Simple mucin-type carbohydrate antigens in major salivary glands.

Therkildsen, Marianne Hamilton; Mandel, Ulla; Thorn, Jennifer M.; Christensen, Maria E.; Dabelsteen, Erik

doi:10.1177/42.9.8064132

Cited by 18 publications

(16 citation statements)

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“…Our results are in agreement with other authors who described the absence of TF in selected tissues like uterus, colon, urothelium or squamous cells (Ravn and Jensen 1988;Mandel et al 1991;Itzkowitz 1992;Langkilde et al 1992). Philipsen et al (1991), Therkildsen et al (1994), and Carneiro et al (1994) reported the presence of TF in acinar cells of pancreas, in salivary glands, and in the stomach, respectively, employing mAbs HH8 and HB-T1. We have not seen TF in these tissues, either with mAb G/A7, HH8 or HB-T1.…”

Section: Discussionsupporting

confidence: 96%

“…Tn expression in some epithelial tissues, for instance salivary gland, stomach, and uterus, has been described previously (Carneiro et al 1994;Tashiro et al 1994;Therkildsen et al 1994). In the present study, other epithelial tissues like small intestine were also found to be positive for Tn.…”

Section: Discussionsupporting

confidence: 68%

“…To this end, comprehensive knowledge of the occurrence of TFRA in normal adult human tissues is of the utmost importance. Several groups have examined normal tissues in the context of their studies (Mandel et al 1991;Philipsen et al 1991;Therkildsen et al 1994), but a systematic and comprehensive analysis is still lacking. The study of s-TF has only recently become possible by a combination of lectin staining with conventional histochemistry (Sata et al 1990).…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Thomsen-Friedenreich-related carbohydrate antigens in normal adult human tissues: a systematic and comparative study

Cao

Stosiek

Springer

et al. 1996

Histochem Cell Biol

142

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A broad variety of normal human tissues were examined for the expression of Thomsen-Friedenreich (TF)-related histo-blood group antigens, TF (Gal beta 1-3GalNAc alpha 1-R), Tn (TF precursor, GalNAc alpha 1-R), sialosyl-Tn (NeuAc alpha 2-6GalNAc alpha 1-R), considered to be useful in cancer diagnosis and immunotherapy, and sialosyl-TF, the cryptic form of TF. These antigens or, more correctly, glycotopes, were determined by immunohistochemistry with at least two monoclonal antibodies (mAbs) each (except sialosyl-TF) as well as by lectin histochemistry. For a better dissection of sialosyl-TF and TF glycotopes, tissue sections were pretreated with galactose oxidase or the galactose oxidase-Schiff sequence. Staining with mAbs appeared to be more restricted than with the lectins used. Distribution patterns among normal epithelia were different for all four antigens. These antigens were also detected in some non-epithelial tissues. They can be classified in the following sequence according to the frequency of their occurrence in normal tissues: sialosyl-TF > > sialosyl-Tn > Tn > TF. Most of the positively staining sites for TF, Tn, and sialosyl-Tn are located in immunologically privileged areas. The complex results obtained with anti-TF mAbs (after treatment of the tissue sections with sialidase from Vibrio cholerae) and the lectins amaranthin and jacalin revealed a differential distribution of the subtypes of sialosyl-TF [NeuAc alpha 2-3Gal beta 1-3GalNAc alpha 1-R and Gal beta 1-3 (NeuAc alpha 2-6)GalNAc alpha 1-R] in normal human tissues. From our data it can be inferred that TF, Tn, and sialosyl-Tn are promising targets for a cancer vaccine.

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Section: Discussionsupporting

confidence: 96%

Section: Discussionsupporting

confidence: 68%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Thomsen-Friedenreich-related carbohydrate antigens in normal adult human tissues: a systematic and comparative study

Cao

Stosiek

Springer

et al. 1996

Histochem Cell Biol

142

View full text Add to dashboard Cite

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“…The finding that MG1 and MG2 are synthesized in different cell types is in accordance with previous reports indicating that different carbohydrate side-chains are attached to the protein cores of MG1 and MG2 (Reddy et al, 1985;Prakobphol et al, 1993), since immunohistological data using MAbs defining different carbohydrate epitopes suggest that the pattern of glycosylation is different in mucous and serous cells (Hamper et al, 1986;Therkildsen et al, 1994).…”

Section: Strategy For Production Of Antibodiessupporting

confidence: 90%

Differential Expression of Human High-molecular-weight Salivary Mucin (MG1) and Low-molecular-weight Salivary Mucin (MG2)

et al. 1996

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Two distinct mucin components of saliva, MG1 and MG2, have been identified based on chemical composition and molecular weights (high and low, respectively) in saliva. With the aim of characterizing the expression pattern of salivary mucins, we have prepared monoclonal antibodies (MAbs) directed against the peptide core of MG1 and against a synthetic peptide derived from the MG2 (MUC7) sequence. MAb PANH2 raised against partially deglycosylated MG1 stained a high-molecular-weight smear in Western blots of partially purified MG1. PANH2 binding was increased by deglycosylation with trifluoromethanesulfonic acid as well as with subsequent periodate treatment, and was eliminated by pronase treatment, strongly suggesting that MAb PANH2 was directed to a peptide epitope of MG1. MAb PANH3 raised against a synthetic peptide derived from the MG2 (MUC7) sequence reacted with the native molecule and stained a narrow smear of ca. 200,000 to 210,000 in Western blots of concentrated saliva and a lower-molecular-weight smear of trifluoromethanesulfonic-acid-treated MG2. Immunohistology on frozen sections of human salivary glands showed that MAb PANH2 selectively labeled mucous cells, whereas MAb PANH3 labeled subpopulations of serous cells. Double-direct immunofluorescence staining with PANH2 and PANH3 demonstrated that the staining patterns were non-overlapping. The development of these antibody probes will facilitate studies of mucin expression in diseases of salivary glands.

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“…Moreover, sialyl-T and T antigen can be used as biomarkers in progression of several carcinomas [36–49]. The antigens have been found to be expressed in gastric carcinomas such as colon cancer [37, 39], breast carcinomas [43, 50], salivary gland carcinomas [38, 45–49], cancer of the human cervix [36], pancreatic tumors [42], ovarian tumors [44] and skin tumors [40, 41]. Since many of these cell types also over-express CD24 [20–22], it is intriguing that the CD24 over-expression may account for the increased sialyl-T in the cancer cells.…”

Section: 0 Results and Discussionmentioning

confidence: 99%

Analysis of Recombinant CD24 Glycans by MALDI-TOF-MS Reveals Prevalence of Sialyl-T Antigen

Motari¹,

Zheng²,

Su³

et al. 2009

Am. J. Biomed. Sci.

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CD24 is a glycosyl-phosphatidyl-inositol linked glycoprotein expressed in a broad range of cell types and is heavily glycosylated. It has been found to be over expressed in cancers and tumors and is also a costimulatory molecule. Therefore, this study was carried out to define the structures of the carbohydrates associated with the CD24 recombinant protein. The CD24 glycoprotein's oligosaccharides were released by chemical and enzymatic means prior to being analyzed by MALDI-TOF-MS. The results obtained showed that CD24 is both N-and O-glycosylated. The major oligosaccharides were found to be Neu5Acα-2,3/6Galβ-1,3GalNAc, NeuAc 2 Gal β-1,3GalNAc 1 (O-glycans), GalNAc 2 GlcNAc 2 Man 3 Fuc 1 , Gal 1 GalNAc 2 GlcNAc 2 Man 3 Fuc 1 , and Gal 2 GalNAc 2 GlcNAc 2 Man 3 Fuc 1 (N-glycans). The results showed that Neu5Acα-2,3/6Galβ-1,3GalNAc (sialyl-tumor antigen, sT), a cancer-associated carbohydrate, was the most abundant glycan associated with CD24. This result raised the intriguing possibility that CD24 may be a major carrier of the sialyl-T abundantly found in cancer cells. Keywords CD24; Glycans; MALDI-TOF-MS; T antigen IntroductionCD24 is a glycosyl-phosphatidyl-inositol (GPI)-anchored glycoprotein with widespread expression in both hematopoietic and non-hematopoietic cells. The protein is composed of 27-35 amino acids with nearly half of the amino acids being serine and threonine [1,2]. Both serine and threonine are potential sites for O-glycosylation and asparagine gives potential for N-glycosylation. The human form of CD24 has an unusual structure with the core having [3]. The CD24 molecule is expressed in developing or regenerating tissue and in pre-B-cells, granulocytes, keratinocytes, and renal tubular epithelial cells [1,4,5]. CD24 is over-expressed in both hematological malignancies and a variety of solid tumors such as gastric, renal, nasopharyngeal, hepatocellular, colonic, and small cell lung carcinomas [6,7].The CD24 gene has been implicated in immunity, cancer and autoimmune diseases. Thus, expressing of CD24 in non-professional antigen-presenting cells, such as activated B cells [8,9], astrocytes and oligodendritic cells [10,11] conveys a potent costimulatory activity. In T cells, CD24 promotes homeostatic proliferation [12]. In contrast, CD24 expression in dendritic cells is a negative regulator that modulates the pace of homeostatic proliferation [13], a process that is important for development of autoimmune diseases and cancer immunotherapy [14,15]. Expression of CD24 in pre-B cells on the other hand, modulates fibronectin/VLA-4:VCAM-1 interactions [16,17]. Outside the immune system, CD24 expressed in the central nervous system (CNS) has been shown to inhibit neurite growth [18]. In humans, CD24 polymorphism controls risk and progression of autoimmune diseases, such as multiple sclerosis [19]. Concerning cancerous cells, CD24 has been found to be prevalent on many tumors and carcinomas [20][21][22]. Carbohydrates of CD24 on tumor cells have been shown to play an important role in metastasi...

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Simple mucin-type carbohydrate antigens in major salivary glands.

Cited by 18 publications

References 5 publications

Thomsen-Friedenreich-related carbohydrate antigens in normal adult human tissues: a systematic and comparative study

Thomsen-Friedenreich-related carbohydrate antigens in normal adult human tissues: a systematic and comparative study

Differential Expression of Human High-molecular-weight Salivary Mucin (MG1) and Low-molecular-weight Salivary Mucin (MG2)

Analysis of Recombinant CD24 Glycans by MALDI-TOF-MS Reveals Prevalence of Sialyl-T Antigen

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