1992
DOI: 10.1111/1523-1747.ep12616087
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Identification and Characterization of a Cell Surface Proteoglycan on Keratinocytes

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Cited by 55 publications
(52 citation statements)
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“…To this end, application of various doses of sTat in combination with CT onto bare skin elicited robust anti-sTat antibody responses. These findings are consistent, i) with the property of Tat to enter into cells [7] and particularly with its capacity to bind to polyanionic glycosaminoglycan heparin sulfate that is present in the epidermis [22,23] and, ii) with the demonstration that ADP-ribosylating exotoxins like CT exert an adjuvant effect to transcutaneously co-delivered antigens [11].…”
Section: Discussionsupporting
confidence: 77%
See 1 more Smart Citation
“…To this end, application of various doses of sTat in combination with CT onto bare skin elicited robust anti-sTat antibody responses. These findings are consistent, i) with the property of Tat to enter into cells [7] and particularly with its capacity to bind to polyanionic glycosaminoglycan heparin sulfate that is present in the epidermis [22,23] and, ii) with the demonstration that ADP-ribosylating exotoxins like CT exert an adjuvant effect to transcutaneously co-delivered antigens [11].…”
Section: Discussionsupporting
confidence: 77%
“…It is composed of 86-101 amino acid residues (depending on the isolate) encoded by two exons. The first 72 amino acid residues (encoded by the first exon) are organized into three functional domains: (i) an acidic N-terminal region (aa [1][2][3][4][5][6][7][8][9][10][11][12][13][14][15][16][17][18][19][20] that binds to cell surface CD26 and is thought to mediate immunosuppressive activity [3]; (ii) a cysteine-rich domain (aa [21][22][23][24][25][26][27][28][29][30][31][32][33][34][35][36][37][38][39][40] that mediates binding to chemokine receptors [4]; and (iii) the basic domain (aa 41-60). The latter domain is responsible for the internalization of extracellular Tat and its import into the nucleus and is also required for binding to short RNA transcripts containing the viral transactivation-responsive element (TAR) [5,6].…”
Section: Introductionmentioning
confidence: 99%
“…Previous studies on CD44 and epidermal differentiation defined CD44v3-10, also called epican, as the most abundant and largest CD44 isoform in human epidermis [45][46][47]. However, our study demonstrate an abundant CD44v2-10 transcript, which is larger than CD44v3-10.…”
Section: Discussioncontrasting
confidence: 76%
“…In addition to the standard or hematopoietic form, CD44 occurs in a variety of variant isoforms that arise from alternative splicing of at least 10 genomic exons in addition to those encoding standard CD44; CD44v8-10, CD44v10, and CD44v3-10 are major variants on human skin keratinocytes, where CD44 molecules are localized primarily on filopodia of cultured cells and at intercellular junctions in tissue sections (31,32). CD44 is expressed throughout the epidermis from the germinative basal layer to the granular layer just below the stratum corneum (33,34).…”
Section: Discussionmentioning
confidence: 99%