Distribution and expression of type VI collagen in photoaged skin

Watson, Rachel; Ball, Stephen G.; Craven, N. M.; Boorsma, J.; East, C.L.; Shuttleworth, C. Adrian; Kielty, Cay M.; Griffiths, C.E.M.

doi:10.1046/j.1365-2133.2001.04012.x

Cited by 39 publications

(26 citation statements)

References 48 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…15 The effect of the aging process on collagen VII biosynthesis and degradation has been previously noted. [16][17][18] In both groups, collagen type VII has increased (Fig 4, B) with significantly positive correlation (r = 10.947, P \.001) ( Table I).…”

Section: Evaluation Of Dermal Collagenmentioning

confidence: 87%

Fractional versus ablative erbium:yttrium-aluminum-garnet laser resurfacing for facial rejuvenation: An objective evaluation

El‐Domyati

Abd-ElRaheem

Abdel-Wahab

et al. 2013

Journal of the American Academy of Dermatology

View full text Add to dashboard Cite

Section: Evaluation Of Dermal Collagenmentioning

confidence: 87%

Fractional versus ablative erbium:yttrium-aluminum-garnet laser resurfacing for facial rejuvenation: An objective evaluation

El‐Domyati

Abd-ElRaheem

Abdel-Wahab

et al. 2013

Journal of the American Academy of Dermatology

View full text Add to dashboard Cite

“…We speculate that this antibody might react to certain incomplete collagen VI molecules. The variant collagen VI alpha 3 chain has been detected in the epidermis in contrast to the usual collagen VI expression in the dermis in photoaged skin 36. Thus, the variable severity in different tissues in Ullrich's disease may be related to a number of factors including differences in remaining collagen VI protein, different expression of collagen VI‐associated molecules such as NG2 proteoglycan, and compensatory expression of other collagen molecules or unknown proteins.…”

Section: Discussionmentioning

confidence: 99%

Abnormal expression of proteoglycans in Ullrich's disease with collagen VI deficiency

et al. 2005

View full text Add to dashboard Cite

Patients with Ullrich's disease have generalized muscle weakness, multiple contractures of the proximal joints, and hyperextensibility of the distal joints. Recently we found a marked reduction of fibronectin receptors in the skin and cultured fibroblasts of two patients with Ullrich's disease with collagen VI deficiency, and speculated that an abnormality of cell adhesion may be involved in the pathogenesis of the disease. In this study, we investigated the expression of proteoglycans and adhesion molecules in Ullrich's disease and other muscle diseases. We found a reduction of NG2 proteoglycan in the membrane of skeletal muscle but not in the skin in Ullrich's disease. By contrast, we found the upregulation of tenascin C in the extracellular matrix of skeletal muscle in Ullrich's disease. Our findings suggest that abnormal expression of proteoglycans and adhesion molecules may be involved in the pathogenesis of the dystrophic muscle changes in Ullrich's disease. Muscle Nerve, 2006

show abstract

“…A cumulative effect of photoexposure can lead to the degradation of elastin and fibrillin in the reticular dermis 18,20. In the reticular dermis of young skin, an abundant amount of MAGP-1 fibers, oriented parallel to the skin’s surface, was observed.…”

Section: Resultsmentioning

confidence: 99%

Investigation of age-related decline of microfibril-associated glycoprotein-1 in human skin through immunohistochemistry study

Zheng¹,

Chen²,

Chen³

et al. 2013

CCID

View full text Add to dashboard Cite

During aging, the reduction of elastic and collagen fibers in dermis can lead to skin atrophy, fragility, and aged appearance, such as increased facial wrinkling and sagging. Microfibril-associated glycoprotein-1 (MAGP-1) is an extracellular matrix protein critical for elastic fiber assembly. It integrates and stabilizes the microfibril and elastin matrix network that helps the skin to endure mechanical stretch and recoil. However, the observation of MAGP-1 during skin aging and its function in the dermis has not been established. To better understand age-related changes in the dermis, we investigated MAGP-1 during skin aging and photoaging, using a combination of in vitro and in vivo studies. Gene expression by microarray was performed using human skin biopsies from young and aged female donors. In addition, immunofluorescence analysis on the MAGP-1 protein was performed in dermal fibroblast cultures and in human skin biopsies. Specific antibodies against MAGP-1 and fibrillin-1 were used to examine protein expression and extracellular matrix structure in the dermis via biopsies from donors of multiple age groups. A reduction of the MAGP-1 gene and protein levels were observed in human skin with increasing age and photoexposure, indicating a loss of the functional MAGP-1 fiber network and a lack of structural support in the dermis. Loss of MAGP-1 around the hair follicle/pore areas was also observed, suggesting a possible correlation between MAGP-1 loss and enlarged pores in aged skin. Our findings demonstrate that a critical “pre-elasticity” component, MAGP-1, declines with aging and photoaging. Such changes may contribute to age-related loss of dermal integrity and perifollicular structural support, which may lead to skin fragility, sagging, and enlarged pores.

show abstract

Distribution and expression of type VI collagen in photoaged skin

Cited by 39 publications

References 48 publications

Fractional versus ablative erbium:yttrium-aluminum-garnet laser resurfacing for facial rejuvenation: An objective evaluation

Fractional versus ablative erbium:yttrium-aluminum-garnet laser resurfacing for facial rejuvenation: An objective evaluation

Abnormal expression of proteoglycans in Ullrich's disease with collagen VI deficiency

Investigation of age-related decline of microfibril-associated glycoprotein-1 in human skin through immunohistochemistry study

Contact Info

Product

Resources

About