The extracellular matrix proteins type I collagen, type III collagen, fibronectin, and laminin 421 stimulate migration of cancer cells

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.

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

Journal of Morphological Sciences ◽

10.4322/jms.109117 ◽

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.

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

Journal of Histochemistry & Cytochemistry ◽

10.1177/34.11.3772076 ◽

1986 ◽

Vol 34 (11) ◽

pp. 1417-1429 ◽

Cited By ~ 90

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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Immunolocalization of bone extracellular matrix proteins (type I collagen, osteonectin and bone sialoprotein) in human dental pulp and cultured pulp cells

International Endodontic Journal ◽

10.1046/j.1365-2591.2003.00669.x ◽

2003 ◽

Vol 36 (6) ◽

pp. 404-410 ◽

Cited By ~ 28

Author(s):

J. M. Q. Garcia ◽

M. D. Martins ◽

R. G. Jaeger ◽

M. M. Marques

Keyword(s):

Extracellular Matrix ◽

Dental Pulp ◽

Type I Collagen ◽

Extracellular Matrix Proteins ◽

Bone Sialoprotein ◽

Matrix Proteins ◽

Type I ◽

Human Dental Pulp ◽

Pulp Cells

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Distribution of endogenous (β-galactoside-specific lectin, fibronectin and type I and III collagens during dermal condensation in chick embryos

Development ◽

10.1242/dev.65.1.41 ◽

1981 ◽

Vol 65 (1) ◽

pp. 41-56

Author(s):

Kunio Kitamura

Keyword(s):

Type I Collagen ◽

Collagen Type ◽

Distribution Patterns ◽

Type Iii Collagen ◽

Type I ◽

Dorsal Skin ◽

Collagen Type Iii ◽

Immunofluorescence Method ◽

Dermal Cells ◽

Fibronectin Type

The distribution of endogenous β-galactoside-specific lectin, fibronectin, type I and III collagens was studied by the indirect immunofluorescence method during the formation of dermal condensation in the feathered region (dorsal skin) of a chick embryo. Endogenous β-galactoside specific lectin was concentrated in the condensed dermal region, coinciding with the formation of condensation of dermal cells. It was also detected in epidermal placodes. Fibronectin was weakly stained in dermis prior to the formation of dermal condensation but not in epidermis. Condensation of dermal cells resulted in the formation of thicker fibrils of fibronectin in the condensed region. Distribution of type I collagen was found to be very different from that of endogenous β-galactoside-specific lectin and fibronectin. Type I collagen in dermis decreased along with the formation of dermal condensation. Epidermis had no type I collagen. Type III collagen was not found in dorsal skin. Relationship found between these distribution patterns and dermal condensation in the embryonicchick skin is discussed.

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

Mediators of Inflammation ◽

10.1155/2017/6573802 ◽

2017 ◽

Vol 2017 ◽

pp. 1-11 ◽

Cited By ~ 8

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.

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