Type V collagen-induced upregulation of capn2 (large subunit of m-calpain) gene expression and DNA fragmentation in 8701-BC breast cancer cells

2011 ◽  
Vol 392 (6) ◽  
Author(s):  
Claudio Luparello ◽  
Rosalia Sirchia

Abstract Type V collagen is known to be over-deposited in the stroma of ductal infiltrating carcinomas of the breast. When used as a substrate, type V collagen restrains growth and invasion, and affects gene expression of 8701-BC ductal infiltrating carcinomas cells. Here we supplement existing data by demonstrating type V collagen dependent upregulation of capn2 gene expression in 8701-BC cells through differential display-PCR and Western blot assays. Furthermore, we suggest that our data obtained by centrifugal sedimentation and electrophoresis strongly suggest a correlation between calpain overproduction and DNA fragmentation, since the incubation with calpain inhibitor partly reverts the latter.






2011 ◽  
Vol 52 (5) ◽  
pp. 348-358 ◽  
Author(s):  
Claudio Luparello ◽  
Rosalia Sirchia ◽  
Alessandra Longo


2019 ◽  
Vol 21 (1) ◽  
Author(s):  
Walcy Rosolia Teodoro ◽  
Zelita Aparecida de Jesus Queiroz ◽  
Lais Araujo dos Santos ◽  
Sergio Catanozi ◽  
Antonio dos Santos Filho ◽  
...  

Abstract Background Type V collagen (Col V) has the potential to become an autoantigen and has been associated with the pathogenesis of systemic sclerosis (SSc). We characterized serological, functional, and histopathological features of the skin and lung in a novel SSc murine model induced by Col V immunization. Methods Female C57BL/6 mice (n = 19, IMU-COLV) were subcutaneously immunized with two doses of Col V (125 μg) emulsified in complete Freund adjuvant, followed by two intramuscular boosters. The control group (n = 19) did not receive Col V. After 120 days, we examined the respiratory mechanics, serum autoantibodies, and vascular manifestations of the mice. The skin and lung inflammatory processes and the collagen gene/protein expressions were analyzed. Results Vascular manifestations were characterized by endothelial cell activity and apoptosis, as shown by the increased expression of VEGF, endothelin-1, and caspase-3 in endothelial cells. The IMU-COLV mice presented with increased tissue elastance and a nonspecific interstitial pneumonia (NSIP) histologic pattern in the lung, combined with the thickening of the small and medium intrapulmonary arteries, increased Col V fibers, and increased COL1A1, COL1A2, COL3A1, COL5A1, and COL5A2 gene expression. The skin of the IMU-COLV mice showed thickness, epidermal rectification, decreased papillary dermis, atrophied appendages, and increased collagen, COL5A1, and COL5A2 gene expression. Anti-collagen III and IV and ANA antibodies were detected in the sera of the IMU-COLV mice. Conclusion We demonstrated that cutaneous, vascular, and pulmonary remodeling are mimicked in the Col V-induced SSc mouse model, which thus represents a suitable preclinical model to study the mechanisms and therapeutic approaches for SSc.



10.1186/bcr60 ◽  
2000 ◽  
Vol 2 (3) ◽  
Author(s):  
Ida Pucci-Minafra ◽  
Cintia Carella ◽  
Rosalia Cirincione ◽  
Silvana Chimenti ◽  
Salvatore Minafra ◽  
...  


Author(s):  
Paula Yume S.S. Corrêa ◽  
Edwin R. Parra ◽  
Renata A. Alveno ◽  
Carolina B. Faustino ◽  
Jymenez de Morais de Morais ◽  
...  


Author(s):  
Arthur J. Wasserman ◽  
Kathy C. Kloos ◽  
David E. Birk

Type I collagen is the predominant collagen in the cornea with type V collagen being a quantitatively minor component. However, the content of type V collagen (10-20%) in the cornea is high when compared to other tissues containing predominantly type I collagen. The corneal stroma has a homogeneous distribution of these two collagens, however, immunochemical localization of type V collagen requires the disruption of type I collagen structure. This indicates that these collagens may be arranged as heterpolymeric fibrils. This arrangement may be responsible for the control of fibril diameter necessary for corneal transparency. The purpose of this work is to study the in vitro assembly of collagen type V and to determine whether the interactions of these collagens influence fibril morphology.





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