Collagen Types I, III and IV in the Placentome and Interplacentomal Maternal and Fetal Tissues in Normal Cows and in Cattle with Retention of Fetal Membranes

2003 ◽  
Vol 174 (4) ◽  
pp. 170-183 ◽  
Author(s):  
A. Boos ◽  
A. Stelljes ◽  
J. Kohtes
Keyword(s):  
Fetal Membranes ◽  
Collagen Types ◽  
Fetal Tissues

Collagen in the fetal membranes of sheep: changes throughout gestation and effects of dexamethasone at 60 days

1997 ◽  
Vol 9 (4) ◽  
pp. 455 ◽  
Author(s):  
Lynne Shandley ◽  
Karen M. Moritz ◽  
Chrishan S. Samuel ◽  
E. Marelyn Wintour
Keyword(s):  
Gel Electrophoresis ◽  
Normal Development ◽  
Allantoic Fluid ◽  
Dry Weight ◽  
Collagen Content ◽  
Fetal Membranes ◽  
Dexamethasone Treatment ◽  
Collagen Types ◽  
Volume Changes ◽  
Volume Increase

The tensile strength of fetal membranes is largely due to their collagen content. In this study we have examined the changes in collagen in the amniotic and allantoic membranes of the sheep over a wide gestational range (27–142 days of gestation; term, 145–150 days). The results have been correlated with volume changes in normal development, and in particular, the changes in allantois have been studied after a rapid and extensive increase in allantoic volume, as a result of maternal dexamethasone treatment (0·76 mg h-1 for 48 h) from Day 60 of gestation. Electron microscopy and immunohistochemistry were used to delineate collagen distribution, and gel electrophoresis was used to assess the relative proportions of each type. In the amnion, collagen content increased from 37±4% to 50±1% dry weight of the tissue from 41–102 days and declined slightly thereafter. In the allantois, collagen content increased from 20±1% at Day 27 to 50±6% at Day 142, significantly correlated with a volume increase from 253 mL to 813±274 mL. Collagen types I (>85%), III (10%) and small amounts of types IV and V (<5%) were identified in both membranes at all ages. When allantoic fluid volume was increased rapidly by maternal dexamethasone infusion, there was a significant decrease in collagen content from 38±6% to 25±2% (P < 0·05). By immunohistochemistry it was observed that both epithelial cells and fibroblasts were synthesizing collagen.

scholarly journals The mRNAs for the three chains of human collagen type XI are widely distributed but not necessarily co-expressed: implications for homotrimeric, heterotrimeric and heterotypic collagen molecules

1995 ◽  
Vol 311 (2) ◽  
pp. 511-516 ◽  
Author(s):  
V C H Lui ◽  
R Y C Kong ◽  
J Nicholls ◽  
A N Y Cheung ◽  
K S E Cheah
Keyword(s):  
Collagen Type ◽  
Subunit Composition ◽  
Messenger Rnas ◽  
Collagen Types ◽  
Fetal Tissues ◽  
Chain Composition ◽  
Collagen Molecules ◽  
Human Collagen ◽  
Human Fetal Tissues ◽  
Cross Type

In cartilage collagen type XI exists as heterotrimeric molecules composed of alpha 1(XI), alpha 2(XI) and alpha 3(XI) subunits. Messenger RNAs for some of the alpha chains of collagen type XI have also been found in non-chondrogenic tissues but the chain composition of the molecule in these sites is not known. Some non-chondrogenic tissues also contain heterotrimers containing collagen alpha 2(V) and alpha 1(XI) chains. We have explored the possibility that collagen type XI could exist in differing trimeric forms in non-chondrogenic tissues and aimed to predict the subunit composition of this collagen in those tissues. The distribution and relative levels of expression of collagen alpha 1(XI), alpha 2(XI) and alpha 3(XI)/alpha 1(II) mRNAs in different human fetal tissues were studied. Expression of mRNAs for all three genes of collagen type XI is not restricted to cartilage but is widespread. However, in some non-chondrogenic tissues, the mRNAs for all three alpha chains of collagen type XI were not co-expressed, but collagen alpha 1(XI) and alpha 2(XI) mRNAs were found either singly or without collagen alpha 3(XI) transcripts. Collagen type XI may therefore exist as homotrimers and/or heterotrimers composed of two collagen alpha(XI) chains in some tissues. The distribution of mRNAs for collagen alpha 2(V) and alpha 1(I) were also studied. Co-expression of collagen type XI, alpha 2(V) and alpha 1(I) mRNAs was found for many tissues. These findings have implications for the possibility of additional chain associations for collagen types XI and V in cross-type heterotrimers within heterotypic fibrils.

scholarly journals Expression of mRNAs coding for the alpha 1 chain of type XIII collagen in human fetal tissues: comparison with expression of mRNAs for collagen types I, II, and III.

1989 ◽  
Vol 109 (3) ◽  
pp. 1371-1379 ◽  
Author(s):  
M Sandberg ◽  
M Tamminen ◽  
H Hirvonen ◽  
E Vuorio ◽  
T Pihlajaniemi
Keyword(s):  
Striated Muscle ◽  
Hybridization Signal ◽  
Northern Hybridization ◽  
Fibrillar Collagen ◽  
Collagen Types ◽  
Root Cells ◽  
Fetal Tissues ◽  
Type Xiii Collagen ◽  
Human Fetal Tissues

This paper describes the topographic distribution of the multiple mRNAs coding for a novel human short-chain collagen, the alpha 1 chain of type XIII collagen. To identify the tissues and cells expressing these mRNAs, human fetal tissues of 15-19 gestational wk were studied by Northern and in situ hybridizations. The distribution pattern of the type XIII collagen mRNAs was compared with that of fibrillar collagen types I, II, and III using specific human cDNA probes for each collagen type. Northern hybridization showed the bone, cartilage, intestine, skin, and striated muscle to contain mRNAs for type XIII collagen. An intense in situ hybridization signal was obtained with the type XIII collagen cDNAs in the epidermis, hair follicles, and nail root cells of the skin, whereas the fibrillar collagen mRNAs were detected in the dermis. Cells in the intestinal mucosal layer also appeared to contain high levels of alpha 1(XIII) collagen mRNAs, but contained none of the fibrillar collagen mRNAs. In the bone and striated muscle, alpha 1(XIII) collagen mRNAs were detected in the mesenchymal cells forming the reticulin fibers of the bone marrow and endomycium. The hybridization signal obtained with the alpha 1(XIII) collagen cDNA probe in cartilaginous areas of the growth plates was similar, but less intense, to that obtained with the type II collagen probe. A clear hybridization signal was also detected at the (pre)articular surfaces and at the margins of the epiphyses, whereas it was weaker in the resting chondrocytes in the middle of the epiphyses. The brain, heart, kidney, liver, lung, placenta, spleen, testis, tendon, and thymus did not appear to contain alpha 1(XIII) collagen mRNAs.

Evidence of MMP/TIMP imbalance in fetal membranes during infection

1998 ◽  
Vol 5 (1) ◽  
pp. 174A-174A
Author(s):  
S FORTUNATO ◽  
R MENON ◽  
S LOMBARDI
Keyword(s):  
Fetal Membranes

Interventional Thermal Injury of the Arterial Wall: Unfolding of von Willebrand Factor and Its Increased Binding to Collagen after 55° C Heating

1996 ◽  
Vol 75 (03) ◽  
pp. 515-519 ◽  
Author(s):  
Mark J Post ◽  
Anke N de Graaf-Bos ◽  
George Posthuma ◽  
Philip G de Groot ◽  
Jan J Sixma ◽  
...  
Keyword(s):  
Von Willebrand Factor ◽  
Conformational Changes ◽  
Arterial Wall ◽  
Platelet Adhesion ◽  
Type I ◽  
Temperature Dependent ◽  
Collagen Types ◽  
Electron Microscopic ◽  
Von Willebrand ◽  
Willebrand Factor

Summary Purpose. Thermal angioplasty alters the thrombogenicity of the arterial wall. In previous studies, platelet adhesion was found to increase after heating human subendothelium to 55° C and decrease after heating to 90° C. In the present electron microscopic study, the mechanism of this temperature-dependent platelet adhesion to the heated arterial wall is elucidated by investigating temperature-dependent conformational changes of von Willebrand factor (vWF) and collagen types I and III and the binding of vWF to heated collagen. Methods. Purified vWF and/or collagen was applied to electron microscopic grids and heated by floating on a salt-solution of 37° C, 55° C or 90° C for 15 s. After incubation with a polyclonal antibody against vWF and incubation with protein A/gold, the grids were examined by electron microscopy. Results. At 37° C, vWF was coiled. At 55° C, vWF unfolded, whereas heating at 90° C caused a reduction in antigenicity. Collagen fibers heated to 37° C were 60.3 ± 3.1 nm wide. Heating to 55° C resulted in the unwinding of the fibers, increasing the width to 87.5 ± 8.2 nm (p < 0.01). Heating to 90° C resulted in denatured fibers with an enlarged width of 85.1 ± 6.1 nm (p < 0.05). Heating of collagen to 55° C resulted in an increased vWF binding as compared to collagen heated to 37° C or to 90° C. Incubation of collagen with vWF, prior to heating, resulted in a vWF binding after heating to 55° C that was similar to the 37° C binding and a decreased binding after 90° C. Conclusions. After 55° C heating, the von Willebrand factor molecule unfolds and collagen types I and III exhibit an increased adhesiveness for von Willebrand factor. Heating to 90° C denatures von Willebrand factor and collagen. The conformation changes of von Willebrand factor and its altered binding to collagen type I and III may explain the increased and decreased platelet adhesion to subendothelium after 55° C and 90° C heating, respectively.

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