Cathepsin D expression in chronic plaque psoriasis: An immunohistochemical study

dc.AffiliationOctober University for modern sciences and Arts (MSA)
dc.contributor.authorAbdou A.G.
dc.contributor.authorMaraee A.H.
dc.contributor.authorShoeib M.A.E.
dc.contributor.authorElsammie A.A.A.
dc.contributor.authorElnaidany N.F.
dc.contributor.otherPathology Department
dc.contributor.otherMenofiya University
dc.contributor.otherShebein Elkom
dc.contributor.otherEgypt; Dermatology and Andrology Department
dc.contributor.otherFaculty of Medicine
dc.contributor.otherMenofiya University
dc.contributor.otherShebein Elkom
dc.contributor.otherEgypt; Clinical Pharmacy Department
dc.contributor.otherFaculty of Pharmacy
dc.contributor.otherMSA University
dc.contributor.otherOctober City
dc.contributor.otherEgypt
dc.date.accessioned2020-01-25T19:58:29Z
dc.date.available2020-01-25T19:58:29Z
dc.date.issued2011
dc.descriptionScopus
dc.description.abstractCathepsins are lysosomal cysteine proteases, which are involved in a variety of physiologic processes such as proenzyme activation, antigen presentation, tissue remodeling, bone matrix resorption, and pathologic processes such as facilitating tumor invasion and modulating the process of programmed cell death. This study aimed to evaluate the pattern of cathepsin D (CD) expression in chronic plaque psoriasis in comparison to normal skin by means of immunohistochemistry. The study included 34 patients presenting with chronic plaque psoriasis and 10 ageand sex-matched normal subjects as control group. Sixty percent of normal skin showed granular positivity for CD confined to basal layer. CD is upregulated in psoaritic lesion with 94.1% positivity making a significant difference between psoriasis and normal skin as regards the percentage and distribution of CD expression, where the latter was predominantly diffuse in psoriatic lesion. The eight cases exposed to PUVA therapy showed reduction of CD positivity to 62.5% with a predominance of mild staining and focal expression compared to pretreatment biopsies. CD may have a role in the pathogenesis of psoriasis in view of its high percentage and diffuse expression in psoriatic epidermis. CD degradative capacity may be responsible for disordered differentiation and scale formation characteristic of psoriasis. Reduction of CD expression may be one of the pathways of PUVA mechanism of action.en_US
dc.description.urihttps://www.scimagojr.com/journalsearch.php?q=24217&tip=sid&clean=0
dc.identifier.doihttps://doi.org/
dc.identifier.issn1330027X
dc.identifier.otherhttps://doi.org/
dc.identifier.urihttps://t.ly/2ddPR
dc.language.isoEnglishen_US
dc.relation.ispartofseriesActa Dermatovenerologica Croatica
dc.relation.ispartofseries19
dc.subjectCathepsin Den_US
dc.subjectImmunohistochemistryen_US
dc.subjectProteasesen_US
dc.subjectPsoriasisen_US
dc.subjectcathepsin Den_US
dc.subjectmethoxsalenen_US
dc.subjectadolescenten_US
dc.subjectadulten_US
dc.subjectageden_US
dc.subjectarticleen_US
dc.subjectchilden_US
dc.subjectchronic diseaseen_US
dc.subjectchronic psoriasis vulgarisen_US
dc.subjectclinical articleen_US
dc.subjectcontrolled studyen_US
dc.subjectfemaleen_US
dc.subjecthumanen_US
dc.subjecthuman tissueen_US
dc.subjectimmunohistochemistryen_US
dc.subjectmaleen_US
dc.subjectprotein expressionen_US
dc.subjectpsoriasis vulgarisen_US
dc.subjectPUVAen_US
dc.subjectschool childen_US
dc.subjectskin biopsyen_US
dc.subjectAdolescenten_US
dc.subjectAdulten_US
dc.subjectAgeden_US
dc.subjectCathepsin Den_US
dc.subjectChilden_US
dc.subjectChronic Diseaseen_US
dc.subjectFemaleen_US
dc.subjectHumansen_US
dc.subjectImmunohistochemistryen_US
dc.subjectMaleen_US
dc.subjectMiddle Ageden_US
dc.subjectPsoriasisen_US
dc.subjectPUVA Therapyen_US
dc.subjectSkinen_US
dc.subjectYoung Adulten_US
dc.titleCathepsin D expression in chronic plaque psoriasis: An immunohistochemical studyen_US
dc.typeArticleen_US
dcterms.isReferencedByStuart, P., Malick, F., Nair, R.P., Henseler, T., Lim, H.W., Jenisch, S., Analysis of phenotypic variation in psoriasis as a function of age at onset and family history (2002) Arch Dermatol Res, 294, pp. 207-213; Krueger, G.G., Langley, R.G., Leonardi, C., Yeilding, N., Guzzo, C., Wang, Y., A human interleukin-12/23 monoclonal antibody for the treatment of psoriasis (2007) N Engl J Med, 356, pp. 580-592; Dickinson, D.P., Cysteine peptidases of mammals: Their biological roles and potential effects in the oral cavity and other tissues in health and disease (2002) Crit Rev Oral Biol Med, 13, pp. 238-275; Turk, B., Stoka, V., Rozman-Pungercar, J., Cirman, T., Droga-Mazovec, G., Oreic, K., Apoptotic pathways: Involvement of lysosomal proteases (2002) Biol Chem, 383, pp. 1035-1044; Hopkins, A.L., Groom, C.R., The druggable genome (2002) Nat Rev Drug Discov, 1, pp. 727-730; Tang, J., Wong, R.N., Evolution in the structure and function of aspartic proteases (1987) J Cell Biochem, 33, pp. 53-63; Hsueh, W.A., Baxter, J.D., (1991) Human Prorenin. Hypertension, 17, pp. 469-477; Sato, K., Waguri, S., Nitatori, T., Kon, S., Kominami, E., Watanabe, T., Immunocytochemical localization of lysosomal cysteine and aspartatic proteinases, and ubiquitin in rat epidermis (1997) Arch Histol Cytol, 30, pp. 275-287; Kawada, A., Hara, K., Kominami, E., Hiruma, M., Noguchi, H., Ishibashi, A., Processing of cathepsins L, B and D in psoriatic epidermis (1997) Arch Dermatol Res, 289, pp. 87-93; Horikoshi, T., Igarishi, S., Uchiwa, H., Brysk, H., Brysk, M.M., Role of endogenous cathepsin D-like and chymotrypsin-like proteolysis in human epidermal desquamation (1999) Br J Dermatol, 141, pp. 453-459; Serre, G., Mils, V., Haftek, M., Vincent, C., Croute, F., R�ano, A., Identification of late differentiation antigens of human cornified epithelia, expressed in reorganized desmosomes and bound to cross-linked envelope (1991) J Invest Dermatol, 97, pp. 1061-1072; Igarashi, S., Takizawa, T., Takizawa, T., Yasuda, Y., Uchiwa, H., Hayashi, S., Cathepsin D, but not cathepsin E, degrades desmosomes during epidermal desquamation (2004) Br J Dermatol, 151, pp. 355-361; Lazarus, G.S., Poole, R., Immunocytochemical localization of cathepsin D in rabbit skin (1975) Arch Dermatol, 111, pp. 1150-1153; Horikoshi, T., Arany, I., Rajaraman, S., Chen, S.-H., Brysk, H., Lei, G., Isoforms of cathepsin D and human epidermal differentiation (1998) Biochimie (Paris), 80, pp. 605-612; Egberts, F., Heinrich, M., Jensen, J.M., Cathepsin D is involved in the regulation of transglutaminase 1 and epidermal differentiation (2004) J Cell Sci, 117, pp. 2295-2307; Vashishta, A., Saraswat Ohri, S., Vetvickova, J., Fusek, M., Ulrichova, J., Vetvicka, V., Procathepsin D secreted by HaCaT keratinocyte cells - a novel regulator of keratinocyte growth (2007) Eur J Cell Biol, 86, pp. 303-313; Rice, R.H., Green, H., Presence in human epidermal cells of a soluble protein precursor of the crosslinked envelope: Activation of the cross-linking by calcium ions (1979) Cell, 18, pp. 681-694; Dover, R., Watt, F.M., Measurement of the rate of epidermal terminal differentiation: Expression of involucrin by S-phase keratinocytes in culture and in psoriatic plaques (1987) J Invest Dermatol, 89, pp. 349-352; Watt, F.M., Boukamp, P., Hornung, J., Fusenig, N.E., Effect of growth environment on spatial expression of involucrin by human epidermal keratinocytes (1987) Arch Dermatol Res, 279, pp. 335-340; Negi, M., Matsui, T., Ogawa, H., Mechanism of human epidermal transglutaminase (1981) J Invest Dermatol, 77, pp. 389-392; Chen, S.H., Arany, I., Apisarnthanarax, N., Rajaraman, S., Tyring, S.K., Horikoshi, T., Response of keratinocytes from normal and psoriatic epidermis to interferon- gamma differs in the expression of zincalpha(2)-glycoprotein and cathepsin D (2000) FASEB J, 14, pp. 565-571; Minarowska, A., Gacko, M., Karwowska, A., Minarowski, L., Human cathepsin D (2008) Folia Histochem Cytobiol, 46, pp. 23-38; Berchem, G.J., Glondu, M., Gleizes, M., Brouillet, J.P., Garcia, M., Liaudet-Coopman, E., Cathepsin-D affects multiple steps of tumor progression: Proliferation, angiogenesis and apoptosis (2002) Oncogene, 21, pp. 5951-5955; Abdou, A.G., Hanout, H.M., Evaluation of survivin and NF-kappaB in psoriasis, an immunohistochemical study (2008) J Cutan Pathol, 35, pp. 445-451; Gonzlez-Vela, M.C., Garijo, M.F., Fernndez, F., Buelta, L., Val-Bernal, J.F., Cathepsin D in host stromal cells is associated with more highly vascular and aggressive invasive breast carcinoma (1999) Histopathology, 34, pp. 35-42; Lsch, A., Schindl, M., Kohlberger, P., Lahodny, J., Breitenecker, G., Horvat, R., Cathepsin D in ovarian cancer: Prognostic value and correlation with p53 expression and microvessel density (2004) Gynecol Oncol, 92, pp. 545-552; Briozzo, P., Badet, J., Capony, F., Pieri, I., Montcourrier, P., Barritault, D., MCF7 mammary cancer cells respond to bFGF and internalize it following its release from extracellular matrix: A permissive role of cathepsin D (1991) Exp Cell Res, 194, pp. 252-259; Piwnica, D., Fernandez, I., Binart, N., Touraine, P., Kelly, P.A., Goffin, V., A new mechanism for prolactin processing into 16K PRL by secreted cathepsin D (2006) Mol Endocrinol, 20, pp. 3263-3278; Vallat, V.P., Gilleaudeau, P., Battat, L., Wolfe, J., Nabeya, R., Heftler, N., PUVA bath therapy strongly suppresses immunological and epidermal activation in psoriasis: A possible cellular basis for remittive therapy (1994) J Exp Med, 180, pp. 283-296
dcterms.sourceScopus

Files

Original bundle

Now showing 1 - 2 of 2
Loading...
Thumbnail Image
Name:
avatar_scholar_256.png
Size:
6.31 KB
Format:
Portable Network Graphics
Description:
Loading...
Thumbnail Image
Name:
Cathepsin_D_Expression_in_Chronic_Plaque_Psoriasis.pdf
Size:
293.29 KB
Format:
Adobe Portable Document Format
Description: