Collagen type VI expression during cardiac development and in human fetuses with trisomy 21 (original) (raw)
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The biochemical and ultrastructural demonstration of collagen during early heart development
Developmental Biology, 1974
A correlative ultrastructural and biochemical study was made of cardiac collagen in the chick embryo, spanning stages 9-to 11 (6 to 13 somites). Analysis (carboxymethyl cellulose chromatography, SDS acrylamide gel electrophoresis and levels of proline hydroxylation) of collagen synthesized in situ permitted classification of this collagen as type I-like (al :a2 = 2: 1). Correlative electron microscopy of hearts fixed in situ showed the appearance of striated collagen fibrils in the cardiac jelly, thus complementing the biochemical findings. Although the electron microscope showed the presence of developing basal laminae and laminalike material, synthesis of the type of collagen reported as unique to basal laminae was not detected, and we propose that these basal laminae may lack type IV collagen. Embryonic stages 9-to 11 are the earliest stages in which collagen synthesis has been demonstrated, and this is the first report of the occurrence of I _ collagen in cardiac jelly of early hearts.
Type II collagen is transiently expressed during avian cardiac valve morphogenesis
Developmental Dynamics, 1994
We present new evidence of the temporal and spatial expression of type I1 collagen in the embryonic chick heart during the very early stages of its development. In particular, we emphasize the distribution of its mRNA and protein during valve formation. Type I1 collagen as well as several other fibrillar collagens (types I, 111, and V) are present in stage 18 endocardial cushion mesenchymal cells. At stage 23, al(I1) collagen transcripts and the cognate polypeptide colocalize in the atrioventricular valves. As development proceeds, the relative abundance of al(I1) collagen transcripts decreases during the stages studied (stages 22 to 45; day 3.5 to day 19) as assayed by RNA blotting of extracts of whole hearts. Type I1 collagen protein was immunologically undetectable in stage 38 (day 12) hearts, although collagens I, 111, and V persisted and localize in the valve regions, in the endothelial lining of the heart, and in the epicardium. In keeping with other observations of type I1 collagen expression in non-chondrogenic regions of a variety of vertebrate embryos, the avian heart also exhibits transient type I1 collagen expression.
Developmental Dynamics, 2008
Heart valve function is achieved by organization of matrix components including collagens, yet the distribution of collagens in valvular structures is not well defined. Therefore, we examined the temporal and spatial expression of select fibril-, network-, beaded filament-forming, and FACIT collagens in endocardial cushions, remodeling, maturing, and adult murine atrioventricular heart valves. Of the genes examined, col1a1, col2a1, and col3a1 transcripts are most highly expressed in endocardial cushions. Expression of col1a1, col1a2, col2a1, and col3a1 remain high, along with col12a1 in remodeling valves. Maturing neonate valves predominantly express col1a1, col1a2, col3a1, col5a2, col11a1, and col12a1 within defined proximal and distal regions. In adult valves, collagen protein distribution is highly compartmentalized, with ColI and ColXII observed on the ventricular surface and ColIII and ColVa1 detected throughout the leaflets. Together, these expression data identify patterning of collagen types in developing and maintained heart valves, which likely relate to valve structure and function.
Embryogenesis of the rat heart: the expression of collagenases
Basic Research in Cardiology, 2002
Little is known about extracellular matrix (ECM) remodeling during heart development. Matrix degrading metalloproteinases are possible candidates contributing to degradation of ECM during these complex biological events. We described here different forms of MMPs, based on their substrate specificity, molecular weight, immunolocalization and in situ zymography within embryonic rat myocardium at different stages of heart development (from embryonic day -ED12 until ED 21). Murine collagenase-3 (MMP-13), stromelysin (MMP-3) and gelatinases A&B (MMP-2 & -9) were expressed in prenatal hearts, as demonstrated by quantitative zymography and immunohistochemistry. MMP-2, -3 and -9 were found within myocardium of avascular (ED12) and vascularized heart (ED14-21). An extensive immunolabeling over the heart trabeculae, epicardial tissue and a weaker labeling in the endocardial and truncoconal cushion tissue was observed at all stages of the heart development. Utilizing quantitative zymography we found that MMP-13 activity gradually increased from ED14-ED16 reaching a plateau from ED16-ED21, while MMP-2 activity demonstrated a transient increase starting at ED13, peaked at ED16 and declined thereafter. As to MMP-9 activity, it was seen only between ED16 and ED 18. In situ zymography with gelatin as a substrate represented activity of MMPs within the myocardium of the atria and the ventricles and a very strong activity in the interstitial tissue of the endocardial and the conotruncal cushion tissue. Conclusion MMPs expressed in embryonic heart correspond to all major classes of these enzymes. They may contribute to embryonic remodeling of the heart.
Expression of Type XVII Collagen .ALPHA.1 Chain mRNA in the Mouse Heart
Japanese Heart Journal, 1998
The type X\'II collagen al chain has been identified as a component of the type I hemidesmosome, and is thus thought to play a role in extracellular matrix ECM maintenance and signal transduction between the cell and the EC\I. We examined the expression of type XVII collagen al chain mRNA in the mouse heart by Northern blot analysis and determined the sequential changes of its expression in different developmental stages of the heart using the reverse transcriptase-polymerase chain reaction (RT-PCR) method..Vorthem blotting: Total RNA was extracted from 10 adult mouse hearts by the guanidine/cesium method. Hybridization was performed with mouse cDNA for a1 XVIL collagen. RT-PCP,• Total RNA was extracted from 7 embryos. 4 neonates and 8 adult mice. Reverse transcription was performed using oligo-dT primer and \I\ILV. Amplification was carried out in a1 XVIIi collagen and glyceraldehyde 3-phosphate dehvdrogenase (GAPDH). GAPDH served as an internal control. Northern blotting revealed a 5.6 kb signal that was identical to that of the a1 XVII) of skin and transformed keratinocyte reported previously. The sequences of the PCR products were also identical to those reported. The normalized expression ratios of al XVII) were 0.91 ± 0.20 in the embryonic heart, 0.36 ± 0.20 in the neonatal heart and 0.96 ± 0.21 in the adult heart. In conclusion, we identified the expression of type XVII collagen al chain mRNA in the mouse heart, suggesting that the type I hemidesmosome is located in the heart. The results of the RT-PCR at different developmental stages of the heart suggest that type XVII collagen contributes not only to cardiogenesis in the embryonic stage but also to maintenance of architecture and function in the adult heart.
Pregnancy Differentially Regulates the Collagens Types I and III in Left Ventricle from Rat Heart
BioMed Research International, 2014
The pathologic cardiac remodeling has been widely documented; however, the physiological cardiac remodeling induced by pregnancy and its reversion in postpartum are poorly understood. In the present study we investigated the changes in collagen I (Col I) and collagen III (Col III) mRNA and protein levels in left ventricle from rat heart during pregnancy and postpartum. Col I and Col III mRNA expression in left ventricle samples during pregnancy and postpartum were analyzed by using quantitative PCR. Data obtained from gene expression show that Col I and Col III in left ventricle are upregulated during pregnancy with reversion in postpartum. In contrast to gene expression, the protein expression evaluated by western blot showed that Col I is downregulated and Col III is upregulated in left ventricle during pregnancy. In conclusion, the pregnancy differentially regulates collagens types I and III in heart; this finding could be an important molecular mechanism that regulates the ventricular stiffness in response to blood volume overload present during pregnancy which is reversed in postpartum.
Distribution of collagens and fibronectin in the subepicardium during avian cardiac development
Anatomy and Embryology, 1992
The development of the layer of connective tissue between ventricular epicardium and myocardium was studied during chick morphogenesis using electron microscopy, light microscopy and immunohistochemical techniques. This layer, called the subepicardium, increases rapidly in volume from embryonic day 6 to 11 (E6 Ell) during mesenchymal cell invasion. Fibrous, matrix components are initially apparent at Ell to El6, and as fibrous connective tissue structures accumulate, subepicardial volume decreases. Antibody labeling shows that fibronectin is an early, prominent constituent of the subepicardium, and by ES, the subepicardium is the cardiac site most enriched in fibronectin. Collagen type III is present in circumferentially-oriented fibers at E8. During subsequent cardiac growth, collagen type III fibers become broadly distributed in the subepicardium, with some fibers appearing to attach myocardium to epicardium. Collagen type I fibers are not apparent until El0. At El2 collagen type I fibers are distributed circumferentially around the heart in bundles crimped into waves of low amplitude. Other collagen type I fibers are oriented radially in the subepicardium. During late cardiac morphogenesis and in fully-differentiated hearts, fibronectin and collagen types I and III are more concentrated in the subepicardium than within the myocardium. These observations suggest that the composition and organization of the subepicardial connective tissue may make important contributions to cardiac mechanics from the latter half of embryonic development through adulthood.
Hemodynamics Modify Collagen Deposition in the Early Embryonic Chicken Heart Outflow Tract
Journal of Cardiovascular Development and Disease, 2017
Blood flow is critical for normal cardiac development. Hemodynamic stimuli outside of normal ranges can lead to overt cardiac defects, but how early heart tissue remodels in response to altered hemodynamics is poorly understood. This study investigated changes in tissue collagen in response to hemodynamic overload in the chicken embryonic heart outflow tract (OFT) during tubular heart stages (HH18 to HH24,~24 h). A suture tied around the OFT at HH18 was tightened to constrict the lumen for~24 h (constriction range at HH24: 15-60%). Expression of fibril collagens I and III and fibril organizing collagens VI and XIV were quantified at the gene and protein levels via qPCR and quantitative immunofluorescence. Collagen I was slightly elevated upstream of the band and in the cushions in banded versus control OFTs. Changes in collagen III were not observed. Collagen VI deposition was elevated downstream of the band, but not overall. Collagen XIV deposition increased throughout the OFT, and strongly correlated to lumen constriction. Interestingly, organization of collagen I fibrils was observed for the tighter banded embryos in regions that also showed increase in collagen XIV deposition, suggesting a potentially key role for collagens I and XIV in the structural adaptation of embryonic heart tissue to hemodynamic overload.