Glycolic Acid Treatment Increases Type I Collagen mRNA and Hyaluronic Acid Content of Human Skin

This study aimed to clarify the characteristics of rat vocal fold scarring by examining the alteration of key components in the extracellular matrix: hyaluronic acid, collagen, and fibronectin. Under monitoring with a 1.9-mm-diameter telescope, unilateral vocal fold stripping was performed, and larynges were harvested at 2, 4, 8, and 12 weeks after operation. The vocal folds were histologically analyzed with Alcian blue stain, trichrome stain, and immunofluorescence of collagen type I, collagen type III, and fibronectin. The scarred vocal folds showed less hyaluronic acid and more collagen types I and III than did the controls at all time points. Type III was stable for 12 weeks, while type I declined until 8 weeks and thereafter remained unchanged. Fibronectin increased for 4 weeks and then decreased; it was close to the control level at 8 and 12 weeks. These results suggest that the tissue remodeling process in scarred vocal folds slows down around 2 months after wounding.

Download Full-text

Ionizing Radiation Induces Cytokines, MMP-1, TIMP-1 and Supresses Type I Collagen mRNA Expressions in Human Gingival Fibroblasts

International Journal of Hematology and Oncology ◽

10.4999/uhod.14371 ◽

2014 ◽

Vol 24 (3) ◽

pp. 149-156

Author(s):

Guler Yavas

Keyword(s):

Ionizing Radiation ◽

Type I Collagen ◽

Human Gingival Fibroblasts ◽

Type I ◽

Gingival Fibroblasts ◽

Collagen Mrna

Download Full-text

Mechanical stretch modulates TGF-β1 and α1(I) collagen expression in fetal human intestinal smooth muscle cells

AJP Gastrointestinal and Liver Physiology ◽

10.1152/ajpgi.1999.277.5.g1074 ◽

1999 ◽

Vol 277 (5) ◽

pp. G1074-G1080 ◽

Cited By ~ 14

Author(s):

Jorge A. Gutierrez ◽

Hilary A. Perr

Keyword(s):

Smooth Muscle ◽

Smooth Muscle Cells ◽

Type I Collagen ◽

Intestinal Smooth Muscle ◽

Type I ◽

Collagen Mrna ◽

Collagen Expression ◽

Collagen Protein ◽

Mrna Content ◽

Tgf Β1

Intestinal muscle undergoes stretch intermittently during peristalsis and persistently proximal to obstruction. The influence of this pervasive biomechanical force on developing smooth muscle cell function remains unknown. We adapted a novel in vitro system to study whether stretch modulates transforming growth factor-β1 (TGF-β1) and type I collagen protein and component α1 chain [α1(I) collagen] expression in fetal human intestinal smooth muscle cells. Primary confluent cells at 20-wk gestation, cultured on flexible silicone membranes, were subjected to two brief stretches or to 18 h tonic stretch. Nonstretched cultures served as controls. TGF-β1 protein was measured by ELISA and type I collagen protein was assayed by Western blot. TGF-β1 and α1(I) collagen mRNA abundance was determined by Northern blot analysis, quantitated by phosphorimaging, and normalized to 18S rRNA. Transcription was examined by nuclear run-on assay. Tonic stretch increased TGF-β1 protein 40%, type I collagen protein 100%, TGF-β1 mRNA content 2.16-fold, and α1(I) collagen mRNA 3.80-fold and enhanced transcription of TGF-β1 and α1(I) collagen by 3.1- and 4.25-fold, respectively. Brief stretch stimulated a 50% increase in TGF-β1 mRNA content but no change in α1(I) collagen. Neutralizing anti-TGF-β1 ablated stretch-mediated effects on α1(I) collagen. Therefore, stretch upregulates transcription for TGF-β1, which stimulates α1(I) collagen gene expression in smooth muscle from developing gut.

Download Full-text

Methylpiperidinopyrazole Attenuates Estrogen-Induced Mitochondrial Energy Production and Subsequent Osteoblast Maturation via an Estrogen Receptor Alpha-Dependent Mechanism

Molecules ◽

10.3390/molecules25122876 ◽

2020 ◽

Vol 25 (12) ◽

pp. 2876

Author(s):

Poh-Shiow Yeh ◽

Jui-Tai Chen ◽

Yih-Giun Cherng ◽

Shun-Tai Yang ◽

Yu-Ting Tai ◽

...

Keyword(s):

Energy Production ◽

Estrogen Receptor Alpha ◽

Type I Collagen ◽

Atp Synthesis ◽

Neonatal Rat ◽

Type I ◽

Collagen Mrna ◽

Adenosine Phosphate ◽

Mitochondrial Energy Production ◽

Osteoblast Maturation

An estrogen deficiency is the main cause of osteoporosis in postmenopausal women. In bone remodeling, estrogen receptors (ERs) can mediate estrogen-transducing signals. Methylpiperidinopyrazole (MPP) is a highly specific antagonist of ER-alpha (ERα). This study was designed to evaluate the effects of MPP on estrogen-induced energy production, subsequent osteoblast maturation, and the possible mechanisms. Exposure of primary osteoblasts isolated from neonatal rat calvarias to MPP did not affect cell morphology or survival. Estradiol can induce translocation of ERα into mitochondria from the cytoplasm. Interestingly, pretreatment of rat calvarial osteoblasts with MPP lowered estrogen-induced ERα translocation. Sequentially, estrogen-triggered expressions of mitochondrial energy production-linked cytochrome c oxidase (COX) I and COX II messenger (m)RNAs were inhibited following pretreatment with MPP. Consequently, MPP caused decreases in estrogen-triggered augmentation of the activities of mitochondrial respiratory complex enzymes and levels of cellular adenosine phosphate (ATP). During progression of osteoblast maturation, estrogen induced bone morphogenetic protein (BMP)-6 and type I collagen mRNA expressions, but MPP treatment inhibited such induction. Consequently, estrogen-induced osteoblast activation and mineralization were attenuated after exposure to MPP. Taken together, MPP suppressed estrogen-induced osteoblast maturation through decreasing chromosomal osteogenesis-related BMP-6 and type I collagen mRNA expressions and mitochondrial ATP synthesis due to inhibiting energy production-linked COX I and II mRNA expressions. MPP can appropriately be applied to evaluate estrogen-involved bioenergetics and osteoblast maturation.

Download Full-text

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

AJP Cell Physiology ◽

10.1152/ajpcell.00057.2012 ◽

2012 ◽

Vol 303 (5) ◽

pp. C577-C588 ◽

Cited By ~ 36

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.

Download Full-text