-
[show abstract]
[hide abstract]
ABSTRACT: The mAb16D10 was raised against a pathological onco-glycoform of bile salt-dependent lipase isolated from the pancreatic juice of a patient suffering from a pancreatic adenocarcinoma. We previously showed that mAb16D10 specifically discriminates human pancreatic tumor tissues from other cancer and nontumor tissues. In this study, we report that mAb16D10 inhibited the proliferation of only human pancreatic tumor cells expressing 16D10 plasma membrane Ag. Interaction of mAb16D10 with its cognate surface Ag on pancreatic cells promoted cell death by activation of the p53- and caspase-dependent apoptotic pathway, and silencing of p53 decreased cell death. The decreased proliferation was also partly due to cell cycle arrest in G1/S phase, mAb16D10 triggering of glycogen synthase kinase-3β (GSK-3β) activation, degradation of β-catenin, and decreased expression of cyclin D1. GSK-3β positively affected p53 expression in pancreatic tumor cells after mAb16D10 binding. Inhibition of GSK-3β activity reversed the effects induced by mAb16D10 in SOJ-6 cells, supporting the pivotal role of GSK-3β signaling in the mechanisms of action induced by mAb16D10. Also, mAb16D10 cell treatment led to membrane overexpression of E-cadherin. Both E-cadherin and tumor Ag were localized in membrane lipid cholesterol-rich microdomains and are thought to belong to signaling platforms involved in the induction of cell cycle arrest and cell death. Overall, this study reveals that mAb16D10 holds great potential to prevent pancreatic tumor proliferation by apoptotic cell death, thus promising therapeutic prospects for treatment of pancreatic adenocarcinoma, a highly lethal disease.
The Journal of Immunology 09/2012; 189(7):3386-96. · 5.79 Impact Factor
-
Cécile Franceschi,
Aurélie Collignon,
Daniel Isnardon,
Liliane Benkoel,
Alain Vérine,
Françoise Silvy, Jean-Paul Bernard,
Dominique Lombardo,
Evelyne Beraud,
Daniel Olive,
Eric Mas
[show abstract]
[hide abstract]
ABSTRACT: Aberrant glycosylation or overexpression of cell-surface glycosylated tumor-associated Ags (TAA) distinguish neoplastic from normal cells. Interactions of TAA MUC1 and HER2/neu with dendritic cells (DC) preclude efficient processing, which impairs immune responses. It is thus important to define the mechanisms of interactions between DC and glycosylated TAA and their trafficking and processing for further T cell activation. In this work, we study interactions between DC and the oncofetal fucose-rich glycovariants of bile salt-dependent lipase (BSDL), expressed in pancreatic cancer tissues and referred to as pathological BSDL carrying the fucosylated J28 glycotope (pBSDL-J28) because it is characterized by the mAb J28. The expression of pBSDL-J28 was assessed by immunohistochemistry and quantified by confocal microscopy. Nontumoral pancreatic tissues and cells do not express pBSDL-J28. Using multidisciplinary approaches and functional studies, we provide the first evidence, to our knowledge, that this tumoral glycoprotein is rapidly internalized by human DC through macropinocytosis and endocytosis via mannose receptors and then transported to late endosomes for processing. Interestingly, pBSDL-J28 per se induced DC maturation with increased expression of costimulatory and CD83 molecules associated with cytokine secretion (IL-8 and IL-6). Surprisingly, DC retained their full ability to internalize Ags, making this maturation atypical. Finally, the allogeneic pBSDL-J28-treated DC stimulated lymphocyte proliferation. Besides, pulsing DC with pBSDL-J28 C-terminal glycopolypeptide and maturation with CD40L triggered CD4(+) and CD8(+) T cell proliferation. Therefore, interactions of pBSDL-J28, expressed on tumoral pancreatic tissue, with DC may lead to adequate Ag trafficking and processing and result in T cell activation.
The Journal of Immunology 02/2011; 186(7):4067-77. · 5.79 Impact Factor
-
Liliane Benkoël, Jean-Paul Bernard,
Marie-José Payan-Defais,
Lydie Crescence,
Cécile Franceschi,
Mireille Delmas,
Mehdi Ouaissi,
Bernard Sastre,
José Sahel,
Anne-Marie Benoliel,
Pierre Bongrand,
Françoise Silvy,
Laurent Gauthier,
François Romagné,
Dominique Lombardo,
Eric Mas
[show abstract]
[hide abstract]
ABSTRACT: We have shown that the 16D10 antigen located on the mucin-like COOH-terminal domain of the feto-acinar pancreatic protein (FAPP) is expressed at the surface of human pancreatic tumor cell lines such as SOJ-6 cell line. Furthermore, an in vivo study indicates that targeting this cell-membrane glycopeptide by the use of the monoclonal antibody (mAb) 16D10 inhibits the growth of SOJ-6 xenografts in nude mice. To validate the potential use of the mAb16D10 in immune therapy, this study examined the expression of 16D10 antigens at the surface of human pancreatic adenocarcinomas versus control tissues. We examined the reactivity of mAb16D10 and mAb8H8 with pancreatic ductal adenocarcinomas (PDAC) compared with controls by using immunohistochemistry and confocal laser scanning microscopy. mAb8H8 does react with control or nontumoral human pancreatic tissues. mAb16D10 has a strong and specific reactivity with PDAC and does not react with other cancers of epithelia or normal tissues tested. Notable, mAb16D10 mostly recognizes membrane of tumoral cells. Furthermore, mAb8H8 and mAb16D10 recognized a protein of 110 to 120 kDa in homogenates of nontumoral and tumoral human pancreatic tissues, respectively. This size correlates with that of FAPP or with that of the normal counterpart of FAPP, the so-called bile salt-dependent lipase. The results suggest that mAb16D10 presents a unique specificity against PDAC; consequently, it could be effective in immune therapy of this cancer. Furthermore, mAb16D10 and mAb8H8 pair might be useful for diagnosis purpose in discriminating tumoral from nontumoral human pancreatic tissues.
Molecular Cancer Therapeutics 03/2009; 8(2):282-91. · 5.23 Impact Factor
-
Mehdi Ouaïssi,
Igor Sielezneff,
Ricardo Silvestre,
Bernard Sastre, Jean-Paul Bernard,
Joelle Simony Lafontaine,
Marie José Payan,
Laetitia Dahan,
Nicolas Pirrò,
Jean François Seitz,
Eric Mas,
Dominique Lombardo,
Ali Ouaissi
[show abstract]
[hide abstract]
ABSTRACT: Alterations in HDACs gene expression have been reported in a number of human cancers. No information is available concerning the status of HDACs in pancreatic cancer tumors. The aim of the present study was to evaluate the expression levels of members of class I (HDAC1, 2,, 3), class II (HDAC4, 5, 6, and 7), and class III (SIRT1, 2, 3, 4, 5, and 6) in a set of surgically resected pancreatic tissues.
Total RNA was isolated from 11 pancreatic adenocarcinomas (PA): stage 0 (n = 1), IB (n = 1), IIB (n = 6), III (n = 1), IV (n = 2), one serous cystadenoma (SC), one intraductal papillary mucinous tumor of the pancreas (IMPN), one complicating chronic pancreatitis (CP), and normal pancreas (NP) obtained during donor liver transplantation. Moreover, six other control pancreatic were included. HDACs gene expression was conducted using quantitative real-time polymerase chain reaction (qPCR). Protein expression levels were analyzed by Western blot and their localization by immunohistochemistry analyses of cancer tissues sections.
Remarkably, 9 of the 11 PA (approximately 81%) showed significant increase of HDAC7 mRNA levels. In contrast to PA samples, message for HDAC7 was reduced in CP, SC, and IMPN specimens. The Western blot analysis showed increased expression of HDAC7 protein in 9 out of 11 PA samples, in agreement with the qPCR data. Most of the PA tissue sections examined showed intense labeling in the cytoplasm when reacted against antibodies to HDAC7.
The data showed alteration of HDACs gene expression in pancreatic cancer. Increased expression of HDAC7 discriminates PA from other pancreatic tumors.
Annals of Surgical Oncology 06/2008; 15(8):2318-28. · 4.17 Impact Factor
-
[show abstract]
[hide abstract]
ABSTRACT: In human pancreatic adenocarcinoma, alterations of glycosylation processes leads to the expression of tumor-associated carbohydrate antigens, representing potential targets for cancer immunotherapy. Among these pancreatic tumor-associated carbohydrate antigens, the J28 glycotope located within the O-glycosylated mucin-like C-terminal domain of the fetoacinar pancreatic protein (FAPP) and expressed at the surface of human tumoral tissues, can be a good target for anticancer therapeutic vaccines. However, the oncodevelopmental self character of the J28 glycotope associated with the low immunogenicity of tumor-associated carbohydrate antigens may be a major obstacle to effective anti-tumor vaccine therapy. In this study, we have investigated a method to increase the immunogenicity of the recombinant pancreatic oncofetal J28 glycotope by glycoengineering Galalpha1,3Galss1,4GlcNAc-R (alphaGal epitope) which may be recognized by natural anti-alphaGal antibody present in humans. For this purpose, we have developed a stable Chinese hamster ovary cell clone expressing the alphaGal epitope by transfecting the cDNA encoding the alpha1,3galactosyltransferase. These cells have been previously equipped to produce the recombinant O-glycosylated C-terminal domain of FAPP carrying the J28 glycotope. As a consequence, the C-terminal domain of FAPP produced by these cells carries the alphaGal epitope on oligosaccharide structures associated with the J28 glycotope. Furthermore, we show that this recombinant "alpha1,3galactosyl and J28 glycotope" may not only be targeted by human natural anti-alphaGal antibodies but also by the mAbJ28, suggesting that the J28 glycotope remains accessible to the immune system as vaccinating agent. This approach may be used for many identified tumor-associated carbohydrate antigens which can be glycoengineered to carry a alphaGal epitope to increase their immunogenicity and to develop therapeutic vaccines.
Glycobiology 07/2007; 17(6):620-30. · 3.58 Impact Factor
-
[show abstract]
[hide abstract]
ABSTRACT: Clinical symptoms of inflammatory bowel disease (IBD)-associated pancreatitis are found in approximately 2% of patients, but the frequency of the disease could be much higher since IBD-associated pancreatitis could be mainly a silent disease. The aim of this study was to describe the radiological and biological features of IBD-associated pancreatitis and assess its frequency by comparing data from IBD patients with or without a history of pancreatitis.
79 patients were prospectively enrolled (median age 36 years). Symptoms of pancreatitis had been previously recorded in 30 of them (group P; the other 49 patients (group C) had no history of pancreatitis. Pancreatic ductal changes were investigated by pancreato-MRI. Exocrine function was assessed by the fecal elastase test and by assaying serum amylase, lipase, C-reactive protein, PAP, IgG4 and pancreatic autoantibodies.
Increased levels of amylase and lipase occurred in 11% of IBD patients, that frequency being significantly higher in group P (23%) than in group C (4%) (p = 0.01). Low fecal elastase reflecting impaired exocrine function was observed in 30% of patients and again significantly more in group P (50%) than in group C (17%) (p = 0.04). The frequency of elevated values varied from 12% for amylase and lipase to 18% for PAP, 20% for pancreatic autoantibodies and 45% for CRP, without a difference between groups P and C. Silent exocrinopathy was observed in both groups, pancreatic autoantibodies and pancreatic duct alterations being found in 20 and 11% of patients, respectively.
Finding pancreatic insufficiency in about 30% of the included patients and in 50% of those with a previous history of pancreatitis suggests that IBD might be associated with chronic pancreatic alteration. Episodes of mild acute pancreatitis observed in some patients are not always due to adverse effects of treatments and can be acute manifestations of the chronic disease.
Pancreatology 02/2006; 6(5):464-71. · 1.99 Impact Factor
-
[show abstract]
[hide abstract]
ABSTRACT: The alphaGal epitope is a carbohydrate structure, Galalpha1,3Galbeta1,4GlcNAc-R, synthesized on glycoconjugates in many mammals by alpha1,3galactosyltransferase. Humans do not express this epitope and present in serum large amounts of naturally occuring antibodies, which recognize the alphaGal epitopes and participate in the hyperacute rejection of xenograft. Studies indicated that the fundamental mechanism of hyperacute rejection involving the alphaGal epitope expression can be used in cancer therapy. We have previously suggested that the alphaGal epitope expression by human pancreatic tumoral cells could decrease the tumorigenic behavior of these cells. To determine whether the expression of the alphaGal epitope can modify the tumorigenicity of pancreatic cancer cells, we used a Syrian golden hamster pancreatic adenocarcinoma experimental model. The expression of alphaGal epitopes in the Syrian golden hamster pancreatic cancer cell line HaP-T1 was obtained by selecting stable cell clones transfected with murine alpha1,3galactosyltransferase gene. The alphaGal epitope expression resulted in a delay in the tumoral development of HaP-T1 cells in vivo after allograft transplantation of Syrian golden hamsters (2.5-fold, P < 0.05) and of nude mice. This result is associated with an 100% increase in survival time of nude mice bearing tumors expressing the alphaGal epitope. Our results confirm that the cell surface expression of alphaGal epitope decreases the tumorigenic behavior of pancreatic cancer cells. This novel property may be useful for the development of cancer gene immunotherapy strategy.
Molecular Carcinogenesis 04/2005; 42(4):202-12. · 3.16 Impact Factor
-
[show abstract]
[hide abstract]
ABSTRACT: The Gal epitope is a carbohydrate structure, Gal1,3Galβ1,4GlcNAc-R, synthesized on glycoconjugates in many mammals by 1,3galactosyltransferase. Humans do not express this epitope and present in serum large amounts of naturally occuring antibodies, which recognize the Gal epitopes and participate in the hyperacute rejection of xenograft. Studies indicated that the fundamental mechanism of hyperacute rejection involving the Gal epitope expression can be used in cancer therapy. We have previously suggested that the Gal epitope expression by human pancreatic tumoral cells could decrease the tumorigenic behavior of these cells. To determine whether the expression of the Gal epitope can modify the tumorigenicity of pancreatic cancer cells, we used a Syrian golden hamster pancreatic adenocarcinoma experimental model. The expression of Gal epitopes in the Syrian golden hamster pancreatic cancer cell line HaP-T1 was obtained by selecting stable cell clones transfected with murine 1,3galactosyltransferase gene. The Gal epitope expression resulted in a delay in the tumoral development of HaP-T1 cells in vivo after allograft transplantation of Syrian golden hamsters (2.5-fold, P < 0.05) and of nude mice. This result is associated with an 100% increase in survival time of nude mice bearing tumors expressing the Gal epitope. Our results confirm that the cell surface expression of Gal epitope decreases the tumorigenic behavior of pancreatic cancer cells. This novel property may be useful for the development of cancer gene immunotherapy strategy. © 2005 Wiley-Liss, Inc.
Molecular Carcinogenesis 03/2005; 42(4):202 - 212. · 3.16 Impact Factor
-
[show abstract]
[hide abstract]
ABSTRACT: The enzyme alpha1,3galactosyltransferase synthesizes the alphaGal epitope, a carbohydrate structure (Galalpha1,3Galbeta1,4GlcNAc-R), on glycoconjugates in lower mammals. The enzyme is absent in humans but large amounts of natural antibodies that recognize alphaGal epitopes are present in human serum. It is likely that these antibodies contribute to the host defense and participate in the hyperacute rejection of xenograft. Previous studies indicated that the glycosyltransferase gene transfer into tumoral cells can modify the structure of glycoconjugates at the cell surface and, as a consequence, modulates the metastatic and tumorigenic behaviors of these cells. The aim of our study was to determine whether the expression of alphaGal epitope can modify the tumorigenicity of human pancreatic cancer cells. The expression of alphaGal epitopes in the human pancreatic cancer cell lines BxPC-3 and Panc-1 was obtained by selecting stable cell clones transfected with murine alpha1,3galactosyltransferase gene. The expression of the enzyme activity in BxPC-3 and Panc-1 cells resulted in the formation at the cell surface of alphaGal epitopes that are recognized by human anti-alphaGal antibodies. alphaGal epitope expression at the surface of pancreatic cancer cells was associated with the fixation of complement 1q to human anti-alphaGal antibodies. The alphaGal epitope expression also resulted in a delay in the tumoral development of BxPC-3 and Panc-1 cells in vivo after xenograft transplantation of nude mice. In addition to the impairment of the metastatic potential of murine tumor cell lines and the activation of immune response, our study provides evidence that the cell surface expression of alphaGal epitopes also modulates the tumorigenic behavior of human pancreatic cancer cells.
International Journal of Cancer 01/2004; 107(6):910-8. · 5.44 Impact Factor
-
[show abstract]
[hide abstract]
ABSTRACT: The enzyme α1,3galactosyltransferase synthesizes the αGal epitope, a carbohydrate structure (Galα1,3Galβ1,4GlcNAc-R), on glycoconjugates in lower mammals. The enzyme is absent in humans but large amounts of natural antibodies that recognize αGal epitopes are present in human serum. It is likely that these antibodies contribute to the host defense and participate in the hyperacute rejection of xenograft. Previous studies indicated that the glycosyltransferase gene transfer into tumoral cells can modify the structure of glycoconjugates at the cell surface and, as a consequence, modulates the metastatic and tumorigenic behaviors of these cells. The aim of our study was to determine whether the expression of αGal epitope can modify the tumorigenicity of human pancreatic cancer cells. The expression of αGal epitopes in the human pancreatic cancer cell lines BxPC-3 and Panc-1 was obtained by selecting stable cell clones transfected with murine α1,3galactosyltransferase gene. The expression of the enzyme activity in BxPC-3 and Panc-1 cells resulted in the formation at the cell surface of αGal epitopes that are recognized by human anti-αGal antibodies. αGal epitope expression at the surface of pancreatic cancer cells was associated with the fixation of complement 1q to human anti-αGal antibodies. The αGal epitope expression also resulted in a delay in the tumoral development of BxPC-3 and Panc-1 cells in vivo after xenograft transplantation of nude mice. In addition to the impairment of the metastatic potential of murine tumor cell lines and the activation of immune response, our study provides evidence that the cell surface expression of αGal epitopes also modulates the tumorigenic behavior of human pancreatic cancer cells. © 2003 Wiley-Liss, Inc.
International Journal of Cancer 12/2003; 107(6):910 - 918. · 5.44 Impact Factor
-
[show abstract]
[hide abstract]
ABSTRACT: Digestive bleeding is a rare complication of jejunal diverticulas whose diagnosis and treatment are difficult. We report a case of hematochezia whose origin was not determined by endoscopic investigations. Coelio-mesenteric arteriography showed a leakage of contrast medium from a jejunal arterial branch and allowed a successful embolization of the arterial branches feeding the bleeding point.
Gastroentérologie Clinique et Biologique 07/2003; 27(6-7):648-50. · 0.80 Impact Factor
-
[show abstract]
[hide abstract]
ABSTRACT: Celiac plexus block guided by ultrasonography is an efficient technique for treatment of pain due to solar syndrome. Neurological complication of this therapeutic method can be avoided using an anterior route. We report the occurrence of splenic necrosis after celiac plexus block, which represents an exceptional complication of the therapeutic procedure.
Gastroentérologie Clinique et Biologique 04/2003; 27(3 Pt 1):339-40. · 0.80 Impact Factor
-
[show abstract]
[hide abstract]
ABSTRACT: The long-term efficacy of endoscopic treatment in pancreas divisum is controversial. This study evaluated the long-term results of dorsal duct stent insertion and endoscopic sphincterotomy of the minor papilla in patients presenting with recurrent acute pancreatitis or chronic pain.
Pancreas divisum was diagnosed in 175 patients between 1980 and 1998. Twenty-four patients seen with recurrent acute pancreatitis without underlying chronic calcifying pancreatitis or significant alcohol consumption were included in this study with a follow-up of at least 24 months. Eight were treated by sphincterotomy of the minor papilla alone, and 16 underwent dorsal duct stent insertion for a median duration of 8 months.
The median duration of follow-up after endoscopic management was 39 months (range 24-105; interquartile range 40.5). All patients had recurrent acute pancreatitis before endoscopic treatment during a median period of 5 years. At the end of the follow-up there were only 2 recurrences of acute pancreatitis (p < 0.01). The number of patients with chronic pain before endoscopic treatment and at the end of follow-up decreased from 20 of 24 (83%) to 7 of 24 (29%) without reaching statistical significance. The 25% recurrence rate was estimated at 50 months by Kaplan-Meier analysis. Nine patients presented with a dilated dorsal duct before endoscopic treatment. After stent insertion, dorsal duct dilatation appeared in all 16 patients who underwent stent placement, and pancreatic duct stenosis developed in 3. Four patients (19%) required further treatment for pain recurrence or acute pancreatitis, with surgical procedures being performed in 2 cases. Complications occurred in 9 of 24 patients (38%), mainly acute pancreatitis or stenosis of the minor papilla. All complications except one were managed conservatively. Complications seemed to be less frequent after minor papilla sphincterotomy than after pancreatic stent insertion (25% vs. 44%).
In patients with pancreas divisum, both dorsal duct stent insertion and minor papilla sphincterotomy decrease the rate of recurrent acute pancreatitis, whereas relief of chronic pain was less obvious.
Gastrointestinal Endoscopy 04/2002; 55(3):376-81. · 4.88 Impact Factor
-
[show abstract]
[hide abstract]
ABSTRACT: Pancreatitis-associated protein (PAP) is a pancreatic stress protein also expressed in the ileum but not in the colon. Its serum concentration is increased in patients with small bowel inflammation due to untreated celiac disease. We searched to determine whether PAP could be a serum marker for ileal location of active Crohn's disease (CD).
A multicenter prospective study was conducted, including 54 healthy controls and 124 patients with CD of whom 38 had quiescent ileal or ileocolonic disease (group A), 45 had active ileal or ileocolonic disease (group B), 18 had quiescent colon-only CD (group C), and 28 had active colonic disease (group D). Active disease was defined by a Crohn's disease activity index > 150 and serum C-reactive protein (CRP) > 10 mg/mL. Location of lesions was assessed by endoscopy. PAP was assayed in serum, the upper threshold for normal values being 50 ng/mL.
In group B, 27 patients (60%) had elevated serum PAP, compared to one in group A (2.5%), one in group C (5.3%), three in group D (10.7%) and none in the control group (P<0.01). By contrast, serum levels of C-reactive protein did not differ between patients with active CD and either ileal location (group B) or pure colonic location (group D) (38 +/-10.5 vs 41.6 +/- 6.4 mg/mL, NS). Within group B, serum PAP concentration was correlated with none of the epidemiological, clinical or biological data available. Increased serum level of PAP diagnosed ileal location in active CD with a sensitivity of 60%, a specificity of 94%, a positive predictive value of 84% and a negative predictive value of 81%.
Elevated serum PAP (> 50 ng/mL ) is significantly associated with disease activity and ileal location
Gastroentérologie Clinique et Biologique 01/2002; 26(1):23-8. · 0.80 Impact Factor
-
Marc Barthet,
Patrick Hastier, Jean-Paul Bernard,
Gilbert Bordes,
John Frederick,
Serge Allio,
Pierre Mambrini,
Marie-Christine Saint-Paul,
Jean-Pierre Delmont,
Jacques Salducci,
Jean-Charles Grimaud,
Jos|[eacute]| Sahel
[show abstract]
[hide abstract]
ABSTRACT: OBJECTIVE: Several cases of pancreatitis have been described during the course of Crohn's disease (CD) or ulcerative colitis (UC), but many of them were related to either biliary lithiasis or drug intake. We tried to evaluate the clinical and morphological features of so-called idiopathic pancreatitis associated with inflammatory bowel disease and to define their pathological characteristics.
The American Journal of Gastroenterology 07/1999; 94(8):2141-2148. · 7.28 Impact Factor
-
[show abstract]
[hide abstract]
ABSTRACT: Feto-acinar pancreatic protein (FAPP) characterized by mAbJ28 reactivity is a specific component associated with ontogenesis and behaves as an oncodevelopment-associated antigen. We attempted to determine whether pancreatic tumoral SOJ-6 cells are expressed at their surface FAPP antigens and to examine if specific antibodies directed against these FAPP epitopes could decrease the growth of pancreatic tumors in a mice model. For this purpose, we used specific antibodies against either the whole FAPP, the O-glycosylated C-terminal domain, or the N-terminal domain of the protein. Our results indicate that SOJ-6 cells expressed at their surface a 32-kDa peptide corresponding to the C-terminal domain of the FAPP. Furthermore, we show, by using endoproteinase Lys-C or geldanamycin, a drug able to impair the FAPP secretion, that this 32-kDa peptide expressed on the SOJ-6 cell surface comes from the degradation of the FAPP. Finally, an in vivo prospective study using a preventative tumor model in nude mice indicates that targeting this peptide by the use of mAb16D10 inhibits the growth of SOJ-6 xenografts. The specificity of mAb16D10 for pancreatic tumors and the possibility to obtain recombinant structures of mucin-like peptides recognized by mAb16D10 and mAbJ28 are promising tools in immunologic approaches to cure pancreatic cancers.
Neoplasia 6(6):713-24. · 5.95 Impact Factor
