scholarly journals Expression of 92-kD type IV collagenase/gelatinase (gelatinase B) in osteoarthritic cartilage and its induction in normal human articular cartilage by interleukin 1.

1993 ◽  
Vol 92 (1) ◽  
pp. 179-185 ◽  
Author(s):  
M Mohtai ◽  
R L Smith ◽  
D J Schurman ◽  
Y Tsuji ◽  
F M Torti ◽  
...  
Keyword(s):  
Articular Cartilage ◽  
Interleukin 1 ◽  
Human Articular Cartilage ◽  
Type Iv Collagenase ◽  
Osteoarthritic Cartilage ◽  
Gelatinase B ◽  
Type Iv ◽  
Normal Human

scholarly journals Immunolocalization of type III collagen in human articular cartilage prepared by high-pressure cryofixation, freeze-substitution, and low-temperature embedding.

1995 ◽  
Vol 43 (4) ◽  
pp. 421-427 ◽  
Author(s):  
R D Young ◽  
P A Lawrence ◽  
V C Duance ◽  
T Aigner ◽  
P Monaghan
Keyword(s):  
High Pressure ◽  
Articular Cartilage ◽  
Polyclonal Antibodies ◽  
Freeze Substitution ◽  
Immunogold Electron Microscopy ◽  
Type Iii Collagen ◽  
Human Articular Cartilage ◽  
Chemical Fixation ◽  
Osteoarthritic Cartilage ◽  
Type Iii

We localized Type III collagen by immunogold electron microscopy in resin sections of intact normal and osteoarthritic human articular cartilage. Comparisons of antibody staining between tissue prepared by high-pressure cryofixation and freeze-substitution without fixatives and that exposed to conventional mild chemical fixation with paraformaldehyde showed that dedicated cryotechniques yielded superior preservation of epitopes that are modified by chemical fixation, and simultaneously provided good ultrastructural preservation. Type III collagen was detected with two polyclonal antibodies, one against the triple-helical domain of the molecule and a second against the more antigenic, globular amino pro-peptide domain, which in this collagen is retained in the extracellular matrix after secretion. Positive labeling was seen in association with the major interstitial fibrils, suggesting co-polymerization of Types III and II collagen in cartilage. Type III collagen could not be detected in aldehyde-fixed normal cartilage. In fixed osteoarthritic cartilage, Type III was detectable only when the antibody to the amino pro-peptide was employed. In contrast, high-pressure cryofixation and freeze-substitution preserved epitopes for both antibodies, permitting immunodetection of Type III collagen in normal and osteoarthritic cartilage. Cryotechniques offer exciting possibilities for significantly improving the immunolocalization of collagens and other fixative-sensitive antigens in situ.

scholarly journals Age-related changes in the composition and structure of human articular-cartilage proteoglycans

1978 ◽  
Vol 176 (3) ◽  
pp. 683-693 ◽  
Author(s):  
M T Bayliss ◽  
S Y Ali
Keyword(s):  
Hyaluronic Acid ◽  
Articular Cartilage ◽  
Age Groups ◽  
Human Articular Cartilage ◽  
Human Cartilage ◽  
Keratan Sulphate ◽  
Age Related ◽  
Composition And Structure ◽  
Normal Human ◽  
Cartilage Proteoglycans

1. Analysis of the purified proteoglycans extracted from normal human articular cartilage with 4M-guanidinium chloride showed that there was an age-related increase in their content of protein and keratan sulphate. 2. The hydrodynamic size of the dissociated proteoglycans also decreased with advancing age, but there was little change in the proportion that could aggregate. 3. Results suggested that some extracts of aged-human cartilage had an increased content of hyaluronic acid compared with specimens from younger patients. 4. Dissociated proteoglycans, from cartilage of all age groups, bind to hyaluronic acid and form aggregates in direct proportion to the hyaluronic acid concentration. 5. Electrophoretic heterogeneity of the dissociated proteoglycans was demonstrated on polyacrylamide/agarose gels. The number of proteoglycan species observed was also dependent on the age of the patient.

Effects of Interleukin-1 and Anti-Inflammatory Drugs on the Degradation of Human Articular Cartilage

Drugs ◽  
1988 ◽  
Vol 35 (Supplement 1) ◽  
pp. 33-41 ◽  
Author(s):  
M. Shinmei ◽  
T. Kikuchi ◽  
K. Masuda ◽  
Y. Shimomura
Keyword(s):  
Articular Cartilage ◽  
Interleukin 1 ◽  
Human Articular Cartilage ◽  
Inflammatory Drugs ◽  
Anti Inflammatory

MODULATION OF ENDOGENOUS OSTEOGENIC PROTEIN-1 (OP-1) BY INTERLEUKIN-1 IN ADULT HUMAN ARTICULAR CARTILAGE

2003 ◽  
Vol 85 ◽  
pp. 67-74 ◽  
Author(s):  
CHARIS MERRIHEW ◽  
STEPHAN SOEDER ◽  
DAVID C. RUEGER ◽  
KLAUS E. KUETTNER ◽  
SUSAN CHUBINSKAYA
Keyword(s):  
Articular Cartilage ◽  
Interleukin 1 ◽  
Human Articular Cartilage ◽  
Adult Human ◽  
Osteogenic Protein

scholarly journals N-terminal sequence of proteoglycan fragments isolated from medium of interleukin-1-treated articular-cartilage cultures. Putative site(s) of enzymic cleavage

1992 ◽  
Vol 284 (2) ◽  
pp. 589-593 ◽  
Author(s):  
P Loulakis ◽  
A Shrikhande ◽  
G Davis ◽  
C A Maniglia
Keyword(s):  
Hyaluronic Acid ◽  
Articular Cartilage ◽  
Amino Acid ◽  
Interleukin 1 ◽  
Human Articular Cartilage ◽  
Terminal Amino Acid ◽  
Protein Core ◽  
Nasal Cartilage ◽  
The Media ◽  
Terminal Amino

Bovine articular cartilage was cultured both in the presence and in the absence of human recombinant interleukin-1 alpha (IL-1) (100 units/ml). Addition of this cytokine stimulated matrix degradation approx. 3-fold. This increased degradation permitted characterization of the large chondroitin sulphate proteoglycan (aggrecan) fragments accumulating in the media. When compared with controls, the proteoglycans isolated from the medium of cultures treated with IL-1 exhibited a decrease in the Kav. (control 0.25; IL-1-treated 0.37), determined by Sepharose CL-2B chromatography. This decrease in proteoglycan size was accompanied by a decreased ability of these monomers to associate with hyaluronic acid. Thus only 20% of the proteoglycans isolated from the medium of IL-1-treated cultures, compared with 39% for control cultures, had the capacity to form high-M(r) aggregates with hyaluronic acid. SDS/PAGE analysis of the proteoglycans from the media of IL-1-treated cultures demonstrated several large proteoglycan protein-core bands (M(r) 144,000-380,000). The protein-core bands with M(r) 144,000-266,000 exhibited a significantly decreased reactivity with monoclonal antibody 1-C-6 (specific for domains G1 and G2). The N-terminal amino acid sequence of four of these protein-core bands (M(r) 144,000, 173,000, 214,000 and 266,000) yielded sequences LGQRPPV-Y-PQLF(E), AGEGP(S)GILEL-GAP(S)-AP(D)M, GLG-VEL-LPGE and (A)RGSVIL-AKPDFEV-P-A. A comparison of these N-terminal amino acid sequences with the published proteoglycan sequence for bovine nasal cartilage [Oldberg, Antonsson & Heinegård (1987) Biochem. J. 243, 255-259], rat chondrosarcoma [Doege, Sasaki, Horigan, Hassell & Yamada (1987) J. Biol. Chem. 262, 17757-17769] and human articular cartilage [Doege, Sasaki, Kimura & Yamada (1991) J. Biol. Chem. 266, 894-902] permitted assignment of their relative positions on the core protein. Furthermore, on the basis of this similarity to published sequence, putative sites of enzymic cleavage were constructed. These theoretical cleavage sites revealed a glutamic acid residue in the P1 position and an uncharged polar or non-polar residue in the P1′ position.

scholarly journals Proteolytic Cascade Enzymes Increase in Focal Cerebral Ischemia in Rat

1996 ◽  
Vol 16 (3) ◽  
pp. 360-366 ◽  
Author(s):  
Gary A. Rosenberg ◽  
Milo Navratil ◽  
Frank Barone ◽  
Giora Feuerstein
Keyword(s):  
Focal Cerebral Ischemia ◽  
Vasogenic Edema ◽  
Artery Occlusion ◽  
Tissue Type ◽  
Intracerebral Injection ◽  
Gelatinase A ◽  
Type Iv Collagenase ◽  
Gelatinase B ◽  
Type Iv ◽  
Wistar Kyoto

Cerebral infarction initiates a cascade of molecular events, leading to proteolytic cell death. Matrix-degrading metalloproteinases (MMPs) are neutral proteases involved in extracellular matrix damage. Type IV collagenase is an MMP that increases cerebral capillary permeability after intracerebral injection and may be important along with plasminogen activators (PA) in secondary brain edema in stroke. Therefore, we measured MMPs and PAs in spontaneously hypertensive (SHR) or Wistar-Kyoto (WKY) rats with permanent middle cerebral artery occlusion (MCAO). Brain tissue was assayed for MMPs and PAs at 1, 3, 12, and 24 h and 5 days after occlusion, using substrate gel Polyacrylamide electrophoresis (zymography). SHR showed an increase in 92-kDa type IV collagenase (gelatinase B) in the infarcted hemisphere compared with the opposite side at 12 and 24 h ( p < 0.05). Gelatinase A remained the same in both infarcted and normal tissue until 5 days after injury, when it increased significantly ( p < 0.05). Urokinase-type PA was increased significantly at 12 and 24 h and 5 days, while tissue-type PA was decreased significantly at 1, 12, and 24 h in the ischemic compared with the nonischemic hemisphere. Gelatinase B was markedly increased in SHR at 12 and 24 h compared with WKY ( p < 0.05). Secondary vasogenic edema is maximal 1–2 days after a stroke, which is the time that gelatinase B was elevated. The time of appearance of gelatinase B suggests a role in secondary tissue damage and vasogenic edema, while gelatinase A may be involved in tissue repair.

scholarly journals Ultrastructure of Chondrocytes in Osteoarthritic Femoral Articular Cartilage

2015 ◽  
Vol 11 (3) ◽  
pp. 221-225
Author(s):  
Nj Goya ◽  
M Gupta ◽  
K Joshi
Keyword(s):  
Electron Microscope ◽  
Articular Cartilage ◽  
Control Group ◽  
Human Articular Cartilage ◽  
Joint Motion ◽  
Age Group ◽  
Radiographic Evidence ◽  
Osteoarthritic Cartilage ◽  
Total Knee ◽  
Ultrastructural Findings

Background Osteoarthritis (OA) is a common problem in elderly, but it is not an inevitable feature of ageing. About 80-90% of individuals of both sexes have radiographic evidence of OA by the time they reach an age of 65. But not all of them have the symptoms like pain and decreased joint motion. Objective The objective of the present study was conducted to find out whether the osteoarthritic changes in human articular cartilage are similar to the ageing process or not. Methods Femoral articular cartilage specimens obtained from 13 osteoarthritic patients (52-80years) undergoing total knee replacement and 9 cadavers of same age group (50-80years) (control) were processed and studied under electron microscope. The ultrastructure of the cartilage from the two groups was compared with each other. Results Under the electron microscope, articular cartilage from control group had chondrocytes having a secretary cell characteristic with prominent nucleus and well developed organelles. In osteoarthritic cartilage, degenerating or necrotic chondrocytes were found. Nuclei of these chondrocytes appeared lobulated or indented. Chondrocytes below the fibrillated surface had dilated and irregular endoplasmic reticulum. Electron dense lipid deposits in the extracelluar matrix as well as intracytoplasmic glycogen deposits were much increased in osteoarthritic cartilage as compared to the control group. Amount of perinuclear intracytoplasmic fine filaments was also increased in the chondrocytes of osteoarthritic cartilage. Conclusion Ultrastructural findings of the osteoarthritic articular cartilage were much different from the ageing non-osteoarthritic cartilage. Hence, OA should be considered a specific process and not simply an inevitable feature of ageing. DOI: http://dx.doi.org/10.3126/kumj.v11i3.12507 Kathmandu Univ Med J 2013; 43(3):221-225

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