scholarly journals Polymerized Type I Collagen Reverts Airway Hyperresponsiveness and Fibrosis in a Guinea Pig Asthma Model

10.5772/25563 ◽  
2012 ◽  
Author(s):  
Blanca Bazn-Perkins ◽  
Maria G. ◽  
Edgar Snchez-Guerrero
Keyword(s):  
Guinea Pig ◽  
Airway Hyperresponsiveness ◽  
Type I Collagen ◽  
Type I ◽  
Asthma Model

Phospholipase A2 activity is increased in guinea pig uterine cervix in late pregnancy and at parturition

1995 ◽  
Vol 269 (5) ◽  
pp. E940-E947 ◽  
Author(s):  
M. R. Rajabi ◽  
A. V. Cybulsky
Keyword(s):  
Guinea Pig ◽  
Type I Collagen ◽  
Late Pregnancy ◽  
Cervical Dilatation ◽  
Type I ◽  
Pla2 Activity ◽  
Phospholipases A2 ◽  
Rate Limiting Step ◽  
Cytosolic Pla2 ◽  
Rate Limiting

Release of arachidonic acid from phospholipids by phospholipases A2 (PLA2) is the rate-limiting step in prostaglandin (PG) synthesis. PGE2 and PGF2 alpha are essential intermediates in interstitial collagenase-mediated degradation of type I collagen, a key step in cervical dilatation at parturition. We demonstrate that PLA2 is present in cytosolic fractions of guinea pig cervix and PLA2 activity is increased during cervical dilatation at parturition. In the cervix of nonpregnant animals, PLA2 activity against phosphatidylcholine (PC) and phosphatidylethanolamine (PE) was 13 +/- 6 and 49 +/- 27 pmol.min-1.mg protein-1, respectively. Levels were similar at day 25 of pregnancy. At day 50, PLA2-PC increased to 190 +/- 54 pmol.min-1.mg-1, and PLA2-PE rose to 592 +/- 127 pmol.min-1.mg-1. At parturition (68 +/- 2 days) there were further increases of 49-67%. PLA2 activity declined toward basal levels 2 days postpartum. Almost 50% of the enhanced cytosolic PLA2 (cPLA2) activity at day 50 or at parturition was of high molecular mass and was identified as the "85-kDa cPLA2." Increases in cPLA2 activity at these time points were not, however, associated with increases in cPLA2 protein or phosphorylation of cPLA2, compared with nonpregnant animals. This study suggests that multiple PLA2 enzymes, including cPLA2, are involved in cervical dilatation at parturition.

scholarly journals Expression of Wnt/β-Catenin Signaling Pathway and Its Regulatory Role in Type I Collagen with TGF-β1 in Scleral Fibroblasts from an Experimentally Induced Myopia Guinea Pig Model

2016 ◽  
Vol 2016 ◽  
pp. 1-10 ◽  
Author(s):  
Min Li ◽  
Ying Yuan ◽  
Qingzhong Chen ◽  
Rao Me ◽  
Qing Gu ◽  
...  
Keyword(s):  
Guinea Pig ◽  
Signaling Pathway ◽  
Type I Collagen ◽  
Intervention Group ◽  
Neutralizing Antibody ◽  
Self Control ◽  
Pig Model ◽  
Type I ◽  
Pathway Expression ◽  
Guinea Pig Model

Background. To investigate Wnt/β-catenin signaling pathway expression and its regulation of type I collagen by TGF-β1 in scleral fibroblasts from form-deprivation myopia (FDM) guinea pig model.Methods. Wnt isoforms were examined using genome microarrays. Scleral fibroblasts from FDM group and self-control (SC) group were cultured. Wnt isoforms,β-catenin, TGF-β1, and type I collagen expression levels were examined in the two groups with or without DKK-1 or TGF-β1 neutralizing antibody.Results. For genome microarrays, the expression of Wnt3 in FDM group was significantly greater as confirmed in retinal and scleral tissue. The expression of Wnt3 andβ-catenin significantly increased in FDM group and decreased significantly with DKK-1. TGF-β1 expression level decreased significantly in FDM group and increased significantly with DKK-1. Along with morphological misalignment inside and outside cells, the amount of type I collagen decreased in FDM group. Furthermore, type I collagen increased and became regular in DKK-1 intervention group, whereas it decreased and rearranged more disorder in TGF-β1 neutralizing antibody intervention group.Conclusions. The activation of Wnt3/β-catenin signaling pathway was demonstrated in primary scleral fibroblasts in FDM. This pathway further reduced the expression of type I collagen by TGF-β1, which ultimately played a role in scleral remodeling during myopia development.

Aerosolized Polymerized Type I Collagen Reduces Airway Inflammation and Remodelling in a Guinea Pig Model of Allergic Asthma

Lung ◽  
2009 ◽  
Vol 188 (2) ◽  
pp. 97-105 ◽  
Author(s):  
Paola Moreno-Alvarez ◽  
Edgar Sánchez-Guerrero ◽  
Erasmo Martínez-Cordero ◽  
Rogelio Hernández-Pando ◽  
María G. Campos ◽  
...  
Keyword(s):  
Guinea Pig ◽  
Airway Inflammation ◽  
Allergic Asthma ◽  
Type I Collagen ◽  
Pig Model ◽  
Type I ◽  
Guinea Pig Model

scholarly journals Antigen-induced airway hyperresponsiveness and obstruction is related to caveolin-1 expression in airway smooth muscle in a guinea pig asthma model

2015 ◽  
Vol 5 (1) ◽  
Author(s):  
Mayra Álvarez-Santos ◽  
Patricia Ramos-Ramírez ◽  
Fernando Gutiérrez-Aguilar ◽  
Sandra Sánchez-Hernández ◽  
Ricardo Lascurain ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Guinea Pig ◽  
Airway Smooth Muscle ◽  
Airway Hyperresponsiveness ◽  
Caveolin 1 ◽  
Asthma Model

Regulation of pancreatic duct epithelial growth in vitro

1990 ◽  
Vol 258 (6) ◽  
pp. G833-G840 ◽  
Author(s):  
T. B. Verme ◽  
S. R. Hootman
Keyword(s):  
Guinea Pig ◽  
Pancreatic Duct ◽  
Type I Collagen ◽  
Basal Medium ◽  
Trophic Factors ◽  
Type I ◽  
Trophic Effect ◽  
Initial Area

Effects of a number of possible trophic factors on growth of guinea pig pancreatic duct epithelial monolayers were investigated. Isolated fragments of main and interlobular ducts were prepared and explanted onto both tissue culture plastic and thick gels of type I collagen. Monolayers growing out from explants were first cultured in a basal medium for 3 or 4 days. Next, the medium was supplemented individually with bombesin, carbachol, caerulein, epidermal growth factor (EGF), secretin, 12-O-tetradecanoylphorbol 13-acetate (TPA), or vasoactive intestinal peptide (VIP). Cells were cultured in the absence or presence of these possible trophic factors, and monolayer areas were determined morphometrically at 0, 2, and 4 days. Rate of growth was determined from increase in area over each 2-day period. Monolayers grown in basal medium alone on plastic increased to 479% of initial area over the 4-day test period; those grown on collagen increased to 523%. Explants cultured in presence of bombesin, carbachol, caerulein, secretin, TPA, and VIP on either substrate grew at rates not significantly different from those cultured in basal medium. By contrast, duct monolayers grown on plastic or collagen in presence of 10 nM EGF expanded in area to 722 and 1,070%, respectively, of their initial areas. The EC50 for this trophic effect was approximately 1 nM. These results show that EGF exerts a potent trophic effect on guinea pig pancreatic duct cells in vitro but also indicate that cell division in the pancreatic main and interlobular ducts is not regulated by caerulein and related peptide hormones that have been reported to have growth-promoting effects on exocrine pancreas in vivo.

Development of an assay for the quantification of type I collagen synthesis in the guinea pig

2005 ◽  
Vol 297 (1-2) ◽  
pp. 133-141 ◽  
Author(s):  
Helen L. Quasnichka ◽  
John F. Tarlton ◽  
Janet M. Anderson-MacKenzie ◽  
Michael E.J. Billingham ◽  
Allen J. Bailey ◽  
...  
Keyword(s):  
Guinea Pig ◽  
Collagen Synthesis ◽  
Type I Collagen ◽  
Type I

scholarly journals Identification of the sites in collagen α-chains that bind serum anti-gelatin factor (cold-insoluble globulin)

1978 ◽  
Vol 169 (1) ◽  
pp. 55-59 ◽  
Author(s):  
W Dessau ◽  
B C Adelmann ◽  
R Timpl
Keyword(s):  
Active Region ◽  
Guinea Pig ◽  
Affinity Chromatography ◽  
Human Serum ◽  
Type I Collagen ◽  
Type I ◽  
Inhibition Assay ◽  
Serum Factor ◽  
Cold Insoluble Globulin

Anti-gelatin factor was prepared from guinea-pig and human serum by affinity chromatography on denatured type-I collagen. As shown previously, this component is related to cold-insoluble globulin. It reacted with 125I-labelled denatured collagen, and the reaction could be inhibited by preincubation with unlabelled collagenous components. In the inhibition assay comparable activities were observed for native and denatured type-I, -II, -III and -IV collagens. There was also no difference in reactivity between collagens of different species. The reactive sites in the collagen alpha-chains were located by inhibition assays on distinct CNBr- and collagenase-derived peptides. The results obtained with fragments from alpha1(I)-, alpha2- and alpha1(II)-chains indicate that the most active region is located between positions 643 and 819 of the alpha1-chain. Lower activities were found for other regions of collagen and may indicate that the factor has the potential to interact with several sites in the alpha-chains. The present data agree with observations by Kleinman, McGoodwin & Klebe [Biochem. Biophys. Res. Commun. (1976) 72, 426-432] on the specificity of a serum factor promoting the attachment of fibroblasts to collagen.

Collagen fibrillogenesis in vitro: interaction of types I and V collagen

1986 ◽  
Vol 44 ◽  
pp. 210-211
Author(s):  
Arthur J. Wasserman ◽  
Kathy C. Kloos ◽  
David E. Birk
Keyword(s):  
Type I Collagen ◽  
Corneal Stroma ◽  
Minor Component ◽  
Homogeneous Distribution ◽  
Type I ◽  
Type V Collagen ◽  
Fibril Morphology ◽  
Type V ◽  
In Vitro Interaction

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.

948: Clinical Safety, Histologic Findings and Surgical Methods in Complex Phalloplasty Using Type I Collagen

2007 ◽  
Vol 177 (4S) ◽  
pp. 314-314 ◽  
Author(s):  
Joon-Yang Kim ◽  
Hoon Seog Jean ◽  
Beom Joon Kim ◽  
Kye Yong Song
Keyword(s):  
Type I Collagen ◽  
Type I ◽  
Clinical Safety ◽  
Surgical Methods
Sign in / Sign up

Export Citation Format

Share Document