Prevalence and possible pathological significance of calcium phosphate salt accumulation in tendon matrix degeneration

Article Abstract:

Calcium salt deposits found in the muscle fibers of patients with calcifying tendinitis or degenerative tendinitis may play a role in the development of these conditions. Researchers analyzed the calcium, phosphorous, and salt content of muscle fiber samples taken from 27 patients with shoulder tendinitis, 4 patients with calcifying tendinitis, 60 normal supraspinatus tendons, and 16 normal biceps. Among the 27 patients with shoulder tendinitis, nine had elevated calcium levels and five had elevated phosphorous levels. Calcium salts identified in this group included hydroxyapatite and calcium pyrophosphate. All four patients with calcifying tendinitis had elevated levels of calcium and phosphorous with the most likely calcium salt in this group being hydroxyapatite. The technique used in this study could not distinguish between dissolved and undissolved salts.

Health aspects, Development and progression, Calcium in the body, Calcium (Nutrient), Calcification, Tendinitis

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Identification of tissue inhibitor of metalloproteinase-2 (TIMP-2)-progelatinase complex as the third metalloproteinase inhibitor peak in rheumatoid synovial fluid

Article Abstract:

A tissue inhibitor of metalloproteinase-2 (TIMP)-progelatinase complex was identified in synovial fluid of patients with rheumatoid arthritis. Synovial fluid is the fluid secreted by the connective tissue membrane lining the cavity of movable joints. A study used gelatin-Sepharose chromatography to determine the identity of a TIMP found in synovial fluid from 10 patients with rheumatoid arthritis. The TIMP was identified as TIMP-2 bound to progelatinase. Metalloproteinases are a group of enzymes that degrade different types of extracellular matrix such as collagen. Collagen is the protein that is a major component of the white fibers found in connective tissue, cartilage and bone. TIMPs inhibit the activity of metalloproteinases. Two other types of TIMPs have been identified in the synovial fluid of patients with rheumatoid arthritis.

Research, Analysis, Rheumatoid arthritis, Synovial fluid, Enzyme inhibitors

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Human shoulder tendon biopsy samples in organ culture produce procollagenase and tissue inhibitor of metalloproteinases

Article Abstract:

Severely damaged tendons may be capable of producing the necessary enzymes to repair themselves. Tendons produce an enzyme called collagenase that breaks down the fibers of the tendons and an enzyme called tissue inhibitor of metalloproteinase (TIMP) that inhibits collagenase. Researchers tested 11 normal and 10 abnormal tendon tissue samples from 18 patients with late-stage tendon disease for collagenase and TIMP activity. All of the samples contained collagenase and TIMP. TIMP levels were higher than collagenase levels in nearly all of the samples. The TIMP levels were high enough to inhibit collagenase activity. Both of these enzymes are necessary in the repair of connective tissue.

Wound healing, Tendon injuries

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