Collagen type III deficiency in patients with rupture of intracranial saccular aneurysms

1987 ◽  
Vol 67 (5) ◽  
pp. 690-696 ◽  
Author(s):  
John R. Østergaard ◽  
Hans Oxlund
Keyword(s):  
Brachial Artery ◽  
Collagen Type ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Biomechanical Properties ◽  
Control Group ◽  
Type I ◽  
Collagen Type Iii ◽  
Type Iii ◽  
Saccular Aneurysms

✓ Samples of the middle cerebral artery (MCA) and the brachial artery were obtained post mortem from 14 patients who died following rupture of intracranial saccular aneurysms and from a control group of 14 age- and sex-matched patients who died of causes unrelated to aneurysm rupture. The biomechanical properties of ring-shaped arterial specimens were investigated by loading the specimens at a constant deformation rate until rupture. The relative amounts of collagen type I and type III were determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) studies of cyanogen bromide peptides of collagen prepared from the arterial samples. A deficiency of collagen type III was demonstrated in specimens of the MCA in six of 14 patients with a ruptured intracranial saccular aneurysm. This deficiency was not accompanied by alterations in the mechanical arterial strength but resulted in a significant increase in the extensibility at stress values corresponding to blood pressures between 100 and 200 mm Hg. No difference was found between aneurysm patients and the control group in regard to the biomechanical properties of the brachial artery, despite the presence of a significant deficiency of collagen type III. The increase in vascular extensibility of the MCA may represent alterations in the fibrous structure and functional integrity of the cerebral arteries of aneurysm patients with collagen type III deficiency. Together with aggravating hemodynamic stresses, this deficiency may be an important factor in the pathogenesis of saccular aneurysms.

Alteration of the collagen type III/type I ratio and intracranial saccular aneurysms in GH-secreting hypophyseal adenomas

1988 ◽  
Vol 9 (4) ◽  
pp. 365-368 ◽  
Author(s):  
M. Acqui ◽  
L. Ferrante ◽  
L. Matronardi ◽  
R. d'Addetta
Keyword(s):  
Collagen Type ◽  
Type I ◽  
Collagen Type Iii ◽  
Type Iii ◽  
Saccular Aneurysms

scholarly journals In Situ Cytokine Expression and Morphometric Evaluation of Total Collagen and Collagens Type I and Type III in Keloid Scars

2017 ◽  
Vol 2017 ◽  
pp. 1-11 ◽  
Author(s):  
Isabela Rios da Silva ◽  
Luciana Colombo Rodrigues da Cunha Tiveron ◽  
Marcos Vinicius da Silva ◽  
Alberto Borges Peixoto ◽  
Carla Aparecida Xavier Carneiro ◽  
...  
Keyword(s):  
Statistical Difference ◽  
Collagen Type ◽  
Control Group ◽  
Type Iii Collagen ◽  
Type I ◽  
Collagen Type Iii ◽  
Type Iii ◽  
Total Collagen ◽  
Initial Injury

Keloids are characterized by excessive collagen deposition and growth beyond the edges of the initial injury, and cytokines may be related to their formation. The objective of this study was to evaluate the collagen fibers, analyze in situ expression of cytokines in keloid lesions, and compare to the control group. Results showed that there was a predominance of women and nonwhite and direct black ancestry. Keloid showed a significant increase in total and type III collagen. Significantly, the expression of mRNA for TGF-βin keloid was increased, the expressions of IFN-γ, IFN-γR1, and IL-10 were lower, and IFN-γR1 and TNF-αhad no statistical difference. Correlations between collagen type III and TGF-βmRNA expression were positive and significant, IFN-γ, IFN-γR1, and IL-10 were negative and significant, and TNF-αshowed no statistical difference. We conclude that there was a significant increase of total collagen in keloid and predominance of collagen type III compared to the controls, showing keloid as an immature lesion. There is a significant increase in TGF-βmRNA in keloid lesions, and a significant decrease in IFN-γand IL-10, suggesting that these cytokines are related to keloid lesions.

Demonstration by Immunofluorescence That Host Collagen Replaces Dermal Microimplants of Bovine Collagen

1987 ◽  
Vol 4 (1) ◽  
pp. 15-19 ◽  
Author(s):  
Karen E. Burke ◽  
Gail Naughton
Keyword(s):  
Host Response ◽  
Collagen Type ◽  
Type I ◽  
Collagen Type Iii ◽  
Type Iii ◽  
Bovine Collagen ◽  
Collagen Implant ◽  
Human Dermis ◽  
Dermal Collagen ◽  
Human Collagen

It has previously been demonstrated with sequential biopsies analyzed by standard histological stains, immunofluorescence, and electron microscopy that an injectable form of type I bovine dermal collagen (Zyderm® Collagen Implant, or ZCI) in the human dermis stimulates a host response. This host response results in implant degradation and replacement by newly generated host collagen. However, definitive proof that the human collagen is deposited directly on the bovine collagen implants is lacking. This study reports for the first time simultaneous labeling of the ZCI with fluorescein and the host collagen type III with rhodamine. These experiments show that human collagen type III is synthesized directly on the bovine collagen implants.

Immunolocalization of collagen types I and III, tenascin, and fibronectin in intramembranous bone.

1991 ◽  
Vol 39 (5) ◽  
pp. 599-606 ◽  
Author(s):  
D H Carter ◽  
P Sloan ◽  
J E Aaron
Keyword(s):  
Collagen Type ◽  
Bone Matrix ◽  
Bone Modeling ◽  
Type I ◽  
Collagen Type Iii ◽  
Fibrous Stroma ◽  
Marrow Cavity ◽  
Type Iii ◽  
Intramembranous Bone ◽  
Mineralized Matrix

Structural components of the organic bone matrix were located by immunohistochemical techniques in fresh-frozen sections of normal and dysplastic bone. Fine and coarse birefringent fibers were identified as separate and distinctive features in the extracellular matrix by antibodies raised against human collagen Type III. The glycoprotein tenascin was located on a proportion of the fibers in a characteristic beaded pattern, which was absent in dysplastic bone. The fibers originated in the periosteum or in the fibrous stroma of the marrow cavity and were oriented with regard to both the spatial and the lamellar organization of the bone. The disposition and composition of the fibers suggests that they form a preliminary framework on which intramembranous bone modeling proceeds, and that the specific location of tenascin on the fibers in normal developing membrane bone may be important in determining the alignment of the bone tissue. Epitopes recognized by the collagen Type I and fibronectin antibodies were demonstrated throughout the mineralized matrix, but their incorporation into the collagen "Type III" fibers was evident only outside the mineralized matrix.

scholarly journals Effect of acute resistance exercise and sex on human patellar tendon structural and regulatory mRNA expression

2009 ◽  
Vol 106 (2) ◽  
pp. 468-475 ◽  
Author(s):  
Bridget E. Sullivan ◽  
Chad C. Carroll ◽  
Bozena Jemiolo ◽  
Scott W. Trappe ◽  
S. Peter Magnusson ◽  
...  
Keyword(s):  
Resistance Exercise ◽  
Mrna Expression ◽  
Patellar Tendon ◽  
Type I Collagen ◽  
Collagen Type ◽  
Collagen Type I ◽  
Tissue Inhibitors Of Metalloproteinases ◽  
Type I ◽  
Collagen Type Iii ◽  
Type Iii

Tendon is mainly composed of collagen and an aqueous matrix of proteoglycans that are regulated by enzymes called matrix metalloproteinases (MMPs) and tissue inhibitors of metalloproteinases (TIMPs). Although it is known that resistance exercise (RE) and sex influence tendon metabolism and mechanical properties, it is uncertain what structural and regulatory components contribute to these responses. We measured the mRNA expression of tendon's main fibrillar collagens (type I and type III) and the main proteoglycans (decorin, biglycan, fibromodulin, and versican) and the regulatory enzymes MMP-2, MMP-9, MMP-3, and TIMP-1 at rest and after RE. Patellar tendon biopsy samples were taken from six individuals (3 men and 3 women) before and 4 h after a bout of RE and from a another six individuals (3 men and 3 women) before and 24 h after RE. Resting mRNA expression was used for sex comparisons (6 men and 6 women). Collagen type I, collagen type III, and MMP-2 were downregulated ( P < 0.05) 4 h after RE but were unchanged ( P > 0.05) 24 h after RE. All other genes remained unchanged ( P > 0.05) after RE. Women had higher resting mRNA expression ( P < 0.05) of collagen type III and a trend ( P = 0.08) toward lower resting expression of MMP-3 than men. All other genes were not influenced ( P > 0.05) by sex. Acute RE appears to stimulate a change in collagen type I, collagen type III, and MMP-2 gene regulation in the human patellar tendon. Sex influences the structural and regulatory mRNA expression of tendon.

scholarly journals Connective tissue, glial and neuronal expressions in testis of the African giant rat (Cricetomys gambianus)

2017 ◽  
Vol 34 (03) ◽  
pp. 186-193
Author(s):  
T. Falade ◽  
M. Olude ◽  
O. Mustapha ◽  
E. Mbajiorgu ◽  
A. Ihunwo ◽  
...  
Keyword(s):  
Connective Tissue ◽  
Type I Collagen ◽  
Collagen Type ◽  
Neuronal Cells ◽  
Collagen Type I ◽  
Type I ◽  
Collagen Type Iii ◽  
Neuronal Markers ◽  
Type Iii ◽  
African Giant Rat

Abstract Introduction: This study was carried out to investigate the expression of connective tissue (Collagens I and III), glia and neuronal markers in the testis of the African giant rat using histology and immunohistochemistry techniques. Materials and Methods: Eight (8) apparently healthy wild male African giant rats were used for this experiment, divided into 2 groups (juvenile and adult) of 4 animals each. The testes were harvested following intracardial perfusion of the rats and histology was performed using Haematoxylin-Eosin stain and Mallory-Heideinhain rapid one- step staining for connective tissue. Immunohistochemical identification was achieved using the following antibodies: anti-collagen type I, anti-collagen type III, anti-glial fibrillary acidic protein and anti-p75 nerve growth factor for the expression of collagen type I, collagen type III, astrocyte-like cell and neuronal cells respectively. Photomicrography was achieved using Axioskop® microscope and quantitative data were analyzed using student t-test. Results: The cyto-architecture of the testis was typical in the African giant rat. The connective tissue expressed in the juvenile and adult group, signaling of glial-like cells were seen in the perivascular region across the experimental groups. Immuno-localization of neuronal cells were seen in the interstitial spaces across all the groups, but with more expressions in the juvenile. Conclusion: This work has provided a clear description of the expression of connective tissue, neuronal and glial cells in the testis of the African giant rat and their possible relationships across juvenile and adult groups.

Enhancement by Heparin of Affinity between Cold-Insoluble Globulin and Native Collagen Type III

1979 ◽  
Author(s):  
H. Hörmann ◽  
F. Jilek
Keyword(s):  
Collagen Type ◽  
Weight Ratio ◽  
Collagen Type I ◽  
Type I ◽  
Collagen Type Iii ◽  
Type Iii ◽  
Soluble Collagen ◽  
Native Collagen ◽  
Collagen Molecules ◽  
Cold Insoluble Globulin

Affinity between collagen and cold-insoluble globulin was measured by complexing soluble 125-J labelled collagen preparations with the globulin. Precipitates containing considerable activity were formed at 4°C and 22°C by denatured soluble collagen, type I and type III, but only little by native soluble collagen. The precipitation of native collagen, type III, by cold-insoluble globulin was enhanced by heparin. Under optimal conditions at a weight ratio or heparin and cold-insoluble globulin of about 1:1 up to 60% of the collagen applied was insolubilized. Native collagen, type I, was complexed far less effectively even in presence of heparin. Electronmicroscopic and precipitation experiments using 125-J labelled cold-insoluble globulin indicated that heparin might induce a partial conversion of cold-insoluble globulin to a fibrillar derivative which exhibited improved binding properties for the rod-like native collagen molecules. – Supported by Deutsche Forschungsgemeinschaft, Project Ho 740/1.

scholarly journals Immunohistochemical distribution of collagens types IV, V, and VI and of pro-collagens types I and III in human alveolar bone and dentine.

1986 ◽  
Vol 34 (11) ◽  
pp. 1417-1429 ◽  
Author(s):  
J Becker ◽  
D Schuppan ◽  
H Benzian ◽  
T Bals ◽  
E G Hahn ◽  
...  
Keyword(s):  
Type I Collagen ◽  
Collagen Type ◽  
Alveolar Bone ◽  
Organic Matrix ◽  
Collagen Type I ◽  
Basement Membranes ◽  
Type I ◽  
Collagen Type Iii ◽  
Type Iii ◽  
Hard Tissues

The aim of the present study was to characterize the composition of the organic matrix in alveolar jaw bone and dentine using antibodies against pro-collagens Types I and III and collagens Types IV, V, and VI. After demineralization of oral hard tissues in 0.2 N HCl, antigenicity was well preserved and the distribution of the pro-collagens and collagens could be demonstrated. Staining for pro-collagen Type I was prominent around osteoblasts and in pre-dentine, indicating active de novo synthesis of Type I pro-collagen. Pro-collagen Type I was ubiquitous but was less abundant in bone and dentine, whereas pro-collagen Type III was seen only in areas of bone remodeling, in peritubular spaces, and in pre-dentine. Type IV collagen was limited to the basement membranes of vessels in osteons and bone marrow. Type V collagen was detected neither in pre-dentine nor in bone. In contrast, Type VI collagen was found in dentine and bone, showing a faint but homogeneous staining which, similarly to pro-collagen Type III, was pronounced around osteoblasts and in pre-dentine, areas of active bone and dentine formation. This study showed that the organic matrix of dentine and bone contains Type VI as well as Type I collagen. Pro-collagen Type III (and to a lesser extent collagen Type VI) is transiently produced during new formation and remodeling of oral hard tissues, and disappears once the matrix calcifies. Type I pro-collagen qualifies as a general marker protein for increased osteoblastic activity. We conclude that immunostaining for the different collagen/pro-collagen types can be used to assess normal or abnormal stages of bone/dentine formation.

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