Expression of 36-kDa microfibril-associated glycoprotein (MAGP-36) in human keratinocytes and its localization in skin

Hirano, Eiichi; Fujimoto, Norihiro; Tajima, S.; Akiyama, Minoru; Ishibashi, Akira; Kobayashi, Ryōji; Okamoto, Kouji

doi:10.1016/s0923-1811(01)00148-7

Cited by 20 publications

(15 citation statements)

References 35 publications

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“…Skin punch biopsies from the ventral upper arms of healthy Caucasian females in their twenties and fifties were also used for total RNA extraction. Quantitative RT-PCR analysis showed that expression of MFAP-4 was significantly lower in the photoaging skin model, which is consistent with a previous report40 (Fig. 1a).…”

Section: Resultssupporting

confidence: 93%

“…Those reports are of great importance to comprehend the mechanisms underlying the construction of elastic fibers, whereas it remains to be determined how many other molecules are involved in elastogenesis to completely understand the process of elastic fiber formation. For example, MAGP-36, a homologue of MFAP-4 detected around elastic fibers in various animals, was reported to have disappeared in photoaged dermis but accumulated in disintegrated elastic fibers in the lesional skin of pseudoxanthoma elasticum, an elastin-related disorder40. These findings encouraged us to explore the function of MFAP-4 in human skin using an in vivo photodamaged/photoaged skin model with human skin xenografted on SCID mice in concert with a lentiviral vector to over-express MFAP-4 as well as in vitro NHDFs combined with siRNA technology.…”

Section: Discussionmentioning

confidence: 99%

“…An immunohistochemical study demonstrated that MAGP-36, which is localized around elastic fibers in the rat aorta and is rich in elastin-associated microfibrils, had disappeared in photoaged dermis and could be found in the accumulation of disintegrated elastic fibers in the lesional skin of pseudoxanthoma elasticum, an elastin-related disorder40. That report strongly suggested that MAGP-36 is a microfibrilar-associated protein, although little is known about its role(s) in human elastic tissues.…”

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confidence: 99%

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Essential role of microfibrillar-associated protein 4 in human cutaneous homeostasis and in its photoprotection

Kasamatsu

Hachiya

Fujimura

et al. 2011

Sci Rep

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UVB-induced cutaneous photodamage/photoaging is characterized by qualitative and quantitative deterioration in dermal extracellular matrix (ECM) components such as collagen and elastic fibers. Disappearance of microfibrillar-associated protein 4 (MFAP-4), a possible limiting factor for cutaneous elasticity, was documented in photoaged dermis, but its function is poorly understood. To characterize its possible contribution to photoprotection, MFAP-4 expression was either augmented or inhibited in a human skin xenograft photodamage murine model and human fibroblasts. Xenografted skin with enhanced MFAP-4 expression was protected from UVB-induced photodamage/photoaging accompanied by the prevention of ECM degradation and aggravated elasticity. Additionally, remarkably increased or decreased fibrillin-1-based microfibril development was observed when fibroblasts were treated with recombinant MFAP-4 or with MFAP-4-specific siRNA, respectively. Immunoprecipitation analysis confirmed direct interaction between MFAP-4 and fibrillin-1. Taken together, our findings reveal the essential role of MFAP-4 in photoprotection and offer new therapeutic opportunities to prevent skin-associated pathologies.

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Section: Resultssupporting

confidence: 93%

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

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Essential role of microfibrillar-associated protein 4 in human cutaneous homeostasis and in its photoprotection

Kasamatsu

Hachiya

Fujimura

et al. 2011

Sci Rep

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“…[6][7][8][9][10] MAGP36 is known to interact directly with ECM fibers, including elastin, collagen, and calvasculin. [6][7][8]11 Moreover, MAGP36 was demonstrated to bind integrin receptors on human aortic SMCs in an RGD-dependent manner.…”

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confidence: 97%

MFAP4 Promotes Vascular Smooth Muscle Migration, Proliferation and Accelerates Neointima Formation

Schlosser¹,

Pilecki²,

Hemstra³

et al. 2016

ATVB

101

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V ascular smooth muscle cell (VSMC) activation and phenotypic switching are critical for remodeling processes in vascular proliferative disorders, including intimal hyperplasia. Both the migratory and proliferative activities of VSMCs, as well as the interplay between the extracellular matrix (ECM) and integrin receptors essentially, contribute to neointimal hyperplasia and restrictive remodeling processes in the vessels.1 Among integrins, the particular role of integrin α V β 3 in the induction of VSMC responses has been shown both in vivo and in vitro.

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“…It has been hypothesized that MFAP4 plays a role in maintaining the integrity of the extracellular matrix (ECM) in organs of high tensile strength, such as the aorta (45), in elastogenesis and elastic fiber formation (15,20,46), and in skin photoprotection, e.g., through interactions with fibrillin (17,20). Moreover, in silico studies have recently predicted that Mfap4 Ϫ/Ϫ mice might develop pulmonary emphysema (4) and circulating levels of MFAP4 are associated to the severity in chronic obstructive lung disease, indicative for a role in disease (19).…”

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confidence: 99%

Characterization of spontaneous air space enlargement in mice lacking microfibrillar-associated protein 4

Holm

Wulf-Johansson

Hvidsten

et al. 2015

American Journal of Physiology-Lung Cellular and Molecular Phys

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protein 4 (MFAP4) is localized to elastic fibers in blood vessels and the interalveolar septa of the lungs and is further present in bronchoalveolar lavage. Mfap4 has been previously suggested to be involved in elastogenesis in the lung. We tested this prediction and aimed to characterize the pulmonary function changes and emphysematous changes that occur in Mfap4-deficient (Mfap4 Ϫ/Ϫ ) mice. Significant changes included increases in total lung capacity and compliance, which were evident in Mfap4 Ϫ/Ϫ mice at 6 and 8 mo but not at 3 mo of age. Using in vivo breath-hold gated microcomputed tomography (micro-CT) in 8-mo-old Mfap4 Ϫ/Ϫ mice, we found that the mean density of the lung parenchyma was decreased, and the low-attenuation area (LAA) was significantly increased by 14% compared with Mfap4 ϩ/ϩ mice. Transmission electron microscopy (TEM) did not reveal differences in the organization of elastic fibers, and there was no difference in elastin content, but a borderline significant increase in elastin mRNA expression in 3-mo-old mice. Stereological analysis showed that alveolar surface density in relation to the lung parenchyma and total alveolar surface area inside of the lung were both significantly decreased in Mfap4 Ϫ/Ϫ mice by 25 and 15%, respectively. The data did not support an essential role of MFAP4 in pulmonary elastic fiber organization or content but indicated increased turnover in young Mfap4 Ϫ/Ϫ mice. However, Mfap4 Ϫ/Ϫ mice developed a spontaneous loss of lung function, which was evident at 6 mo of age, and moderate air space enlargement, with emphysema-like changes.air space enlargement; gene deficiency; MFAP4 MFAP4 IS A 36-KDA GLYCOPROTEIN composed of a short NH 2 -terminal region comprising one cysteine residue and an ArgGly-Asp (RGD) integrin-binding motif, followed by a COOHterminal fibrinogen-related domain (FReD) (51). The MFAP4 protein is a disulfide-linked dimer that forms higher homooligomeric structures via noncovalent interactions (26,38). FReDs are found in various human proteins involved in distinct functions, including innate immunity, tissue growth, and remodeling (43).MFAP4 is considered to be the human homolog to a 36-kDa microfibril-associated glycoprotein (MAGP-36) originally found to be localized to the elastin-microfibril interface in the porcine aorta (23). MFAP4 was later detected in a variety of both elastic and nonelastic tissues in various species

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Expression of 36-kDa microfibril-associated glycoprotein (MAGP-36) in human keratinocytes and its localization in skin

Cited by 20 publications

References 35 publications

Essential role of microfibrillar-associated protein 4 in human cutaneous homeostasis and in its photoprotection

Essential role of microfibrillar-associated protein 4 in human cutaneous homeostasis and in its photoprotection

MFAP4 Promotes Vascular Smooth Muscle Migration, Proliferation and Accelerates Neointima Formation

Characterization of spontaneous air space enlargement in mice lacking microfibrillar-associated protein 4

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