The Third Dimension of Rheumatoid Arthritis

1970 ◽  
Vol 28 ◽  
pp. 338-339
Author(s):  
Jeanne M. Riddle ◽  
Gilbert B. Bluhm
Keyword(s):  
Rheumatoid Arthritis ◽  
Electron Microscopy ◽  
Membrane Surface ◽  
Three Dimensional ◽  
Joint Space ◽  
Cell Contact ◽  
Synovial Lining ◽  
Synovial Lining Cells ◽  
Third Dimension ◽  
Dynamic Quality

Our application of scanning electron microscopy to the investigation of synovial membrane surface topography in humans has yielded new morphologic information. Samples of synovium removed from patients with advanced rheumatoid arthritis exhibited projecting villi such as those depicted in Fig. 1 as a prominent feature of their three-dimensional microarchi-tecture. In addition, localized areas of fibrin deposition, large parallel folds and focal irregular cavities were observed. Synovial lining cells were protuberant, increased in number and variable in size with many larger synoviocytes evident. Individual synoviocytes or small clusters were separated by only narrow areas of intercellular matrix. Membrane activities such as erythrophagocytosis and pinocytosis, the latter illustrated in Fig. 2, attested to the dynamic quality of the synovial lining cells as they participated in this inflammatory disease state. Frequently individual synovial lining cells were connected by slender, intercellular cytoplasmic spans. This form of cellular linkage illustrated in Fig. 2-was heretofore undiscovered by studies utilizing either light or transmission electron microscopy. Large finger-like structures depicted in Fig. 2 also jutted from some synoviocytes and either extended into the joint space or bridged gaps between adjacent synovial lining cells. In the latter situation, these filopodia perhaps served as a second type of adhesive cell contact as the layers of synoviocytes increased in depth.

scholarly journals Biologically active thrombomodulin is synthesized by adherent synovial fluid cells and is elevated in synovial fluid of patients with rheumatoid arthritis

Blood ◽  
1993 ◽  
Vol 81 (3) ◽  
pp. 726-733 ◽  
Author(s):  
EM Conway ◽  
B Nowakowski
Keyword(s):  
Rheumatoid Arthritis ◽  
Synovial Fluid ◽  
Protein C ◽  
Inflammatory Process ◽  
Biologically Active ◽  
Northern Analysis ◽  
Synovial Lining ◽  
Local Synthesis ◽  
Synovial Lining Cells ◽  
Synovial Fluid Cells

Abstract Thrombomodulin (TM) is a transmembrane glycoprotein that interacts with thrombin, thereby serving as a cofactor in the activation of protein C, a major physiologically relevant natural anticoagulant. Although initially described as a vascular endothelial cell receptor, TM has also been reported to be synthesized by several cells, including megakaryocytes, platelets, monocytes, neutrophils (PMN), mesothelial cells, and synovial lining cells. A prominent feature of rheumatoid arthritis (RA) is infiltration of PMN into the joint space. To determine whether TM might play a role in the inflammatory process, we examined synovial fluid for the presence of TM in 10 patients with RA and five patients with osteoarthritis (OA). We determined that the mean synovial fluid and plasma TM levels in the OA group were 23.5 ng/mL and 24.2 ng/mL, respectively, whereas those with RA had a significantly elevated mean synovial fluid TM level of 136.2 ng/mL as compared with the plasma TM concentration of 43.9 ng/mL (P < .05). Synovial fluid TM levels did not correlate with PMN counts (r = .261). Purified TM from synovial fluid was identical in molecular weight to plasma-derived TM and was biologically functional with respect to protein C cofactor activity. Using direct immunofluorescence, we determined that adherent cultured synovial fluid cells that are not monocytoid in origin express surface and cytoplasmic TM, thereby providing an alternative source of the protein. Biologic activity of the cell-surface TM was confirmed by acceleration of thrombin-dependent protein C activation. Northern analysis of RNA extracted from the cultured cells indicated that TM messenger RNA was present, suggesting local synthesis. Our results indicate that in RA-associated synovial effusions, biologically active TM is increased, the source of which may be from plasma, PMN, and/or synovial lining cells. TM may play a regulatory role either in fibrin deposition in the inflamed joint and/or in the progression of the inflammatory process.

scholarly journals Localization of Cathepsins B and D in the Synovial Lining Cells of the Normal Rat Temporomandibular Joint by Immuno-light and -electron Microscopy.

1994 ◽  
Vol 27 (5) ◽  
pp. 441-450 ◽  
Author(s):  
TAMOTSU KIYOSHIMA ◽  
MIZUHO A. KIDO ◽  
TAKAYUKI TSUKUBA ◽  
HIDETAKA SAKAI ◽  
KENJI YAMAMOTO ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Temporomandibular Joint ◽  
Light And Electron Microscopy ◽  
Synovial Lining ◽  
Synovial Lining Cells ◽  
Normal Rat

scholarly journals Ultrastructure of the adhesion of bacteria to the epithelial cell membrane of three-day postnatal rat tongue mucosa: a transmission and high-resolution scanning electron microscopic study

2007 ◽  
Vol 18 (4) ◽  
pp. 320-323 ◽  
Author(s):  
Ii-sei Watanabe ◽  
Koichi Ogawa ◽  
Marcelo Cavenaghi Pereira da Silva ◽  
Aracy Akiko Motoyama ◽  
Eduardo Shigueaki Kado ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
High Resolution ◽  
Cell Membrane ◽  
Membrane Surface ◽  
Three Dimensional ◽  
Electron Microscopic ◽  
Tem Analysis ◽  
Native Flora ◽  
Scanning Electron Microscopic Study ◽  
Scanning Electron

Togue mucosa surface of 3-day postnatal rats was examined under transmission electron microscopy (TEM) and high-resolution scanning electron microscopy (HRSEM). For HRSEM analysis, the specimens were fixed in the same solution for 24 h, postfixed in 2% osmiun tetroxide, critical-point dried and coated with platinum-palladium. For TEM analysis, the specimens were fixed using modified Karnovsky solution and embedded in Spurr resin. The results revealed the presence of numerous microplicae in the membrane surface of keratinized epithelial cells to which groups of bacteria were attached. These bacteria were staphylococcus and coccus organized either in rows or at random, which were visualized in three-dimensional HRSEM images. At high magnification, the TEM images revealed the adhesion of bacteria to the cell membrane through numerous filamentous structures comprising the glycocalyx. The fine fibrillar structures rising from each bacterium and from cell membrane were clearly seen. These characteristics on bacteria structure may be used for future control or prevention of bacterial diseases and for installation of the oral native flora.

scholarly journals Biologically active thrombomodulin is synthesized by adherent synovial fluid cells and is elevated in synovial fluid of patients with rheumatoid arthritis

Blood ◽  
1993 ◽  
Vol 81 (3) ◽  
pp. 726-733 ◽  
Author(s):  
EM Conway ◽  
B Nowakowski
Keyword(s):  
Rheumatoid Arthritis ◽  
Synovial Fluid ◽  
Protein C ◽  
Inflammatory Process ◽  
Biologically Active ◽  
Northern Analysis ◽  
Synovial Lining ◽  
Local Synthesis ◽  
Synovial Lining Cells ◽  
Synovial Fluid Cells

Thrombomodulin (TM) is a transmembrane glycoprotein that interacts with thrombin, thereby serving as a cofactor in the activation of protein C, a major physiologically relevant natural anticoagulant. Although initially described as a vascular endothelial cell receptor, TM has also been reported to be synthesized by several cells, including megakaryocytes, platelets, monocytes, neutrophils (PMN), mesothelial cells, and synovial lining cells. A prominent feature of rheumatoid arthritis (RA) is infiltration of PMN into the joint space. To determine whether TM might play a role in the inflammatory process, we examined synovial fluid for the presence of TM in 10 patients with RA and five patients with osteoarthritis (OA). We determined that the mean synovial fluid and plasma TM levels in the OA group were 23.5 ng/mL and 24.2 ng/mL, respectively, whereas those with RA had a significantly elevated mean synovial fluid TM level of 136.2 ng/mL as compared with the plasma TM concentration of 43.9 ng/mL (P < .05). Synovial fluid TM levels did not correlate with PMN counts (r = .261). Purified TM from synovial fluid was identical in molecular weight to plasma-derived TM and was biologically functional with respect to protein C cofactor activity. Using direct immunofluorescence, we determined that adherent cultured synovial fluid cells that are not monocytoid in origin express surface and cytoplasmic TM, thereby providing an alternative source of the protein. Biologic activity of the cell-surface TM was confirmed by acceleration of thrombin-dependent protein C activation. Northern analysis of RNA extracted from the cultured cells indicated that TM messenger RNA was present, suggesting local synthesis. Our results indicate that in RA-associated synovial effusions, biologically active TM is increased, the source of which may be from plasma, PMN, and/or synovial lining cells. TM may play a regulatory role either in fibrin deposition in the inflamed joint and/or in the progression of the inflammatory process.

Thrombin-Cleaved Osteopontin Is Regulated by Thrombin-Activatable Carboxypeptidase B in Rheumatoid Arthritis.

Blood ◽  
2007 ◽  
Vol 110 (11) ◽  
pp. 1744-1744
Author(s):  
Timothy Myles ◽  
Shadi A. Sharif ◽  
Xiao-Yan Du ◽  
Jason J. Song ◽  
Price Elizabeth ◽  
...  
Keyword(s):  
Rheumatoid Arthritis ◽  
Joint Space ◽  
Statistical Correlation ◽  
Binding Motif ◽  
Carboxypeptidase B ◽  
Cytokine Analysis ◽  
C Terminus ◽  
Synovial Lining Cells ◽  
Homeostatic Response ◽  
Multiplex Cytokine

Abstract The pro-inflammatory cytokine osteopontin (OPN) is present in rheumatoid arthritis (RA) synovial fluids (SF). OPN can be cleaved by thrombin exposing the cryptic C-terminal α4β1/α9β1 integrin-binding motif (SVVYGLR). We have previously shown that thrombin-activated proCPB (CPB) can remove the C-terminal arginine from the SVVYGLR motif abrogating its α4β1 binding. Using peptides based on the C-terminus of thrombin-cleaved OPN (OPN-R) and thrombin/CPB-cleaved OPN (OPN-L), rabbit anti-OPN-R and anti-OPN-L antibodies were generated. Specificity of these antibodies was demonstrated by western blot analysis. Specific ELISAs for OPN-R and OPN-L showed significant elevation of OPN-R and OPN-L levels in SF from patients with RA (n=26) as compared to osteoarthritis (OA, n=18) and psoriatic arthritis (PA, n=10). (OPN-R median values: 138.6 ng/mL (RA), 10.6 ng/mL (OA), and 2.2 ng/mL (PA) p &lt;0.001; OPN-L median values 205.3 ng/mL (RA), 25.9 ng/mL (OA), and undetectable in PA p &lt;0.003). Multiplex cytokine analysis showed that elevated OPN-R and OPN-L levels in RA were significantly correlated with multiple inflammatory cytokines including IL-6, IL-12p40 and FGF-2, while OPN-FL levels only exhibited a statistical correlation with IL-6. Synovial lining cells expressed functional TM that supported the activation of proCPB to CPB by thrombin. ProCPB activation by thrombin, which may occur either systemically or locally within the inflamed joint space, inactivates thrombin-cleaved OPN and C5a and represents a homeostatic response in modulating the inflammatory process in RA.

Sign in / Sign up

Export Citation Format

Share Document