Tendon degeneration and chronic shoulder pain: changes in the collagen composition of the human rotator cuff tendons in rotator cuff tendinitis.
OBJECTIVE
To analyse the collagen composition of normal adult human supraspinatus tendon and to compare with: (1) a flexor tendon (the common biceps tendon) which is rarely involved in any degenerative pathology; (2) degenerate tendons from patients with chronic rotator cuff tendinitis.


METHODS
Total collagen content, collagen solubility and collagen type were investigated by hydroxyproline analysis, acetic acid and pepsin digestion, cyanogen bromide peptide analysis, SDS-PAGE and Western blotting.


RESULTS
The collagen content of the normal cadaver supraspinatus tendons (n = 60) was 96.3 micrograms HYPRO/mg dry weight (range 79.3-113.3) and there was no significant change across the age range 11 to 95 years. There was no significant difference from the common biceps tendon [93.3 (13.5) micrograms HYPRO/mg dry weight, n = 24]. Although extremely insoluble in both acetic acid and pepsin, much of the collagen was soluble after cyanogen bromide digestion [mean 47.9% (29.8)]. Seventeen per cent (10/60) of the 'normal' cadaver supraspinatus tendon sample contained more than 5% type III collagen, although none of the common biceps tendons had significant amounts. Degenerate supraspinatus and subscapularis tendons had a reduced collagen content [83.8 (13.9) micrograms/mg dry weight and 76.9 (16.8) micrograms/mg dry wt respectively) and were more soluble in acetic acid, pepsin and cyanogen bromide (p < 0.001). Eighty two per cent (14/17) of supraspinatus tendons and 100% (8/8) of subscapularis tendons from patients with tendinitis contained more than 5% type III collagen.


CONCLUSIONS
The changes in collagen composition in rotator cuff tendinitis are consistent with new matrix synthesis, tissue remodelling and wound healing, in an attempt to repair the tendon defect, even in old and degenerate tendons. An increase in type III collagen in some 'normal' cadaver supraspinatus tendons is evidence that changes in collagen synthesis and turnover may precede tendon rupture. These changes may be the result of repeated minor injury and microscopic fibre damage or a consequence of local factors such as reduced vascular perfusion, tissue hypoxia, altered mechanical forces and the influence of cytokines. These collagenous changes may accumulate with age and substantially weaken the tendon structure, predisposing the tendon to rotator cuff tendinitis and eventual tendon rupture.
Rheumatology Research Unit, Addenbrooke's Hospital, Cambridge, United Kingdom.
G P
GP
Riley
R L
RL
Harrall
C R
CR
Constant
M D
MD
Chard
T E
TE
Cawston
B L
BL
Hazleman
D000293:Adolescent; D000328:Adult; D000368:Aged; D000369:Aged, 80 and over; D015153:Blotting, Western; D002648:Child; D002908:Chronic Disease; D003094:Collagen / Q000032:analysis*; D003488:Cyanogen Bromide; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D006801:Humans; D008297:Male; D008875:Middle Aged; D010146:Pain / Q000378:metabolism; D017006:Rotator Cuff / Q000737:chemistry*; D012785:Shoulder Joint; D012995:Solubility; D052256:Tendinopathy / Q000378:metabolism*; D013710:Tendons / Q000737:chemistry
D003094:Collagen; D003488:Cyanogen Bromide