Marked suppression by salicylate of the augmented proteoglycan synthesis in osteoarthritic cartilage

Palmoski, Marshall J.; Colyer, Robert A.; Brandt, Kenneth D.

doi:10.1002/art.1780230114

Cited by 97 publications

(31 citation statements)

References 30 publications

(4 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…12 normal adult mongrel dogs underwent transection of the right ACL through a sterile incision using a standard surgical procedure employed in this laboratory (8,9). Briefly, the joint capsule was entered via an oblique anteromedial approach.…”

Section: Methodsmentioning

confidence: 99%

“…Briefly, the joint capsule was entered via an oblique anteromedial approach. The ACL was transected with a scalpel, and the cartilage was not damaged (8). After suturing, the animals were allowed to ambulate in their pens until they were killed with an overdose of sodium pentothal 8-14 wk postoperatively.…”

Section: Methodsmentioning

confidence: 99%

“…Portions of one biopsy from each dog were sectioned (6 Mm) and stained with Safranin-O-Fast green (23). The other piece was analyzed for uronic acid concentration (24, 25) and water content (8).…”

Section: Methodsmentioning

confidence: 99%

See 2 more Smart Citations

Cartilage matrix glycoprotein is present in serum in experimental canine osteoarthritis.

Fife¹,

Brandt²

1989

J. Clin. Invest.

View full text Add to dashboard Cite

We have described previously a disulfide-bonded 550,000-D cartilage matrix glycoprotein (CMGP), which is found in normal hyaline cartilage, fibrocartilage, and the vitreous of the eye, and consists of subunits with apparent molecular weights of 130,000 in 4% gels (116,000 in 9% gels). In osteoarthritic cartilage from dogs subjected to transection of the anterior cruciate ligament (ACL), CMGP is cleaved to major immunoreactive fragments with apparent molecular weights of 65,000 and 75,000 after reduction with 2-mercaptoethanol. In the present study, using immunolocation analysis, a monoclonal antibody to CMGP did not react with serum from 8 of 12 dogs before ACL transection but did react with serum from seven of these animals 4 wk after surgery and with serum from 10 dogs at sacrifice, 8-14 wk after ACL transection. Serum from four dogs reacted with the monoclonal antibody before ACL transection. Serum from two dogs was negative at all time points. Immunolocation studies using a polyclonal antiserum to CMGP were performed in seven of these dogs and produced results identical with the monoclonal antibody in four dogs. In contrast, analysis of serial serum samples from three dogs with cartilage atrophy revealed no evidence of CMGP at any time point. These data suggest that CMGP may be a serum marker for osteoarthritis in this canine model.

show abstract

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

See 1 more Smart Citation

Cartilage matrix glycoprotein is present in serum in experimental canine osteoarthritis.

Fife¹,

Brandt²

1989

J. Clin. Invest.

View full text Add to dashboard Cite

show abstract

“…Full-thickness core biopsy specimens of articular cartilage were obtained from the weight-bearing surfaces of the femoral condyles of all operated and unoperated knees for routine histologic study. Biopsy specimens from each knee from 6 dogs were used for uronic acid and water content determinations (4,5), and specimens from each knee from 3 dogs were used for immunofluorescence studies (25). The rest of the cartilage from each knee from 5 dogs was shaved with a scalpel and handled separately for extraction.…”

mentioning

confidence: 99%

“…Uronic acid content of the cartilage was determined by the carbazole method (30). Water content of the cartilage was determined as described previously (4,5,15).…”

mentioning

confidence: 99%

Alterations in a cartilage matrix glycoprotein in canine osteoarthritis

Fife

1986

Arthritis & Rheumatism

View full text Add to dashboard Cite

A number of biochemical abnormalities have been described in osteoarthritic (OA) cartilage, but little study has been devoted to changes in the noncollagenous, nonproteoglycan proteins of cartilage in this condition. Using a canine model of OA produced by transection of the anterior cruciate ligament of the knee, we have demonstrated that distinct alterations occur in a 550,000-dalton cartilage matrix glycoprotein in OA canine cartilage. This protein is a major protein constituent of normal articular cartilage. Fragments which are immunologically cross-reactive with the 550,000-dalton protein were more abundant in OA cartilage than in normal articular cartilage. Immunofluorescence studies revealed that staining with specific antiserum to the protein was absent in OA cartilage. This was the only noncollagenous, nonproteoglycan protein noted to undergo significant changes in this model of OA.Osteoarthritis (OA) is a common joint disease which causes considerable morbidity. It has been difficult to study this condition in humans because of variability in the severity of the osteoarthritic lesion in human cartilage. A canine model created by anterior

show abstract

Effects of salicylate on chondrocytes from osteoarthritic and contralateral knees of dogs with unilateral anterior cruciate ligament transection

Slowman‐Kovacs

Albrecht

Brandt

1989

Arthritis & Rheumatism

Self Cite

View full text Add to dashboard Cite

Salicylates suppress net glycosaminoglycan synthesis in articular cartilage. The inhibitory effect is greater in osteoarthritic (OA) cartilage than in normal cartilage. Whether the isolated OA chondrocyte is inherently more susceptible to the effects of salicylate on glycosaminoglycan metabolism has not been determined. The results of this study show that, after isolation from the extracellular matrix, normal and OA chondrocytes in suspension culture are similarly susceptible to the metabolic effects of salicylate. However, chondrocytes from the contralateral knees of dogs with unilateral OA were notably resistant to the effects of salicylate.Salicylates produce reversible, concentrationdependent suppression of proteoglycan (PG) synthesis by normal articular cartilage in vitro. The effect is much greater in osteoarthritic (OA) cartilage than in normal cartilage (1). Since uptake of ''C-acetylsalicylic acid by slices of OA cartilage has been shown to be significantly greater than that by normal cartilage (I), the depletion of negatively charged PGs in the matrix of OA cartilage presumably facilitated diffusion of the weakly acidic salicylate into the matrix. This possibility was supported by data demonstrating increased suppression of PG synthesis in normal cartilage after enzymatic depletion of its PGs (2).The above data do not exclude the additional possibility that in OA, the chondrocyte, which is intrinsically hypermetabolic (3,4), may be more susceptible than normal to the effects of salicylate. In the present study, we used isolated chondrocytes in suspension cultures, rather than cartilage organ cultures, to examine the susceptibility of the OA chondrocyte to salicylate. MATERIALS AND METHODSSurgical procedures. OA was induced in a standard manner in 9 normal adult mongrel dogs (25-30 kg) by transection of the anterior cruciate ligament of the right knee (1). Postoperatively, all dogs bore weight on the operated limb by the third day and ambulated freely in caged runs (4 feet x 8 feet) until they were killed 10-13 weeks later. Nine additional adult mongrel dogs that underwent no surgical procedure were used as normal controls.Tissues. At the time the dogs were killed, fullthickness samples of the articular cartilage and underlying subchondral bone were obtained from the central regions of the habitually loaded area of the medial femoral condyle of both knees of each animal for histologic study. Slices of articular cartilage (10-15 mg wet weight) were taken from the same sites for determination of dry weight and uronic acid concentration. The remainder of the cartilage from the articular surfaces of the medial and lateral femoral condyles and tibia1 plateaus was used for isolation of chondrocytes.

show abstract

Marked suppression by salicylate of the augmented proteoglycan synthesis in osteoarthritic cartilage

Cited by 97 publications

References 30 publications

Cartilage matrix glycoprotein is present in serum in experimental canine osteoarthritis.

Cartilage matrix glycoprotein is present in serum in experimental canine osteoarthritis.

Alterations in a cartilage matrix glycoprotein in canine osteoarthritis

Effects of salicylate on chondrocytes from osteoarthritic and contralateral knees of dogs with unilateral anterior cruciate ligament transection

Contact Info

Product

Resources

About