Changes of Biochemical and Biomechanical Properties in Dupuytren Disease

2000 ◽  
Vol 124 (9) ◽  
pp. 1275-1281
Author(s):  
Mahmoud Melling ◽  
Daniela Karimian-Teherani ◽  
Sascha Mostler ◽  
Mark Behnam ◽  
Grazyna Sobal ◽  
...  
Keyword(s):  
Structural Changes ◽  
Clinical Stage ◽  
Young Modulus ◽  
Biomechanical Properties ◽  
Collagen Content ◽  
Type Iii Collagen ◽  
Biophysical Properties ◽  
Type Iii ◽  
Palmar Aponeurosis ◽  
Dupuytren Disease

Abstract Background.—The major biochemical characteristic of Dupuytren disease is the progressive and irreversible deposition of excess fibrous collagen characterized by an enhanced type III collagen proportion. Objective.—To investigate the influence of changes of the collagen spectrum on the biophysical properties of the palmar aponeurosis. Design.—Variably affected palmar regions from 30 individuals with Dupuytren disease were classified according to histologic test results and clinical stage. Biochemical, biomechanical, and thermal contracture studies were performed. Results.—The relative type III collagen content increased with increasing tissue involvement and was found to correlate with calorimetric and biomechanical properties with the exception of the Young modulus. In experiments on the thermal isometric contracture, the collagen denaturation temperature decreased with increasing type III collagen content, ie, increasing involvement. To study the dependence of biophysical properties from the collagen type distribution independent of structural changes, as seen in Dupuytren disease, we investigated rat skins from animals of an age range characterized by dramatic changes in type III collagen content (0–18 months). Biomechanical data also correlated significantly with type III collagen content in rat skin with the exception of the time constant of stress relaxation. Conclusion.—In light of these results, we suggest that structural changes, such as reduced collagen fibril diameters, associated with alterations in the type III collagen proportion may influence biophysical properties of connective tissues in the involved palmar aponeurosis in addition to alterations of the cross-linking pattern.

Type I and Type III Collagen Content of Healing Wounds in Fetal and Adult Rats

1988 ◽  
Vol 187 (4) ◽  
pp. 493-497 ◽  
Author(s):  
J. R. Merkel ◽  
B. R. DiPaolo ◽  
G. G. Hallock ◽  
D. C. Rice
Keyword(s):  
Collagen Content ◽  
Type Iii Collagen ◽  
Type I ◽  
Adult Rats ◽  
Type Iii ◽  
Healing Wounds

Immunohistochemical Analysis of Type III and IV Collagens in Tubulointerstitial Damage in Human Benign Nephrosclerosis

1995 ◽  
Vol 23 (6) ◽  
pp. 480-486 ◽  
Author(s):  
M S Razzaque ◽  
M Cheng ◽  
Y Horita ◽  
M Nishihara ◽  
T Harada ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Basement Membrane ◽  
Structural Changes ◽  
Immunohistochemical Analysis ◽  
Type Iii Collagen ◽  
Type Iii ◽  
Type Iv ◽  
Tubulointerstitial Damage ◽  
Basement Membrane Collagen ◽  
Immunohistochemical Techniques

Prolonged hypertension causes structural changes including glomerulosclerosis and tubulointerstitial damage of the kidney, termed benign nephrosclerosis. It is generally accepted that, in benign nephrosclerosis, increased accumulation of extracellular matrix in the glomeruli results in glomerulosclerosis. Little is known, however, about the possible role of the extracellular matrix in the tubulointerstitial damage in benign nephrosclerosis. In this study, the possible roles of type IV basement-membrane collagen and type III interstitial collagen in tubulointerstitial damage caused by hypertension were explored. Immunohistochemical techniques were used to investigate the distribution of type III and type IV collagens in the kidney sections of 15 patients with benign nephrosclerosis with tubulointerstitial damage and in 10 controls. In the control renal sections strong immunostaining for type III collagen was found in the interstitium and immunostaining for type IV collagen was present in the tubular basement membrane and weakly in the interstitium. In the patients with tubulointerstitial damage there was increased immunostaining for both type III and type IV collagens in the expanded interstitium and damaged tubules than was found in the control kidney sections. These findings indicate that increased accumulation of both type III and type IV collagens might play a significant role in the tubulointerstitial damage in benign nephrosclerosis.

scholarly journals Immunohistochemical analysis of collagen content and types in the rectus abdominis muscle of cadavers of different ages

2011 ◽  
Vol 26 (suppl 2) ◽  
pp. 3-7 ◽  
Author(s):  
Eliziane Nitz de Carvalho Calvi ◽  
Fábio Xerfan Nahas ◽  
Marcus Vinícius Jardini Barbosa ◽  
Silvia Saiuli Miki Ihara ◽  
José Augusto Calil ◽  
...  
Keyword(s):  
Rectus Sheath ◽  
Immunohistochemical Analysis ◽  
Rectus Abdominis ◽  
Collagen Content ◽  
Type Iii Collagen ◽  
Type I ◽  
Rectus Abdominis Muscle ◽  
Type Iii ◽  
Different Ages ◽  
Group A

PURPOSE: To assess the collagen content and types in the rectus abdominis muscle of cadavers of different ages. METHODS: Forty fresh adult male cadavers, at room temperature, were obtained from the Institute of Legal Medicine of Franca and dissected within 24 hours of death. The cadavers were divided into two groups: Group A (n=20), 18 to 30 years of age, and Group B (n=20), 31 to 60 years of age. Bilateral incisions were made in the middle portion of anterior rectus sheath 3 cm superiorly and 2 cm inferiorly to the umbilicus and four fragments of the rectus abdominis muscle were dissected. The samples were fixed in 10% buffered formalin and sent for immunohistochemical analysis to determine collagen content and types. RESULTS: Immunohistochemical results revealed higher amounts of type I and type III collagen in Group A. However, no difference in the amount of type IV collagen was found between the groups. CONCLUSION: The amount of type I and type III collagen was higher in group A.

Changes in the biomechanical properties of skin and aorta induced by corticotrophin treatment

1980 ◽  
Vol 94 (1) ◽  
pp. 132-137 ◽  
Author(s):  
H. Oxlund
Keyword(s):  
Mechanical Properties ◽  
Tensile Strength ◽  
Connective Tissue ◽  
Thoracic Aorta ◽  
Aortic Wall ◽  
Biomechanical Properties ◽  
Elastic Stiffness ◽  
Collagen Content ◽  
Dorsal Skin ◽  
Biophysical Properties

Abstract. The work presented here is an investigation of the effect of elevated levels of corticosteroids on the biophysical properties of skin, aorta and muscle tendon. Rats were given corticotrophin injections for 10, 30 and 60 days to elevate the level of plasma endogenous corticosteroids. The corticotrophin treatments did not change the water or collagen content of specimens from dorsal skin, thoracic aorta and peroneal muscle tendons, tested mechanically. Changes became evident after longer treatment times. For both skin and aorta, the tensile strength, elastic stiffness and failure energy were increased after 60 days of treatment. The corticotrophin treatment did not influence the mechanical properties of muscle tendons. Complete reversibility of changes in the mechanical properties induced by 30 days of corticotrophin treatment was found after an additional period of 30 days of saline injections. This study indicates that an increased level of plasma corticosteroids elicited by corticotrophin treatment may increase the stiffness of the connective tissue of the organism. In the aorta this results in loss of capacitive function with increased haemodynamic strain on the aortic wall.

Methionine-Specific Staining of Collagen

1982 ◽  
Vol 40 ◽  
pp. 294-295
Author(s):  
E.M. Kuhn ◽  
K.D. Marenus ◽  
M. Beer
Keyword(s):  
Amino Acids ◽  
Collagen Fibers ◽  
Type Iii Collagen ◽  
Type I ◽  
Electron Microscopic ◽  
Good Correspondence ◽  
Specific Staining ◽  
Type Iii ◽  
Different Types ◽  
Sulfur Containing

Fibers composed of different types of collagen cannot be differentiated by conventional electron microscopic stains. We are developing staining procedures aimed at identifying collagen fibers of different types.Pt(Gly-L-Met)Cl binds specifically to sulfur-containing amino acids. Different collagens have methionine (met) residues at somewhat different positions. A good correspondence has been reported between known met positions and Pt(GLM) bands in rat Type I SLS (collagen aggregates in which molecules lie adjacent to each other in exact register). We have confirmed this relationship in Type III collagen SLS (Fig. 1).

Structural Insights into the Glycine Pair Motifs in Type III Collagen

2017 ◽  
Vol 3 (3) ◽  
pp. 269-278
Author(s):  
Bo An ◽  
Shu-Wei Chang ◽  
Cody Hoop ◽  
Jean Baum ◽  
Markus J. Buehler ◽  
...  
Keyword(s):  
Type Iii Collagen ◽  
Type Iii ◽  
Structural Insights

scholarly journals Type III Collagen is Required for Adipogenesis and Actin Stress Fibre Formation in 3T3-L1 Preadipocytes

Biomolecules ◽  
2021 ◽  
Vol 11 (2) ◽  
pp. 156
Author(s):  
Mohammad Al Hasan ◽  
Patricia E. Martin ◽  
Xinhua Shu ◽  
Steven Patterson ◽  
Chris Bartholomew
Keyword(s):  
Quantitative Polymerase Chain Reaction ◽  
Type Iii Collagen ◽  
Type Iii ◽  
Actin Stress Fibre ◽  
Matrix Gene ◽  
Gene Transcripts ◽  
Polymerase Chain ◽  
Oil Red O Staining ◽  
Oil Red O

GPR56 is required for the adipogenesis of preadipocytes, and the role of one of its ligands, type III collagen (ColIII), was investigated here. ColIII expression was examined by reverse transcription quantitative polymerase chain reaction, immunoblotting and immunostaining, and its function investigated by knockdown and genome editing in 3T3-L1 cells. Adipogenesis was assessed by oil red O staining of neutral cell lipids and production of established marker and regulator proteins. siRNA-mediated knockdown significantly reduced Col3a1 transcripts, ColIII protein and lipid accumulation in 3T3-L1 differentiating cells. Col3a1−/− 3T3-L1 genome-edited cell lines abolished adipogenesis, demonstrated by a dramatic reduction in adipogenic moderators: Pparγ2 (88%) and C/ebpα (96%) as well as markers aP2 (93%) and oil red O staining (80%). Col3a1−/− 3T3-L1 cells displayed reduced cell adhesion, sustained active β-catenin and deregulation of fibronectin (Fn) and collagen (Col4a1, Col6a1) extracellular matrix gene transcripts. Col3a1−/− 3T3-L1 cells also had dramatically reduced actin stress fibres. We conclude that ColIII is required for 3T3-L1 preadipocyte adipogenesis as well as the formation of actin stress fibres. The phenotype of Col3a1−/− 3T3-L1 cells is very similar to that of Gpr56−/− 3T3-L1 cells, suggesting a functional relationship between ColIII and Gpr56 in preadipocytes.

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