Characterization and synthesis of macromolecules by adult collateral ligament

Hey, Nina J.; Handley, Christopher J.; Ng, Chee Keng; Oakes, Barry W

doi:10.1016/0304-4165(90)90155-p

Cited by 19 publications

(25 citation statements)

References 21 publications

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“…Here, J ¼ detðFÞ is the volume ratio and F is the deformation gradient (Spencer, 1980) (J ¼ 1 À for the permeation experiment), f 0 is the initial volume fraction of the solid phase, taken to be 0.3 for ligament (Atkinson et al, 1997;Butler et al, 1997;Chimich et al, 1992;Hey et al, 1990), f f ¼ 1 À f 0 =J is the current volume fraction of the fluid phase and f s ¼ f 0 =J is the current volume fraction of the solid phase. k 0 represents the intrinsic permeability in the absence of strain.…”

Section: Intrinsic Permeabilitymentioning

confidence: 99%

“…The ground substance matrix is composed of proteoglycans, glycolipids and fibroblasts and holds large amounts of water, with the total water per wet weight measured as 60-70% (Chimich et al, 1992;Hey et al, 1990). The water content of ligaments has a strong influence on viscoelastic material properties (Chimich et al, 1992;Thornton et al, 2000).…”

Section: Introductionmentioning

confidence: 99%

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Permeability of human medial collateral ligament in compression transverse to the collagen fiber direction

Weiss

Maakestad

2006

Journal of Biomechanics

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This study quantified the apparent and intrinsic hydraulic permeability of human medial collateral ligament (MCL) under direct permeation transverse to the collagen fiber direction. A custom permeation device was built to apply flow across cylindrical samples of ligament while monitoring the resulting pressure gradient. MCLs from 5 unpaired human knees were used (donor age 55 AE 16 yr; 4 males, 1 female). Permeability measurements were performed at 3 levels of compressive pre-strain (10%, 20% and 30%) and 5 pressures (0.17, 0.34, 1.03, 1.72 and 2.76 MPa). Apparent permeability was determined from Darcy's law, while intrinsic permeability was determined from the zero-pressure crossing of the pressure-permeability curves at each compressive pre-strain. Resulting data were fit to a finite deformation constitutive law [Journal of Biomechanics 23 (1990) 1145-1156. The apparent permeability of human MCL ranged from 0:40 AE 0:05 to 8:60 AE 0:77 Â 10 À16 m 4 =N s depending on pre-strain and pressure gradient. There was a significant decrease in apparent permeability with increasing compressive pre-strain ðp ¼ 0:024Þ and pressure gradient ðpo0:001Þ; and there was a significant interaction between the effects of compressive pre-strain and pressure ðpo0:001Þ: Intrinsic permeability was 14:14 AE 0:74; 6:30 AE 2:13 and 4:29 AE 1:71 Â 10 À16 m 4 =N s for compressive pre-strains of 10%, 20% and 30%, respectively. The intrinsic permeability showed a faster decrease with increasing compressive pre-strain than that of bovine articular cartilage. These data provide a baseline for investigating the effects of disease and chemical modification on the permeability of ligament and the data should also be useful for modeling the poroelastic material behavior of ligaments. r

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Section: Intrinsic Permeabilitymentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Permeability of human medial collateral ligament in compression transverse to the collagen fiber direction

Weiss

Maakestad

2006

Journal of Biomechanics

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“…The tendon was then chopped into small pieces and incubated in sulfate‐free medium (1 g tissue per 10 mL medium) containing 200 µCi·mL −1 [ 35 S]sulfate at 37 °C for 6 h. The sulfate‐free medium contained 0.13 m sodium chloride, 4.74 m m potassium chloride, 2.54 m m calcium chloride, 1.9 m m magnesium chloride, 10 m m glucose, 1.0 m m l ‐glutamine, 1.19 m m potassium dihydrogen phosphate, 0.02 g·mL −1 Phenol Red and was buffered with 25 m m HEPES adjusted to pH 7.4 with sodium hydroxide [7]. Sulfate‐free medium was used in order to increase the incorporation of [ 35 S]sulfate into proteoglycans as it has previously been reported that the rate of incorporation of [ 35 S]sulfate into proteoglycans by tendon is considerably less than other connective tissues such as articular cartilage, and this necessitated the use of high specific radioactivity [ 35 S]sulfate [8]. It was also shown that the rate of incorporation of [ 35 S]sulfate into proteoglycans was linear over the 6 h incubation period.…”

Section: Tendon Explant Culturesmentioning

confidence: 99%

Large aggregating and small leucine‐rich proteoglycans are degraded by different pathways and at different rates in tendon

Samiric

Ilic

Handley

2004

European Journal of Biochemistry

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S]sulfate lost to the medium and retained in the matrix was determined for each day in culture. It was shown that the rate of catabolism of radiolabelled small proteoglycans (decorin and biglycan) was significantly slower (T ½ > 20 days) compared with the radiolabelled large proteoglycans (aggrecan and versican) that were rapidly lost from the tissue (T ½ 2 days). Both the small and large newly synthesized proteoglycans were lost from the matrix with either intact or proteolytically modified core proteins. When explant cultures of tendon were maintained either at 4°C or in the presence of the lysosomotrophic 2 agent ammonium chloride, inhibition of the cellular catabolic pathway for small proteoglycans was demonstrated indicating the involvement of cellular activity and lysosomes in the catabolism of small proteoglycans. It was estimated from these studies that approximately 60% of the radiolabelled small proteoglycans that were lost from the tissue were degraded by the intracellular pathway present in tendon cells. This work shows that the pathways of catabolism for large aggregating and small leucine-rich proteoglycans are different in tendon and this may reflect the roles that these two populations of proteoglycans play in the maintenance of the extracellular matrix of tendon.

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“…After electrophoresis, some gels were stained with silver (11), and the other gels were subjected to electroelution (250 mA; 4°C; 1.5 h) using polyvinylidene difluoride membranes (Immobilon P; Ref. 16). The resultant membranes were blocked with 5% (w/v) skim milk in 0.8% sodium chloride buffered at pH 7.4 with 4 mM sodium phosphate.…”

Section: Isolation and Purification Of Aggrecan Core Proteins From Fementioning

confidence: 99%

Characterization of Aggrecan Retained and Lost from the Extracellular Matrix of Articular Cartilage

Ilic¹,

Robinson²,

Handley³

1998

Journal of Biological Chemistry

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The catabolism of aggrecan in bovine articular cartilage explants is characterized by the release into the culture medium of high molecular weight aggrecan fragments, generated by the proteolytic cleavage of the core protein between residues Glu 373 and Ala 374 within the interglobular domain. In this study, the position of the carboxyl-terminus of these aggrecan fragments, as well as a major proteolytically shortened aggrecan core protein present in cartilage matrix, have been deduced by characterizing the peptides generated by the reaction of aggrecan core protein peptides with cyanogen bromide. It was shown that two out of three such peptide fragments having an amino terminus starting at Ala 374 have their carboxyl terminus located within the chondroitin sulfate 1 domain. The third and largest aggrecan core protein peptide, with an amino terminus starting at Ala 374 , has a carboxyl terminus in a region of core protein between the chondroitin sulfate 1 domain and the chondroitin sulfate 2 domain. The carboxyl terminus of this peptide appeared to be the same as that of the proteolytically degraded aggrecan core protein, which is retained within the extracellular matrix of the tissue. Another two aggrecan fragments recovered from the medium of explant cultures with amino-terminal sequences in the chondroitin sulfate 2 domain at Ala 1772 and Leu 1872 were shown to have their carboxyl termini within the G3 globular domain. These results suggest that the catabolism of aggrecan between residues Glu 373 and Ala 374 in the interglobular domain by the putative proteinase, aggrecanase, may be dependent on prior proteolytic processing within the carboxyl-terminal region of the core protein.

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Characterization and synthesis of macromolecules by adult collateral ligament

Cited by 19 publications

References 21 publications

Permeability of human medial collateral ligament in compression transverse to the collagen fiber direction

Permeability of human medial collateral ligament in compression transverse to the collagen fiber direction

Large aggregating and small leucine‐rich proteoglycans are degraded by different pathways and at different rates in tendon

Characterization of Aggrecan Retained and Lost from the Extracellular Matrix of Articular Cartilage

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