Changes in the type II and type I collagen messenger RNA population during growth of chondrocytes in 5-bromo-2-deoxyuridine.

Osteogenesis imperfecta (OI) is a heritable disorder that mainly affects the skeleton. The inheritance is mostly autosomal dominant and associated to mutations in one of the two genes, COL1A1 and COL1A2, encoding for the type I collagen α chains. According to more than 1500 described mutation sites and to outcome spanning from very mild cases to perinatal-lethality, OI is characterized by a wide genotype/phenotype heterogeneity. In order to identify common affected molecular-pathways and disease biomarkers in OI probands with different mutations and lethal or surviving phenotypes, primary fibroblasts from dominant OI patients, carrying COL1A1 or COL1A2 defects, were investigated by applying a Tandem Mass Tag labeling-Liquid Chromatography-Tandem Mass Spectrometry (TMT LC-MS/MS) proteomics approach and bioinformatic tools for comparative protein-abundance profiling. While no difference in α1 or α2 abundance was detected among lethal (type II) and not-lethal (type III) OI patients, 17 proteins, with key effects on matrix structure and organization, cell signaling, and cell and tissue development and differentiation, were significantly different between type II and type III OI patients. Among them, some non–collagenous extracellular matrix (ECM) proteins (e.g., decorin and fibrillin-1) and proteins modulating cytoskeleton (e.g., nestin and palladin) directly correlate to the severity of the disease. Their defective presence may define proband-failure in balancing aberrances related to mutant collagen.

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Methylation of type II and type I collagen genes in differentiated and dedifferentiated chondrocytes.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)89563-1 ◽

1985 ◽

Vol 260 (4) ◽

pp. 2374-2378

Author(s):

M P Fernández ◽

M F Young ◽

M E Sobel

Keyword(s):

Type I Collagen ◽

Type I ◽

Type Ii ◽

Collagen Genes

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Type VI collagen expression is upregulated in the early events of chondrocyte differentiation

Development ◽

10.1242/dev.117.1.245 ◽

1993 ◽

Vol 117 (1) ◽

pp. 245-251

Author(s):

R. Quarto ◽

B. Dozin ◽

P. Bonaldo ◽

R. Cancedda ◽

A. Colombatti

Keyword(s):

Suspension Culture ◽

Type I Collagen ◽

Type Ii Collagen ◽

Type I ◽

Type Ii ◽

Type Vi Collagen ◽

Full Spectrum ◽

Collagen Expression ◽

Hypertrophic Chondrocyte

Dedifferentiated chondrocytes cultured adherent to the substratum proliferate and synthesize large amounts of type I collagen but when transferred to suspension culture they decrease proliferation, resume the chondrogenic phenotype and the synthesis of type II collagen, and continue their maturation to hypertrophic chondrocyte (Castagnola et al., 1986, J. Cell Biol. 102, 2310–2317). In this report, we describe the developmentally regulated expression of type VI collagen in vitro in differentiating avian chondrocytes. Type VI collagen mRNA is barely detectable in dedifferentiated chondrocytes as long as the attachment to the substratum is maintained, but increases very rapidly upon passage of the cells into suspension culture reaching a peak after 48 hours and declining after 5–6 days of suspension culture. The first evidence of a rise in the mRNA steady-state levels is obtained already at 6 hours for the alpha 3(VI) chain. Immunoprecipitation of metabolically labeled cells with type VI collagen antibodies reveals that the early mRNA rise is paralleled by an increased secretion of type VI collagen in cell media. Induction of type VI collagen is not the consequence of trypsin treatment of dedifferentiated cells since exposure to the actin-disrupting drug cytochalasin or detachment of the cells by mechanical procedures has similar effects. In 13-day-old chicken embryo tibiae, where the full spectrum of the chondrogenic differentiation process is represented, expression of type VI collagen is restricted to the articular cartilage where chondrocytes developmental stage is comparable to stage I (high levels of type II collagen expression).(ABSTRACT TRUNCATED AT 250 WORDS)

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Role of collagenase in mediating in vitro alveolar epithelial wound repair

Journal of Cell Science ◽

10.1242/jcs.112.2.243 ◽

1999 ◽

Vol 112 (2) ◽

pp. 243-252

Author(s):

E. Planus ◽

S. Galiacy ◽

M. Matthay ◽

V. Laurent ◽

J. Gavrilovic ◽

...

Keyword(s):

Cell Migration ◽

Cell Adhesion ◽

Epithelial Cell ◽

Type I Collagen ◽

Alveolar Epithelial Cell ◽

Cell Monolayer ◽

Type I ◽

Type Ii ◽

Alveolar Epithelial

Type II pneumocytes are essential for repair of the injured alveolar epithelium. The effect of two MMP collagenases, MMP-1 and MMP-13 on alveolar epithelial repair was studied in vitro. The A549 alveolar epithelial cell line and primary rat alveolar epithelial cell cultures were used. Cell adhesion and cell migration were measured with and without exogenous MMP-1. Wound healing of a cell monolayer of rat alveolar epithelial cell after a mechanical injury was evaluated by time lapse video analysis. Cell adhesion on type I collagen, as well as cytoskeleton stiffness, was decreased in the presence of exogenous collagenases. A similar decrease was observed when cell adhesion was tested on collagen that was first incubated with MMP-1 (versus control on intact collagen). Cell migration on type I collagen was promoted by collagenases. Wound healing of an alveolar epithelial cell monolayer was enhanced in the presence of exogenous collagenases. Our results suggest that collagenases could modulate the repair process by decreasing cell adhesion and cell stiffness, and by increasing cell migration on type I collagen. Collagen degradation could modify cell adhesion sites and collagen degradation peptides could induce alveolar type II pneumocyte migration. New insights regarding alveolar epithelial cell migration are particularly relevant to investigate early events during alveolar epithelial repair following lung injury.

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Control of types I and II collagen and fibronectin gene expression in chondrocytes delineated by viral transformation.

Molecular and Cellular Biology ◽

10.1128/mcb.5.5.1002 ◽

1985 ◽

Vol 5 (5) ◽

pp. 1002-1008 ◽

Cited By ~ 33

Author(s):

E S Allebach ◽

D Boettiger ◽

M Pacifici ◽

S L Adams

Keyword(s):

Rous Sarcoma Virus ◽

Type I Collagen ◽

Skin Fibroblasts ◽

Transcriptional Level ◽

Type I ◽

Type Ii ◽

Intact Cells ◽

Rous Sarcoma ◽

Synthetic Rate ◽

Sarcoma Virus

We have analyzed the effects of transformation by Rous sarcoma virus on expression of types I and II collagen and fibronectin genes in vertebral chondrocytes and compared them with expression of these genes in skin fibroblasts. Transformed chondrocytes display a dramatically decreased amount of type II collagen RNA, which can account fully for the decreased synthetic rate of this protein. Paradoxically, these cells also display greatly increased amounts of type I collagen RNAs, which are translated efficiently in vitro, but not in the intact cells. We show here that the type I collagen RNAs in transformed chondrocytes are nearly indistinguishable from those found in skin fibroblasts, and that they clearly differ from the type I collagen RNAs found in normal chondrocytes. Transformed chondrocytes also display an increased amount of fibronectin RNAs, which can account fully for the increased synthetic rate of this protein. Thus, the effects of transformation by Rous sarcoma virus on type I collagen and fibronectin RNAs in chondrocytes are the opposite of those observed in fibroblasts, which display decreased amounts of these three RNAs. These data indicate that the effects of transformation on the genes encoding type I collagen and fibronectin must be modulated by host cell-specific factors. They also imply that the types I and II collagen genes may be regulated by different mechanisms, the type I genes being controlled at both transcriptional and posttranscriptional levels, and the type II gene being controlled primarily at the transcriptional level.

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In situ hybridization reveals differential spatial distribution of mRNAs for type I and type II collagen in the chick limb bud

Development ◽

10.1242/dev.103.1.111 ◽

1988 ◽

Vol 103 (1) ◽

pp. 111-118 ◽

Cited By ~ 1

Author(s):

C.J. Devlin ◽

P.M. Brickell ◽

E.R. Taylor ◽

A. Hornbruch ◽

R.K. Craig ◽

...

Keyword(s):

In Situ Hybridization ◽

Limb Development ◽

Type I Collagen ◽

Type Ii Collagen ◽

Limb Bud ◽

Type I ◽

Type Ii ◽

Mrna Accumulation ◽

Rna Probes

During limb development, type I collagen disappears from the region where cartilage develops and synthesis of type II collagen, which is characteristic of cartilage, begins. In situ hybridization using antisense RNA probes was used to investigate the spatial localization of type I and type II collagen mRNAs. The distribution of the mRNA for type II collagen corresponded well with the pattern of type II collagen synthesis, suggesting control at the level of transcription and mRNA accumulation. In contrast, the pattern of mRNA for type I collagen remained more or less uniform and did not correspond with the synthesis of the protein, suggesting control primarily at the level of translation or of RNA processing.

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Inhibition of Collagen-Induced Platelet Aggregation by Antibodies to Distinct Types of Collagen

10.1055/s-0039-1680529 ◽

1977 ◽

Author(s):

L. Balleisen ◽

R. Timpl ◽

S. Gay

Keyword(s):

Platelet Aggregation ◽

Serum Albumin ◽

Type I Collagen ◽

Collagen Fibers ◽

Type Iii Collagen ◽

Type I ◽

Fibrillar Collagen ◽

Type Ii ◽

Molecular Parameters ◽

Inhibition Reaction

The reaction of platelets with fibrillar collagen was measured by recording aggregation according to Borns method and by retraction of Ancrod-fibrin clots. These reactions could be completely inhibited by coating the fibrils with stoichiometric amounts of purified antibodies to type I, II or III collagens. The inhibition was specific, i. e. antibodies to type I collagen prevented aggregation by type I collagen but not by type II or III collagen. Comparable amounts ofantibodies to fibrinogen or to serum albumin had no effect on the reaction. The data indicate that platelet aggregation by type I or II collagen fibrils is not due to contamination with type III collagen. The inhibition reaction may be useful for further studies on molecular parameters of the interaction between platelets and collagen fibers.

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Maintenance of chondrocyte phenotype during expansion on PLLA microtopographies

Journal of Tissue Engineering ◽

10.1177/2041731418789829 ◽

2018 ◽

Vol 9 ◽

pp. 204173141878982 ◽

Cited By ~ 6

Author(s):

Elisa Costa ◽

Cristina González-García ◽

José Luis Gómez Ribelles ◽

Manuel Salmerón-Sánchez

Keyword(s):

Lactic Acid ◽

Type I Collagen ◽

Collagen Type ◽

Articular Chondrocytes ◽

Collagen Type I ◽

Cell Phenotype ◽

Type I ◽

Type Ii ◽

Collagen Type Ii ◽

Chondrocyte Phenotype

Articular chondrocytes are difficult to grow, as they lose their characteristic phenotype following expansion on standard tissue culture plates. Here, we show that culturing them on surfaces of poly(L-lactic acid) of well-defined microtopography allows expansion and maintenance of characteristic chondrogenic markers. We investigated the dynamics of human chondrocyte dedifferentiation on the different poly(L-lactic acid) microtopographies by the expression of collagen type I, collagen type II and aggrecan at different culture times. When seeded on poly(L-lactic acid), chondrocytes maintained their characteristic hyaline phenotype up to 7 days, which allowed to expand the initial cell population approximately six times without cell dedifferentiation. Maintenance of cell phenotype was afterwards correlated to cell adhesion on the different substrates. Chondrocytes adhesion occurs via the α5 β1 integrin on poly(L-lactic acid), suggesting cell–fibronectin interactions. However, α2 β1 integrin is mainly expressed on the control substrate after 1 day of culture, and the characteristic chondrocytic markers are lost (collagen type II expression is overcome by the synthesis of collagen type I). Expanding chondrocytes on poly(L-lactic acid) might be an effective solution to prevent dedifferentiation and improving the number of cells needed for autologous chondrocyte transplantation.

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Collagen metabolism in two types of autosomal dominant osteopetrosis during stimulation with thyroid hormones

Acta Endocrinologica ◽

10.1530/eje.0.1330557 ◽

1995 ◽

Vol 133 (5) ◽

pp. 557-563 ◽

Cited By ~ 7

Author(s):

Jens Bollerslev ◽

Sian Thomas ◽

Ellen Grodum ◽

Kim Brixen ◽

Ole Djøseland

Keyword(s):

Thyroid Hormones ◽

Type I Collagen ◽

Autosomal Dominant ◽

Collagen Metabolism ◽

Significant Response ◽

Type I ◽

Type Ii ◽

Creatinine Ratio ◽

Carboxy Terminal ◽

Autosomal Dominant Osteopetrosis

Bollerslev J, Thomas S, Grodum E, Brixen K, Djøseland 0. Collagen metabolism in two types of autosomal dominant osteopetrosis during stimulation with thyroid hormones. Eur J Endocrinol 1995;133:557–63. ISSN 0804–4643 In order to investigate collagen metabolism in two different types of autosomal dominant osteopetrosis (ADO), eight patients with type I (aged 23–61 years, mean 40.4 years) and nine patients with type II ADO (aged 20–49 years, mean 32.8 years) were compared with ten normal controls (aged 22–54 years, mean 35.4 years). The subjects were treated with 100 μg of triiodothyronine (T3) daily for 7 days and followed for a total of 4 weeks. Serum T3 increased in all subjects and a corresponding suppression of thyroid-stimulating hormone (TSH) was observed. Serum carboxy-terminal propeptide of type I collagen (S-PICP) in the control and type I groups showed no difference at baseline, whereas type II was lower than controls (p < 0.01). No significant alterations following stimulation were observed in any of the groups. Serum BGP (osteocalcin) values in the two patient groups were insignificantly lower than controls both at baseline and throughout the study. Following stimulation, a significant response was seen in the three groups (p < 0.001). The increases during the treatment period (delta values) for controls, type I and type II were 47.6% (p < 0.01), 51.7% (p = 0.05) and 34.8% (NS), respectively, with no difference between the groups. Serum bone-specific alkaline phosphatase (S-ALP) was not different between the groups and no alterations were observed in relation to treatment. The serum N-terminal propeptide of type III collagen (S-PIIINP) showed no difference at baseline between type I and controls but was significantly higher (p < 0.003) in type II than in the controls. After stimulation, significant responses were observed in all three groups (p < 0.001). Serum PIIINP increased following 1 week of treatment by 64% (p < 0.01), 41% (p < 0.02) and 18% (NS), respectively. Serum carboxy-terminal telopeptide of type I collagen (SICTP) did not differ between type I and controls at baseline but was increased in type II (p < 0.04), as it was throughout the observation period (p < 0.12 and p < 0.02). A significant response was observed in the three groups following stimulation. The delta values were 69% (p = 0.005), 56% (p < 0.02) and 34% (p < 0.02), respectively. The urinary hydroxyproline (OHP)/creatinine ratio did not differ between the groups either at baseline or following stimulation. A significant response (p < 0.001) was observed, with delta values of 44.2% (p < 0.06), 35.9% (p < 0.04) and 34.3% (p < 0.01), respectively. The two bone resorptive markers (S-ICTP and OHP/creatinine ratio) were correlated significantly at baseline for all three groups. It is concluded that collagen metabolism is disturbed in type II ADO, which might reflect an increased turnover of extra-osseous collagen. Because ICTP levels are increased in disorders with increased extra-osseous collagen turnover, we question the suitability of this parameter as a sensitive marker of bone resorption. Jens Bollerslev, Department of Medical Endocrinology, National University Hospital, N-0027 Oslo, Norway

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Human platelet-rich plasma improves the nesting and differentiation of human chondrocytes cultured in stabilized porous chitosan scaffolds

Journal of Tissue Engineering ◽

10.1177/2041731417697545 ◽

2017 ◽

Vol 8 ◽

pp. 204173141769754 ◽

Cited By ~ 6

Author(s):

Maria Sancho-Tello ◽

Sara Martorell ◽

Manuel Mata Roig ◽

Lara Milián ◽

MA Gámiz-González ◽

...

Keyword(s):

Type I Collagen ◽

Articular Chondrocytes ◽

Platelet Rich Plasma ◽

Cartilage Regeneration ◽

Cell Number ◽

Type I ◽

Type Ii ◽

Cell Counts ◽

Porous Chitosan ◽

Chitosan Scaffolds

The clinical management of large-size cartilage lesions is difficult due to the limited regenerative ability of the cartilage. Different biomaterials have been used to develop tissue engineering substitutes for cartilage repair, including chitosan alone or in combination with growth factors to improve its chondrogenic properties. The main objective of this investigation was to evaluate the benefits of combining activated platelet-rich plasma with a stabilized porous chitosan scaffold for cartilage regeneration. To achieve this purpose, stabilized porous chitosan scaffolds were prepared using freeze gelation and combined with activated platelet-rich plasma. Human primary articular chondrocytes were isolated and cultured in stabilized porous chitosan scaffolds with and without combination to activated platelet-rich plasma. Scanning electron microscopy was used for the morphological characterization of the resulting scaffolds. Cell counts were performed in hematoxylin and eosin–stained sections, and type I and II collagen expression was evaluated using immunohistochemistry. Significant increase in cell number in activated platelet-rich plasma/stabilized porous chitosan was found compared with stabilized porous chitosan scaffolds. Chondrocytes grown on stabilized porous chitosan expressed high levels of type I collagen but type II was not detectable, whereas cells grown on activated platelet rich plasma/stabilized porous chitosan scaffolds expressed high levels of type II collagen and type I was almost undetectable. In summary, activated platelet-rich plasma increases nesting and induces the differentiation of chondrocytes cultured on stabilized porous chitosan scaffolds.

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