Immunohistochemical localization of lysyl oxidase in normal human skin

Kobayashi, Hiromi; Chanoki, Miyako; Fushida, Hiroyo; Yashiro, Noriko; Fukai, Kazuyoshi; Maekawa, Naoki; Kono, Toru; Ishii, Masamitsu; Hamada, Toshio; Ooshima, Akira

doi:10.1016/0923-1811(91)90214-i

Cited by 10 publications

(10 citation statements)

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“…Our immunohistochemical data was largely consistent with previously published localizations of LOX monoclonal antibodies in human tissues (Wakashima and Ooshima 1990, Kobayashi et al 1994). Our LOX antibody was primarily localized to connective tissue where fibrillar collagens and elastin are found.…”

Section: Discussionsupporting

confidence: 91%

Comparative immunocytochemical localization of lysyl oxidase (LOX) and the lysyl oxidase-like (LOXL) proteins: changes in the expression of LOXL during development and growth of mouse tissues

et al. 2004

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Lysyl oxidase (LOX) and lysyl oxidase-like (LOXL) are extracellular enzymes that deaminate peptidyl lysyl residues involved in the cross-linking of fibrillar collagens and elastin. While LOX is required for the survival of newborn mice, the role of LOXL during development remains unclear. Studies have shown that the same cell types express LOX and LOXL in the same tissues, but no functional differences have been established. We have compared the immunohistochemical localization of LOX and LOXL in various tissues from normal, young adult mice. LOX and LOXL were co-localized in the skin, aorta, heart, lung, liver and cartilage, but were localized to different areas in the kidney, stomach, small intestine, colon, retina, ovary, testis and brain. LOXL expression was further examined in tissues from different developmental stages. In embryonic mice (10.5-14.5 dpc), LOXL immunostaining was abundant in the heart, liver, intestine, and neural tube. LOXL was present in most major organs in late fetal (16.5 dpc) and newborn mice, but generally diminished as animals aged. Immunoreactivity was significantly reduced in the heart, lung, kidney and liver of 2 year-old mice, but remained prevalent in the skin and tongue. LOX and LOXL were also found in the nuclei of cells in a number of tissues. These results indicate that LOXL has a role during mouse development and in the maintenance of adult tissues.

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Section: Discussionsupporting

confidence: 91%

Comparative immunocytochemical localization of lysyl oxidase (LOX) and the lysyl oxidase-like (LOXL) proteins: changes in the expression of LOXL during development and growth of mouse tissues

et al. 2004

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“…Macrophages are good candidates, since cells with the same localization and morphology have been shown to express IL-1b, IL-6, and tumor necrosis factor (TNF)-a messenger RNAs as well as macrophage markers in human AE (Bresson-Hadni et al 1994b). Expression of lysyl oxidase has been shown in a variety of cell types (Kobayashi et al 1994;Wakasaki and Ooshima 1990) and, thus, no other cell present in the liver and/or liver in®ltrates can be ruled out without further characterization.…”

Section: Discussionmentioning

confidence: 99%

Echinococcus multilocularis: relationship between susceptibility/ resistance and liver fibrogenesis in experimental mice

Guérret

Vuitton

Liance

et al. 1998

Parasitology Research

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To analyze collagen and other matrix protein deposits in experimental alveolar echinococcosis as well as the expression of lysyl oxidase, the enzyme that initiates the first steps in the pyridinoline cross-linking of collagen, and to establish a relationship between resistance/susceptibility to Echinococcus multilocularis larval growth and fibrogenesis, we compared AKR/J mice (susceptible to E. multilocularis infection) with NMRI mice (resistant hosts) in this study. Collagen deposits in the lesions were evaluated using a colorimetric method; the nature of matrix proteins involved in the periparasitic fibrosis and lysyl oxidase expression were assessed using immunostaining on tissue sections. The results obtained in this sequential study confirm that fibrogenesis is an important aspect of the host immune reaction against parasitic development and that both the extent and the course of matrix protein deposition differ in the liver of susceptible and resistant mice, respectively. The long-lasting expression of alpha-actin and lysyl oxidase by host cells in NMRI mice suggests that in this resistant strain, fibrosis was not only more developed but also more highly cross-linked and, thus, less sensitive to collagenases than in susceptible mice. A very strong expression of lysyl oxidase by parasitic cells was observed in both strains of mice; the observation that E. multilocularis itself has a role in lysyl oxidase cross-linking of host collagens can be hypothesized and would be a new example of parasite-host interplay.

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“…6,11 HLA content in the dermis decreases as it is produced less by fibroblasts and disappears altogether in the epidermis as a function of age. 12 HLA synthesized in the dermis also sees a decrease in the size of the GAG chain. 3 Both collagen and elastin undergo enzymatic and nonenzymatic cross-links in the ECM as a function of aging 13,14 ( Figure 2).…”

Section: Ahmed Et Almentioning

confidence: 99%

Combining nano-physical and computational investigations to understand the nature of “aging” in dermal collagen

Ahmed¹,

Nash²,

Clark³

et al. 2017

IJN

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The extracellular matrix of the dermis is a complex, dynamic system with the various dermal components undergoing individual physiologic changes as we age. Age-related changes in the physical properties of collagen were investigated in particular by measuring the effect of aging, most likely due to the accumulation of advanced glycation end product (AGE) cross-links, on the nanomechanical properties of the collagen fibril using atomic force microscope nano-indentation. An age-related decrease in the Young’s modulus of the transverse fibril was observed (from 8.11 to 4.19 GPa in young to old volunteers, respectively, P <0.001). It is proposed that this is due to a change in the fibril density caused by age-related differences in water retention within the fibrils. The new collagen–water interaction mechanism was verified by electronic structure calculations, showing it to be energetically feasible.

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Immunohistochemical localization of lysyl oxidase in normal human skin

Cited by 10 publications

References 1 publication

Comparative immunocytochemical localization of lysyl oxidase (LOX) and the lysyl oxidase-like (LOXL) proteins: changes in the expression of LOXL during development and growth of mouse tissues

Comparative immunocytochemical localization of lysyl oxidase (LOX) and the lysyl oxidase-like (LOXL) proteins: changes in the expression of LOXL during development and growth of mouse tissues

Echinococcus multilocularis: relationship between susceptibility/ resistance and liver fibrogenesis in experimental mice

Combining nano-physical and computational investigations to understand the nature of “aging” in dermal collagen

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Immunohistochemical localization of lysyl oxidase in normal human skin

Cited by 10 publications

References 1 publication

Comparative immunocytochemical localization of lysyl oxidase (LOX) and the lysyl oxidase-like (LOXL) proteins: changes in the expression of LOXL during development and growth of mouse tissues

Comparative immunocytochemical localization of lysyl oxidase (LOX) and the lysyl oxidase-like (LOXL) proteins: changes in the expression of LOXL during development and growth of mouse tissues

Echinococcus multilocularis: relationship between susceptibility/ resistance and liver fibrogenesis in experimental mice

Combining nano-physical and computational investigations to understand the nature of &ldquo;aging&rdquo; in dermal collagen

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Combining nano-physical and computational investigations to understand the nature of “aging” in dermal collagen