A protein reminiscent of the epidermal SH-protease inhibitor occurs in squamous epithelia of man and rat

Rinne, Ari; Järvinen, M.; Räsänen, O

doi:10.1016/s0065-1281(78)80024-5

Cited by 53 publications

(13 citation statements)

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“…In this study we have used rabbit antisera made against the purified inhibitors of Atlantic salmon for immunohistochemical localization studies. Cysteine proteinase inhibitors have been shown to localize to squamous epithelial cells and lymphatic tissues in mammalian species (Rinne et al 1978;Davies and Barrett 1984). Cystatin A has been demonstrated in the cytosol by immunoelectron microscopy (Rinne et al 1986b).…”

Section: Discussionmentioning

confidence: 99%

“…Family 1 of the cystatin superfamily, the stefins, (for example, cystatin A), are located in high levels in the skin, tongue, esophagus, and stomach of the rat . Cystatin A has been immunohistochemically located to various types of squamous epithelial cells and dendritic reticulum cells (Rinne et al 1978(Rinne et al , 1983. Also, cystatin A is present in various body fluids such as amniotic fluid and tears (Abrahamson et al 1986).…”

Section: Introductionmentioning

confidence: 99%

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Immunolocalization of cysteine proteinases (cathepsins) and cysteine proteinase inhibitors (salarin and salmon kininogen) in Atlantic salmon, Salmo salar

Tähtinen

Weber

Günther

et al. 2002

Cell and Tissue Research

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Tissue localization of cysteine proteinases (cathepsins) and their inhibitors (salarin, salmon kininogen) was performed in tissues of the Atlantic salmon. In skin, both epidermis and dermis were strongly stained by antisera against salarin and salmon kininogen. In epidermis the intercellular space seemed to be heavily stained (salarin). In kidney, the inhibitors were mainly localized to the interstitial capillaries. Also, some epithelial cells of the tubules (salarin) and some cells of the interstitium were stained. Mostly, the staining had a diffuse cytoplasmic localization. In the liver some hepatocytes were strongly positive for salarin and salmon kininogen. Purified fish cysteine proteinase inhibitors were not found to inhibit the growth of fish pathogenic bacteria and viruses. In the trunk kidney cathepsins B and L were localized in epithelial cells of the tubules (proximal part) and in cells of the interstitium. Mostly, the staining showed a prominent lysosomal localization. In head kidney large macrophage-like cells were positively stained for cathepsin B. The staining was localized to granula/vacuoles in the cytoplasm. In the liver, some hepatocytes were strongly stained and some were less strongly positive for cathepsin B and L. Mostly, the hepatocytes showed lysosomal staining. Cathepsin L was found in some big macrophage-like cells in the spleen. Mucosal epithelial cells of the esophagus and intestine seemed to be strongly stained for cathepsin B and L. The results show that cathepsins and their inhibitors are specifically and widely distributed in the Atlantic salmon skin indicating that they perform some biologically important and specific but so far unknown functions.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Immunolocalization of cysteine proteinases (cathepsins) and cysteine proteinase inhibitors (salarin and salmon kininogen) in Atlantic salmon, Salmo salar

Tähtinen

Weber

Günther

et al. 2002

Cell and Tissue Research

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“…Cystatin A (type 1) was isolated from rat skin (Järvinen & Hopsu-Havu, 1975). It is expressed abundantly in the squamous epithelium of tissues (Rinne et al, 1978;Kominami et al, 1984). Thus, cystatin A is found in tissues protecting against exogenous factors (bacteria and viruses).…”

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confidence: 99%

The cysteine protease inhibitors cystatins inhibit herpes simplex virus type 1-induced apoptosis and virus yield in HEp-2 cells

Peri

Hukkanen

Nuutila

et al. 2007

Journal of General Virology

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The role of cystatins in herpes simplex virus (HSV)-induced apoptosis and viral replication has been studied. Human epithelial (HEp-2) cells infected with wild-type HSV-1 (F), with a deletion virus lacking the anti-apoptotic gene Us3 (R7041) or with a deletion virus lacking the anti-apoptotic genes Us3 and ICP4 (d120) were treated with cystatin A, C or D. Cells and culture media were studied at different time points for replicating HSV-1 and for apoptosis. Cystatins C and D inhibited the yield of replicative HSV-1 significantly in HEp-2 cells. In addition, cystatin D inhibited R7041 and d120 virus-induced apoptosis. Moreover, cystatin A inhibited R7041-induced apoptosis. These inhibitory effects of cystatins on virus replication and apoptosis are likely to be separate functions. Cystatin D treatment decreased cellular cathepsin B activity in HSV-1 infection, suggesting that cathepsin B is involved in virus-induced apoptosis.

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“…ACPI and its antiserum were prepared as described by Jarvinen (1978). The criteria for purity of the antigen and specificity of the antiserum are those of Rinne er al.…”

Section: Lmmunocytochemistry Of Acpimentioning

confidence: 99%

“…This type of approach includes the recent finding that in human lymphoid secondary follicles, in both lymph nodes and tonsillar tissue, DRC express one type of immunoreactive cysteine-proteinase inhibitor, namely acid cysteine-proteinase inhibitor (ACPI) (Rinne et al, 1981(Rinne et al, , 1983; Alavaikko et al, in press). Its biochemical characteristics include: molecular weight 12,000, isoelectric point 4.6-5.0, heat stability and inhibition of cathepsins B and H, papain, ficin and bromelain (Jarvinen, 1978;Jarvinen and Rinne, 1982). It is of particular interest that ACPI was originally isolated and purified from human epidermis (Jarvinen, 1978) and seems to be a constant characteristic of human squamous epithelia (Rinne et al, 1978).…”

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confidence: 99%

Behaviour of dendritic reticulum cells possessing immunoreactive acid cysteine‐proteinase inhibitor in human lymphoid secondary follicles and in follicular‐centre cell lymphomas

Alavaikko

Aine

Rinne

et al. 1985

Intl Journal of Cancer

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In our previous studies acid cysteine-proteinase inhibitor (ACPI) was shown to be a common characteristic of human squamous epithelia and dendritic reticulum cells (DRC) in lymphoid secondary follicles. In the present study, the behaviour of ACPI-immunoreactive DRC in reactive lymphoid secondary follicles and neoplastic follicles of follicular-centre cell (FCC) lymphomas was compared by the peroxidase-antiperoxidase method. The secondary follicles in reactive lymphoid tissues revealed a staining pattern characteristic of DRC comparable with the results of other studies. Contrary to this, the number of ACPI-positive DRC in the neoplastic lymphoid follicles was greatly reduced. This was occasionally accompanied by a weak reaction and in many cases the DRC were totally abolished. Moreover, morphological aberrations were observed in ACPI-positive DRC, especially diminution and shortening of dendritic processes. On occasion, ACPI-positive cell types were observed, which may represent intermediate forms between DRC and fibroblastic reticulum cells. Only one case--with a rather favourable clinical outcome (out of 41 follicular FCC lymphomas) exhibited an ACPI-positive DRC pattern comparable with that of reactive lymphoid follicles. Thus it seems that the ACPI-immunohistochemistry of DRC provides an additional tool for discerning the difference between reactive and neoplastic lymphoid follicles. This method is of particular value since it can be used with formalin-fixed, paraffin-embedded tissues. There was a tendency among the follicular FCC lymphoma patients towards a better survival rate for those with ACPI-positive DRC than for those lacking this cell type, although no statistically significant differences emerged from this limited material.

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A protein reminiscent of the epidermal SH-protease inhibitor occurs in squamous epithelia of man and rat

Cited by 53 publications

References 12 publications

Immunolocalization of cysteine proteinases (cathepsins) and cysteine proteinase inhibitors (salarin and salmon kininogen) in Atlantic salmon, Salmo salar

Immunolocalization of cysteine proteinases (cathepsins) and cysteine proteinase inhibitors (salarin and salmon kininogen) in Atlantic salmon, Salmo salar

The cysteine protease inhibitors cystatins inhibit herpes simplex virus type 1-induced apoptosis and virus yield in HEp-2 cells

Behaviour of dendritic reticulum cells possessing immunoreactive acid cysteine‐proteinase inhibitor in human lymphoid secondary follicles and in follicular‐centre cell lymphomas

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