Cultured Human Keratinocytes Express Tropoelastin

Kajiya, Hiroyoshi; Tanaka, Nobuhiko; Inazumi, Toyoko; Seyama, Yousuke; Tajima, S.; Ishibashi, Akira

doi:10.1111/1523-1747.ep12337639

Cited by 28 publications

(20 citation statements)

References 33 publications

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“…We have reported that a collagenous protein and tropoelastin are secreted by keratinocytes [31, 32]; in addition, we have confirmed the presence of elastin in the epidermis, particularly in the granular layer [unpubl. data].…”

Section: Discussionsupporting

confidence: 58%

Differential Regulation of MMP-2 and MMP-9 Gelatinases in Cultured Human Keratinocytes

et al. 1998

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Background: Among matrix metalloproteinases (MMPs), MMP-2 and MMP-9 are considered to play important roles in the tissue metabolism. Objective: To study the production of MMP-2 and MMP-9 in cultured keratinocytes. Methods: We examined the effect of cell passage number and cell differentiation on these enzymes by zymography and immunocytochemistry. Results: Both MMP-2 and MMP-9 gelatinases were detected in keratinocyte-conditioned media using zymography. The level of MMP-2 in the medium decreased after sequential passage, whereas MMP-9 was detected at a constant level. Treatment of keratinocytes with Ca²⁺, a potent stimulator for cell differentiation, induced secretion of MMP-9, which was confirmed immunocytochemically. Inversely, treatment with retinoic acid, which inhibits cell differentiation, increased the level of MMP-2. Conclusion: These results suggest that keratinocytes regulate their secretion of MMP-2 and MMP-9 gelatinase in distinct and independent patterns during differentiation.

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Section: Discussionsupporting

confidence: 58%

Differential Regulation of MMP-2 and MMP-9 Gelatinases in Cultured Human Keratinocytes

et al. 1998

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“…No data however have been presented on the role of elastin as an epidermal cell constituent. The observation of elastin molecule, but not necessarily elastic fibers, within the epidermis of the SE and other reports in the skin (Haynes et al, 1997;Kajiya et al, 1997;Seo et al, 2001) lead to future studies where it will be interesting to determine whether or not elastin can be deposited in normal human epidermis. In this regard, it is interesting to note that elastin peptides have been reported to influence the keratinocyte migration and differentiation (Fujimoto et al, 2000a, b).…”

Section: Discussionmentioning

confidence: 87%

“…Another candidate substrate for LOX or LOXL between keratinocytes might be elastin. Different reports have described the expression of elastin and microfibril mRNAs in keratinocytes (Haynes et al, 1997;Kajiya et al, 1997). Interestingly, it has been reported that elastin mRNA expression is increased after UV exposure in the epidermal layers (Seo et al, 2001).…”

Section: Discussionmentioning

confidence: 99%

Lysyl Oxidase-Like and Lysyl Oxidase Are Present in the Dermis and Epidermis of a Skin Equivalent and in Human Skin and Are Associated to Elastic Fibers

Noblesse

Cenizo

Bouez

et al. 2004

Journal of Investigative Dermatology

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Elastic fiber formation involves the secretion of tropoelastin which is converted to insoluble elastin by cross-linking, initiated by the oxidative deamination of lysine residues by lysyl oxidase. Five lysyl oxidase genes have been discovered. This study deals with the expression of two isoforms, LOX and LOX-like (LOXL), in human foreskin and in a human skin-equivalent (SE) model that allows the formation of elastic fibers. In this model, keratinocytes are added to a dermal equivalent made of fibroblasts grown on a chitosan-cross-linked collagen-GAG matrix. LOX and LOXL were detected by immunohistochemistry in the dermis and the epidermis of both normal skin and in a SE. This expression was confirmed by in situ hybridization on the SE. LOX and LOXL expression patterns were confirmed in human skin. The ultrastructural localization of LOXL was indicative of its association with elastin-positive materials within the SE and human skin, though interaction with collagen could not be discarded. LOX was found on collagen fibers and could be associated with elastin-positive materials in the SE and human skin. LOXL and LOX were detected in keratinocytes where LOX was mainly expressed by differentiating keratinocytes, in contrast to LOXL that can be found in both proliferating and differentiating fibroblasts. These data favor a role for LOXL in elastic fiber formation, together with LOX, and within the epidermis where both enzymes should play a role in post-translational modification of yet unknown substrates.

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“…Since elastin and Fib-1 have been shown to be expressed by cultured keratinocytes [12,13], our findings indicate that keratinocytes potentially produce the three major components of elastic fibers (elastin, Fib-1 and MAGP-1) which are thought to be necessary to form the elastic fiber network.…”

Section: Discussionmentioning

confidence: 66%

“…Recently both proteins have been shown to be expressed by keratinocytes [12,13]. We studied the expression of MAGP-1 in cultured human keratinocytes and the localization of MAGP-1-immunoreactive fibers in the upper dermis.…”

Section: Introductionmentioning

confidence: 99%

Expression of microfibril-associated glycoprotein-1 (MAGP-1) in human epidermal keratinocytes

2000

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Microfibril-associated glycoprotein (MAGP) is a major structural component of connective tissue microfibrils. We studied the expression of MAGP-1 in cultured human keratinocytes and its modulation during Ca(++)-induced differentiation. RT-PCR and Western blot assays demonstrated the presence of mRNA and the polypeptide of MAGP-1 in cultured keratinocytes. MAGP-1 mRNA levels in cultured keratinocytes during Ca(++)-induced differentiation were enhanced eightfold with a concomitant increase in involucrin (a marker of terminal differentiation) mRNA levels. Double immunofluorescence labeling of cultured keratinocytes demonstrated that both anti-MAGP-1 and anti-involucrin antibodies reacted with the identical cells. The population of MAGP-1-producing cells in cultured keratinocytes significantly increased during Ca(++)-induced differentiation. These results indicate that MAGP-1 expressed by cultured keratinocytes reaches maximum levels at the stage of terminal differentiation in vitro. Double immunostaining of normal human skin with anti-MAGP-1 and anti-elastin antibodies demonstrated the colocalization of MAGP-1-positive and elastin-positive fibers in the superficial and mid-dermis. MAGP-1 produced by keratinocytes may play some functional role in the formation of dermal matrix organization in the dermis.

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Cultured Human Keratinocytes Express Tropoelastin

Cited by 28 publications

References 33 publications

Differential Regulation of MMP-2 and MMP-9 Gelatinases in Cultured Human Keratinocytes

Differential Regulation of MMP-2 and MMP-9 Gelatinases in Cultured Human Keratinocytes

Lysyl Oxidase-Like and Lysyl Oxidase Are Present in the Dermis and Epidermis of a Skin Equivalent and in Human Skin and Are Associated to Elastic Fibers

Expression of microfibril-associated glycoprotein-1 (MAGP-1) in human epidermal keratinocytes

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