements in developing rat tail tendon. An electron microscopical and biochemical investigation

1981 ◽  
Vol 195 (3) ◽  
pp. 573-581 ◽  
Author(s):  
J E Scott ◽  
C R Orford ◽  
E W Hughes
Keyword(s):  
Rapid Growth ◽  
Collagen Fibril ◽  
Chondroitin Sulphate ◽  
Post Partum ◽  
Dermatan Sulphate ◽  
Concentration Method ◽  
Sigmoid Curve ◽  
Tail Tendon ◽  
Electron Microscopical ◽  
Fibril Diameter

1. Developing tail tendons from rats (19-day foetal to 126 days post partum) were examined by electron microscopy after staining for proteoglycan with a cationic copper phthalocyanin dye. Cuprolinic Blue, in a “critical electrolyte concentration” method. Hydroxyproline was measured on papain digests of tendons, from which glycosaminoglycuronans were isolated, characterized and quantified. 2. Mean collagen fibril diameters increased more than 10-fold with age according to a sigmoid curve, the rapid growth phase 2 being during 30-90 days after conception. Fibril periodicities were considerably smaller (50-55 nm) in phases 1 and 2 than in phase 3 (greater than 62 nm). 3. Dermatan sulphate is the main glycosaminoglycuronan in mature tendon. Chondroitin sulphate and hyaluronate preponderate in foetal tissue. 4. Proteoglycan was seen around but not inside collagen fibrils. Proteoglycan and collagen were quantified from electron micrographs. Their ratios behaved similarly to uronic acid/hydroxyproline and hyaluronate/hydroxyproline ratios, which decreased rapidly around birth, and then levelled off to a low plateau coincident with the onset of rapid growth in collagen fibril diameter. 5. Dermatan sulphate/hydroxyproline ratios suggest that the proteoglycan orthogonal array around the fibril is largely dermatan sulphate. In the foetus hyaluronate and chondroitin sulphate exceed that expected to be bound to collagen. 6. An inhibiting action of chondroitin sulphate-rich proteoglycan on fibril diameter growth is suggested. 7. The distributions of hyaluronate, chondroitin sulphate and dermatan sulphate are discussed in the light of secondary structures suggested to be present in hyaluronate and chondroitin sulphate, but not in dermatan sulphate.

scholarly journals Identification of specific binding sites for keratan sulphate proteoglycans and chondroitin-dermatan sulphate proteoglycans on collagen fibrils in cornea by the use of cupromeronic blue in ‘critical-electrolyte-concentration’ techniques

1988 ◽  
Vol 253 (2) ◽  
pp. 607-610 ◽  
Author(s):  
J E Scott ◽  
M Haigh
Keyword(s):  
Collagen Fibril ◽  
Electrolyte Concentration ◽  
Specific Binding ◽  
Corneal Stroma ◽  
Anion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Dermatan Sulphate ◽  
Keratan Sulphate ◽  
Specific Binding Sites ◽  
The One

Proteoglycans (PGs) in bovine corneal stroma were stained with Cupromeronic Blue in ‘critical-electrolyte-concentration’ (CEC) methods for electron microscopy, and were located vis-à-vis collagen fibril a-e banding patterns. Keratanase and chondroitin ABC lyase digestion showed that a + c-band- and d + e-band-associated PGs were keratan sulphate-rich and chondroitin (dermatan) sulphate-rich respectively. The CEC pattern proved that the keratan sulphate PGs at the a and c bands differed. Comparison of their CECs with their behaviour on anion-exchange chromatography confirmed previous (indirect) attempts at identification [Scott & Haigh (1985) Biosci. Rep. 5, 765-774]. Similar arguments were applied to the dermatan sulphate PGs at the d and e bands. These results strongly support the one-PG-one-binding-site hypothesis [e.g. Scott (1988) Biochem. J. 252, 313-323]. Remarkable inter-species variations in the keratan sulphate PG patterns contrast with the relatively constant picture of dermatan sulphate PG-collagen fibril interactions.

Elongated dermatan sulphate in post-inflammatory healing skin distributes among collagen fibrils separated by enlarged interfibrillar gaps

2001 ◽  
Vol 358 (1) ◽  
pp. 157-163 ◽  
Author(s):  
Kumiko KUWABA ◽  
Miya KOBAYASHI ◽  
Yoshihiro NOMURA ◽  
Shinkichi IRIE ◽  
Yoh-ichi KOYAMA
Keyword(s):  
Electron Microscopy ◽  
Collagen Fibril ◽  
Core Protein ◽  
Mouse Skin ◽  
Molecular Size ◽  
Collagen Fibrils ◽  
Dermatan Sulphate ◽  
Disaccharide Composition ◽  
Control Skin

It has been reported that the disaccharide composition of dermatan sulphate shows transient changes after epicutaneous application of the hapten 2,4-dinitrofluorobenzene to mouse skin, and that these changes are most conspicuous in healing skin on day 15 after chemical insult [Kuwaba, Nomura, Irie and Koyama (1999) J. Dermatol. Sci. 19, 23–30]. In the present study it was found that the molecular size of dermatan sulphate was increased on day 15 after hapten application. The molecular size of decorin increased in healing skin, whereas the size of dermatan-sulphate-depleted core protein did not increase. The length and localization of decorin dermatan sulphate were investigated by electron microscopy. Dermatan sulphate filaments oriented orthogonally to collagen fibrils were longer in healing skin than in control skin. In control skin, dermatan sulphate filaments were found among tightly packed collagen fibrils. In contrast, the interfibrillar gaps between each collagen fibril were enlarged in healing skin; elongated dermatan sulphate filaments extended from the surface of collagen fibrils across the enlarged gap. These results suggest that the increase in molecular size of decorin dermatan sulphate is important in organizing collagen fibrils separated by enlarged interfibrillar gaps in healing skin.

Ultrastructural analysis of collagen formation in the developing primate amnion

1990 ◽  
Vol 48 (3) ◽  
pp. 106-107
Author(s):  
Barry F. King ◽  
Grete N. Fry
Keyword(s):  
Golgi Apparatus ◽  
Collagen Fibril ◽  
Fibril Formation ◽  
Amniotic Cavity ◽  
Cytological Evidence ◽  
Mammalian Embryo ◽  
Intracellular Location ◽  
Collagen Formation ◽  
Amniotic Epithelium ◽  
Extraembryonic Mesoderm

The amnion surrounding the mammalian embryo consists of the amniotic epithelium facing the amniotic cavity, a layer of extraembryonic mesoderm bordering the exocoelom and an intervening layer of extracellular matrix (Fig. 1). During gestation the amnion expands remarkably to acommodate the rapidly growing embryo. In this study we have examined the process of collagen fibril formation in the developing amnion of the rhesus monkey between 20 and 60 days of gestation.Most cytological evidence of collagen fibril formation was observed in association with the extraembryonic mesodermal cells rather than the amniotic epithelium. The mesodermal cells h ad abundant cisternae of rough endoplasmic reticulum and a prominent Golgi apparatus. Elongated secretory vacuoles were associated with the Golgi apparatus and often contained parallel aggregates of fine filaments (Fig. 2). In some secretory vacuoles, periodic densities also were observed. Some striated collagen fibrils were observed in an apparent intracellular location in long, membrane-limited compartments (Fig. 3). Still other striated fibrils were observed in dense bodies, presumably lysosomes (Fig. 4).

The Interaction of β2 Glycoprotein-I and Heparin and Its Effect on β2 Glycoprotein-I Antiphospholipid Antibody Cofactor Function in Plasma

1994 ◽  
Vol 72 (04) ◽  
pp. 578-581 ◽  
Author(s):  
T McNally ◽  
S E Cotterell ◽  
I J Mackie ◽  
D A Isenberg ◽  
S J Machin
Keyword(s):  
Solid Phase ◽  
Pharmaceutical Preparations ◽  
Enzyme Linked Immunosorbent Assay ◽  
Antiphospholipid Antibody ◽  
Biological Functions ◽  
Dermatan Sulphate ◽  
Glycoprotein I ◽  
Crossed Immunoelectrophoresis ◽  
Calcium Heparin ◽  
Cofactor Activity

Summaryβ2 glycoprotein-I (β2GPI), a cofactor for antiphospholipid antibody (aPA) binding, binds to many anionic macromolecules including heparin. The nature of this interaction with heparin is not well understood and its effect on the purported biological functions of β2GPI is unknown.We have examined the interactions of dermatan sulphate (DS) and different pharmaceutical preparations of heparin with β2GPI by crossed immunoelectrophoresis (CIE) and investigated the effect of these agents on plasma levels of p2GPI antigen (β2GPI: Ag) by a standardised enzyme linked immunosorbent assay (ELISA). P2GPI aPA cofactor activity (β2GPI:Cof) was also measured using a modified solid phase an-ti-phosphatidylserine (aPS) ELISA. CIE results confirmed a heparin-β2GPI interaction with unfractionated (UF) heparin. β2GPI:Ag levels were unaffected by any of the preparations investigated. There were no significant differences in β2GPI:Cof activities of the samples containing LMW heparins or DS but levels of β2GPI:Cof were increased in samples containing UF sodium and calcium heparin preparations (0.5 IU/ml Monoparin, p <0.05, and 10 IU/ml Liquemin and Calcipa-rine, p <0.05).

scholarly journals Tyrosine-rich acidic matrix protein (TRAMP) accelerates collagen fibril formation in vitro.

1993 ◽  
Vol 268 (26) ◽  
pp. 19826-19832
Author(s):  
J.R. MacBeath ◽  
D.R. Shackleton ◽  
D.J. Hulmes
Keyword(s):  
Collagen Fibril ◽  
Matrix Protein ◽  
Fibril Formation
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