THE RELATION BETWEEN JOINT STIFFNESS UPON EXPOSURE TO COLD AND THE CHARACTERISTICS OF SYNOVIAL FLUID

1952 ◽  
Vol 30 (5) ◽  
pp. 367-377 ◽  
Author(s):  
John Hunter ◽  
E. H. Kerr ◽  
M. G. Whillans

Previous laboratory tests have shown that joint temperatures, on exposure to low ambient temperatures, fall to a greater extent than muscle, rectal, or average skin temperatures. The fall in temperature is accompanied by an increased resistance of joints to movement, and the maximum speed with which the joint can be moved decreases. The predominant type of movement at the human knee joint and interphalangeal joints is a gliding one. The characteristics of synovial fluid explain the increased forces required to move a joint and the loss in speed of movement on exposure to cold. In vivo studies support such predictions.

2014 ◽  
Vol 15 (5) ◽  
pp. 7250-7265 ◽  
Author(s):  
Congming Zhang ◽  
Xiaochun Wei ◽  
Chongwei Chen ◽  
Kun Cao ◽  
Yongping Li ◽  
...  

1985 ◽  
Vol 225 (1) ◽  
pp. 195-201 ◽  
Author(s):  
D A Swann ◽  
F H Silver ◽  
H S Slayter ◽  
W Stafford ◽  
E Shore

Lubricin was isolated from bovine ankle, metacarpophalangeal and knee and human knee synovial fluids. The lubricins isolated from the bovine joint fluids had the same amino acid and carbohydrate compositions, but differences were observed in the relative molecular masses. The Mr values of bovine metacarpophalangeal and ankle lubricin determined by light-scattering measurements were about 200 000, whereas values of 132 000 and 143 000 were obtained for the bovine knee lubricin. The human knee lubricin had a similar carbohydrate composition to bovine knee lubricin except for the higher glucosamine content, and the amino acid composition differed slightly. The human sample had a lower glutamic acid content and a leucine/isoleucine ratio of 2:1 compared with 1:1 in the bovine. The Mr value of the human knee lubricin (166 000) was also lower than that of the bovine metacarpophalangeal and ankle samples. The Mr value of the bovine knee lubricin determined by sedimentation-equilibrium measurements was 171 000. The length measurements determined by electron microscopy and also the sedimentation measurements showed considerable polydispersity and indicate that the degree of extension of lubricin molecules can vary. Friction measurements showed that the human knee synovial-fluid lubricin had equivalent lubricating ability in a test system in vitro to that observed for lubricin isolated from normal bovine synovial fluids. The lubricating ability of lubricin was concentration-dependent, and each lubricin sample was able to act as a lubricant in vitro in an equivalent manner to whole synovial fluid at concentrations that are thought to occur in vivo.


1994 ◽  
Vol 27 (6) ◽  
pp. 809 ◽  
Author(s):  
Steve McFaull ◽  
Mario Lamontagne

2003 ◽  
Vol 11 (12) ◽  
pp. 839-844 ◽  
Author(s):  
S. Fuchs ◽  
B. Rolauffs ◽  
S. Arndt ◽  
C.O. Tibesku ◽  
P. Prehm

Radiology ◽  
2015 ◽  
Vol 277 (2) ◽  
pp. 477-488 ◽  
Author(s):  
Fang Liu ◽  
Kwang Won Choi ◽  
Alexey Samsonov ◽  
Richard G. Spencer ◽  
John J. Wilson ◽  
...  

2001 ◽  
Vol 358 (3) ◽  
pp. 615-626 ◽  
Author(s):  
John D. SANDY ◽  
Christie VERSCHAREN

Studies of aggrecan proteolysis in human joints have implicated both the aggrecanase [ADAMTS, a disintegrin-like and metalloprotease (reprolysin-type) with thrombospondin type 1 motif] and matrix metalloproteinase (MMP) families. We have analysed the aggrecan core protein species present in vivo in both articular cartilage and synovial fluids from normal, acutely injured and osteoarthritic joints. Normal cartilage contains at least seven major G1 domain (the N-terminal globular domain of aggrecan)-bearing species, of which three (full-length core, G1-NITEGE373 and G1-VDIPEN341) have been identified. The C-terminals of the others are unknown but digestion of fetal human aggrecan with MMP-3 and crude aggrecanase suggests that they are products of MMP-like activity in vivo. Normal synovial fluids contain at least 10 species, of which nine result from ADAMTS-dependent cleavage, and this cleavage occurs at all of the five known aggrecanase sites. Aggrecan fragments in the cartilage and synovial fluids of acutely injured joints are generally similar to normal, but all contain a markedly increased ratio of G1-NITEGE to G1-VDIPEN. Aggrecan from the cartilage of late-stage osteoarthritis patients is remarkably similar to normal, whereas the synovial fluid aggrecan is more fragmented than that from normal or injured knees. The analyses suggest that the role of the ADAMTS and these MMP-like activities in human cartilage are distinctly different. Excessive ADAMTS activity in vivo is destructive to cartilage matrix, since the bulk of the glycosaminoglycan (GAG)-bearing products are released from the tissue into the synovial fluid following cleavage of the Glu373–Ala374 bond. In contrast, the MMP-like activity appears to be essentially non-destructive, since much of the GAG-bearing product is retained in the tissue following cleavages that are in the more C-terminal regions of the molecule.


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