scholarly journals Hyaluronic acid, HAS1, and HAS2 are significantly upregulated during muscle hypertrophy

2012 ◽  
Vol 303 (5) ◽  
pp. C577-C588 ◽  
Author(s):  
Sarah Calve ◽  
Jahdonna Isaac ◽  
Jonathan P. Gumucio ◽  
Christopher L. Mendias
Keyword(s):  
Skeletal Muscle ◽  
Hyaluronic Acid ◽  
Type I Collagen ◽  
Muscle Growth ◽  
Type I ◽  
Muscle Adaptation ◽  
Cell Recruitment ◽  
Regeneration In Vitro ◽  
Muscle Progenitor Cell

Hyaluronic acid (HA) is a component of the extracellular matrix (ECM) in most vertebrate tissues and is thought to play a significant role during development, wound healing, and regeneration. In vitro studies have shown that HA enhances muscle progenitor cell recruitment and inhibits premature myotube fusion, implicating a role for this glycosaminoglycan in functional repair. However, the spatiotemporal distribution of HA during muscle growth and repair was unknown. We hypothesized that inducing hypertrophy via synergist ablation would increase the expression of HA and the HA synthases (HAS1–HAS3). We found that HA and HAS1–HAS3 were significantly upregulated within the plantaris muscle in response to Achilles tenectomy. HA concentration significantly increased 2.8-fold after 2 days but decreased towards levels comparable to age-matched controls by 14 days. Using immunohistochemistry, we found the colocalization of HAS1–HAS3 with macrophages, blood vessel epithelia, and fibroblasts varied in response to time and/or tenectomy. At the level of gene expression, only HAS1 and HAS2 significantly increased with respect to both time and tenectomy. The profiles of additional genes that influence ECM composition during muscle repair, tenascin-C, type I collagen, the HA-degrading hyaluronidases (Hyal) and matrix metalloproteinases (MMP) were also investigated. Hyal1 and Hyal2 were highly expressed in skeletal muscle but did not change after tenectomy; however, indicators of hypertrophy, MMP-2 and MMP-14, were significantly upregulated from 2 to 14 days. These results indicate that HA levels dynamically change in response to a hypertrophic stimulus and various cells may participate in this mechanism of skeletal muscle adaptation.

scholarly journals Mannose receptor regulates myoblast motility and muscle growth

2006 ◽  
Vol 174 (3) ◽  
pp. 403-413 ◽  
Author(s):  
Katie M. Jansen ◽  
Grace K. Pavlath
Keyword(s):  
Skeletal Muscle ◽  
Transmembrane Protein ◽  
Muscle Growth ◽  
Mannose Receptor ◽  
Time Lapse ◽  
Myoblast Fusion ◽  
Type I ◽  
Matrix Remodeling

Myoblast fusion is critical for the formation, growth, and maintenance of skeletal muscle. The initial formation of nascent myotubes requires myoblast–myoblast fusion, but further growth involves myoblast–myotube fusion. We demonstrate that the mannose receptor (MR), a type I transmembrane protein, is required for myoblast–myotube fusion. Mannose receptor (MR)–null myotubes were small in size and contained a decreased myonuclear number both in vitro and in vivo. We hypothesized that this defect may arise from a possible role of MR in cell migration. Time-lapse microscopy revealed that MR-null myoblasts migrated with decreased velocity during myotube growth and were unable to migrate in a directed manner up a chemoattractant gradient. Furthermore, collagen uptake was impaired in MR-null myoblasts, suggesting a role in extracellular matrix remodeling during cell motility. These data identify a novel function for MR during skeletal muscle growth and suggest that myoblast motility may be a key aspect of regulating myotube growth.

scholarly journals Timely Supplementation of Hydrogels Containing Sulfated or Unsulfated Chondroitin and Hyaluronic Acid Affects Mesenchymal Stromal Cells Commitment Toward Chondrogenic Differentiation

2021 ◽  
Vol 9 ◽  
Author(s):  
Nicola Alessio ◽  
Antonietta Stellavato ◽  
Domenico Aprile ◽  
Donatella Cimini ◽  
Valentina Vassallo ◽  
...  
Keyword(s):  
Hyaluronic Acid ◽  
Mesenchymal Stromal Cells ◽  
Stromal Cells ◽  
Type I Collagen ◽  
Chondrocyte Differentiation ◽  
Type I ◽  
Cell Commitment ◽  
Transplant Procedure

Mesenchymal stromal cells (MSCs) are currently used for cartilage cell therapy because of their well proven capacity to differentiate in chondrocytes. The advantage of MSC-based therapy is the possibility of producing a high number of chondrocytes for implants. The transplant procedure, however, has some limitations, since MSCs may produce non-functional chondrocytes. This limit has been challenged by cultivating MSC in media with hydrogels containing hyaluronic acid (HA), extractive chondroitin sulfate (CS), or bio-fermentative unsulphated chondroitin (BC) alone or in combination. Nevertheless, a clear study of the effect of glycosaminoglycans (GAGs) on chondrocyte differentiation is still lacking, especially for the newly obtained unsulfated chondroitin of biotechnological origin. Are these GAGs playing a role in the commitment of stem cells to chondrocyte progenitors and in the differentiation of progenitors to mature chondrocytes? Alternatively, do they have a role only in one of these biological processes? We evaluated the role of HA, CS, and – above all – BC in cell commitment and chondrocyte differentiation of MSCs by supplementing these GAGs in different phases of in vitro cultivation. Our data provided evidence that a combination of HA and CS or of HA and BC supplemented during the terminal in vitro differentiation and not during cell commitment of MSCs improved chondrocytes differentiation without the presence of fibrosis (reduced expression of Type I collagen). This result suggests that a careful evaluation of extracellular cues for chondrocyte differentiation is fundamental to obtaining a proper maturation process.

scholarly journals Reducing the Foreign Body Reaction by Surface Modification with Collagen/Hyaluronic Acid Multilayered Films

2014 ◽  
Vol 2014 ◽  
pp. 1-8 ◽  
Author(s):  
Cindy Yi Chi Hsieh ◽  
Fang-Wei Hu ◽  
Wen-Shiang Chen ◽  
Wei-Bor Tsai
Keyword(s):  
Surface Modification ◽  
Hyaluronic Acid ◽  
Foreign Body ◽  
Type I Collagen ◽  
Foreign Body Reaction ◽  
Biological Response ◽  
Multilayer Films ◽  
Type I ◽  
Layer By Layer

Biological response against foreign implants often leads to encapsulation, possibly resulting in malfunction of implants devices. The aim of this study was to reduce the foreign body reaction by surface modification of biomaterials through layer-by-layer deposition of type I collagen (COL)/hyaluronic acid (HA) multilayer films. Polydimethylsiloxane (PDMS) samples were coated with alternative COL and HA layers with different layers. We found that the in vitro adhesion, proliferation, and activation of macrophage-like cells were greatly decreased by COL/HA multilayered deposition. The PDMS samples modified with 20 bilayers of COL/HA were implanted in rats for 3 weeks, and the thickness of encapsulation surrounding the samples was decreased by 29–57% compared to the control unmodified PDMS. This study demonstrates the potential of COL/HA multilayer films to reduce foreign body reaction.

scholarly journals The synergistic effect of type I collagen and hyaluronic acid on the biological properties of Col/HA-multilayer-modified titanium coatings: an in vitro and in vivo study

RSC Advances ◽  
2017 ◽  
Vol 7 (42) ◽  
pp. 25828-25837 ◽  
Author(s):  
Haiyong Ao ◽  
Chucheng Lin ◽  
Binen Nie ◽  
Shengbing Yang ◽  
Youtao Xie ◽  
...  
Keyword(s):  
Hyaluronic Acid ◽  
Synergistic Effect ◽  
Type I Collagen ◽  
Biological Properties ◽  
In Vivo Study ◽  
Type I ◽  
Titanium Coatings

The synergistic effect on osseointegration is existed between Type I collagen (ColI) and hyaluronic acid (HA), and the early osseogenetic activity of ColI/HA multilayer modified titanium coatings (TC) is higher than that ColI modified TC and HA modified TC.

scholarly journals In Vitro Anti-Wrinkle and Skin-Moisturizing Effects of Evening Primrose (Oenothera biennis) Sprout and Identification of Its Active Components

Processes ◽  
2021 ◽  
Vol 9 (1) ◽  
pp. 145
Author(s):  
Tae Heon Kim ◽  
Woo Jung Kim ◽  
Soon Yeong Park ◽  
Hoon Kim ◽  
Dae Kyun Chung
Keyword(s):  
Hyaluronic Acid ◽  
Type I Collagen ◽  
Radical Scavenging ◽  
Reducing Power ◽  
Flavonoid Glycosides ◽  
Type I ◽  
Active Components ◽  
Oenothera Biennis ◽  
Evening Primrose

The present study aimed to investigate the effect of Oenothera biennis sprout extract (OBS-E) on skin-function improvement in an in vitro system and to identify its pharmaceutically active components. OBS-E showed antioxidant ability in radical scavenging and reducing power assays, significantly inhibited matrix metalloproteinases-1 and -2, and increased the production of type I collagen, indicating its anti-wrinkle activity. Furthermore, OBS-E significantly increased the level of hyaluronic acid (HA) and the expression of moisturizing genes, such as hyaluronic acid synthase 2 (HAS2) and aquaporin 3 (AQP3), indicating it is effective in enhancing skin hydration. High-performance liquid chromatography (HPLC) and mass spectrometry (MS) analyses showed that OBS-E contained high levels of polyphenolic acids, such as gallic acid and ellagic acid, in addition to flavonoid glycosides, such as luteolin 7-glucuronide and quercetin 3-glucuronide. Our results suggest that these major phytochemicals are likely to play crucial roles in the expression of antioxidant, anti-wrinkle, and moisturizing activities of OBS-E.

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.

scholarly journals Restoration of Osteogenesis by CRISPR/Cas9 Genome Editing of the Mutated COL1A1 Gene in Osteogenesis Imperfecta

2021 ◽  
Vol 10 (14) ◽  
pp. 3141
Author(s):  
Hyerin Jung ◽  
Yeri Alice Rim ◽  
Narae Park ◽  
Yoojun Nam ◽  
Ji Hyeon Ju
Keyword(s):  
Osteogenesis Imperfecta ◽  
Type I Collagen ◽  
Disease Modeling ◽  
Bone Fragility ◽  
Osteogenic Potential ◽  
Type I ◽  
Gene Correction ◽  
Col1a1 Gene ◽  
Collagen Formation

Osteogenesis imperfecta (OI) is a genetic disease characterized by bone fragility and repeated fractures. The bone fragility associated with OI is caused by a defect in collagen formation due to mutation of COL1A1 or COL1A2. Current strategies for treating OI are not curative. In this study, we generated induced pluripotent stem cells (iPSCs) from OI patient-derived blood cells harboring a mutation in the COL1A1 gene. Osteoblast (OB) differentiated from OI-iPSCs showed abnormally decreased levels of type I collagen and osteogenic differentiation ability. Gene correction of the COL1A1 gene using CRISPR/Cas9 recovered the decreased type I collagen expression in OBs differentiated from OI-iPSCs. The osteogenic potential of OI-iPSCs was also recovered by the gene correction. This study suggests a new possibility of treatment and in vitro disease modeling using patient-derived iPSCs and gene editing with CRISPR/Cas9.

scholarly journals Effects of chitosan-collagen dressing on wound healing in vitro and in vivo assays

2021 ◽  
Vol 19 ◽  
pp. 228080002198969
Author(s):  
Min-Xia Zhang ◽  
Wan-Yi Zhao ◽  
Qing-Qing Fang ◽  
Xiao-Feng Wang ◽  
Chun-Ye Chen ◽  
...  
Keyword(s):  
Wound Healing ◽  
Wound Dressing ◽  
Type I Collagen ◽  
Inhibition Zone ◽  
Negative Control ◽  
Type I ◽  
Nih3t3 Cells ◽  
Post Operation

The present study was designed to fabricate a new chitosan-collagen sponge (CCS) for potential wound dressing applications. CCS was fabricated by a 3.0% chitosan mixture with a 1.0% type I collagen (7:3(w/w)) through freeze-drying. Then the dressing was prepared to evaluate its properties through a series of tests. The new-made dressing demonstrated its safety toward NIH3T3 cells. Furthermore, the CCS showed the significant surround inhibition zone than empty controls inoculated by E. coli and S. aureus. Moreover, the moisture rates of CCS were increased more rapidly than the collagen and blank sponge groups. The results revealed that the CCS had the characteristics of nontoxicity, biocompatibility, good antibacterial activity, and water retention. We used a full-thickness excisional wound healing model to evaluate the in vivo efficacy of the new dressing. The results showed remarkable healing at 14th day post-operation compared with injuries treated with collagen only as a negative control in addition to chitosan only. Our results suggest that the chitosan-collagen wound dressing were identified as a new promising candidate for further wound application.

scholarly journals Relative rates of biosynthesis of collagen type I, type V and type VI in calf cornea

1991 ◽  
Vol 274 (2) ◽  
pp. 615-617 ◽  
Author(s):  
P Kern ◽  
M Menasche ◽  
L Robert
Keyword(s):  
Type I Collagen ◽  
Collagen Type ◽  
Corneal Stroma ◽  
Collagen Type I ◽  
Type I ◽  
Type Vi Collagen ◽  
Sds Page ◽  
Proline Incorporation ◽  
Type V

The biosynthesis of type I, type V and type VI collagens was studied by incubation of calf corneas in vitro with [3H]proline as a marker. Pepsin-solubilized collagen types were isolated by salt fractionation and quantified by SDS/PAGE. Expressed as proportions of the total hydroxyproline solubilized, corneal stroma comprised 75% type I, 8% type V and 17% type VI collagen. The rates of [3H]proline incorporation, linear up to 24 h for each collagen type, were highest for type VI collagen and lowest for type I collagen. From pulse-chase experiments, the calculated apparent half-lives for types I, V and VI collagens were 36 h, 10 h and 6 h respectively.

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