The high prevalence of Helicobacter DNA and the positive findings by IHC in gallbladder and liver raise questions concerning an infectious role of Helicobacter in patients with chronic cholecystitis.

Homeostasis of inorganic phosphate in the human body is maintained by regulated absorption, metabolism, and excretion. Sodium-dependent phosphate transporters (NaPi) mediate the transport of inorganic phosphate (P(i)) in cells in response to dietary phosphate consumption, hormones, and growth factors. NaPi2b is a member of the sodium-dependent phosphate transporter family, with a distinct pattern of expression and regulation. Signaling pathways activated by mitogens, glucocorticoids, and metabolic factors have been implicated in regulating P(i) transport via NaPi2b. Inactivation of NaPi2b function by mutations has been linked to human pathologies, such as pulmonary alveolar microlithiasis. In this study, we describe the generation and characterization of monoclonal antibodies against human NaPi2b. The monoclonal antibodies were shown to recognize specifically transiently overexpressed and endogenous NaPi2b in commonly used immunoassays, including Western blotting, immunoprecipitation, and immunohistochemistry. These properties make them particularly valuable reagents for elucidating NaPi2b function in health and disease.

Äîñë³äaeå íî çì³íè ê³ëüê³ñíî ãî ð³âíÿ ìî ëå êó ëÿð íî ãî øà ïå ðî íó Hsp60 ó òêà íèí³ ñåð öÿ ïðè äè ëÿ-òàö³éí³é êàðä³îì³îïàò³¿ (ÄÊÌÏ). Âè ÿâ ëå íî çðîñ òàí íÿ ñó ìàð íî ãî âì³ñòó Hsp60 ÿê ó ë³çà òàõ òêà íèíè ñåð äåöü ëþ äåé, õâî ðèõ íà ÄÊÌÏ, òàê ³ â ë³çà òàõ òêà íèí ñåð äåöü ìè øåé ³ç åê ñïå ðè ìåí òàëü íèì çà õâîðþ âàí íÿì, ïîä³áíèì äî ÄÊÌÏ ëþ äè íè. Âïåð øå âñòà íîâ ëå íî çá³ëüøåí íÿ ê³ëüêîñò³ Hsp60 ó ì³òî-õîíäð³àëüí³é ôðàêö³¿ òà çíè aeåí íÿ ó öè òîï ëàç ìà òè÷í³é, ùî ìîaeå áóòè îäíèì ³ç ÷èí íèê³â àïîï òî çó êàðä³îì³îöèò³â ïðè ñåð öåâ³é íå äîñ òàò íîñò³, âèê ëè êàí³é 䳺þ õðîí³÷íî ãî ñòðå ñó. Çà ðå çóëü òà òà ìè ³ìó íîã³ñòîõ³ì³÷íî ãî àíàë³çó ñåð äåöü ìè øåé ³ç åê ñïå ðè ìåí òàëü íîþ ïà òî ëî㳺þ, ïîä³áíîþ äî ÄÊÌÏ ëþ äè íè, ïî êà çà íî, ùî ï³äâè ùåí íÿ ê³ëüê³ñíî ãî ð³âíÿ Hsp60 ó òêà íèí³ ñåð öÿ íî ñèòü íå îäíîð³äíèé õàðàê òåð: çíà÷ íå çðîñ òàí íÿ â³äáó âàºòüñÿ ëèøå â îêðå ìèõ êàðä³îì³îöè òàõ, éìîâ³ðíî, â òèõ, äå àê òè âî-âàí³ àí òèñ òðå ñîâ³ ìå õàí³çìè çà õèñ òó êë³òèíè â³ä 䳿 õðîí³÷íî ãî ñòðå ñó. Êëþ ÷îâ³ ñëî âà: ìî ëå êó ëÿðí³ øà ïå ðî íè, Hsp60, äè ëÿ òàö³éíà êàðä³îì³îïàò³ÿ, êàðä³îì³îöèò, àïîï òîç.

Medullary breast carcinoma (MBC) is a relatively rare malignancy with heavy lymphocytic infiltration that despite cytologically anaplastic features and high mitotic index has more favorable prognosis than other types of breast cancer. Lymphocytic infiltration of tumors reflects ongoing immune response against tumor antigens which could represent a great interest as potential targets for cancer immunotherapy. The search for MBC antigens by SEREX methodology has not been successful due to a very high titer of false positive clones, representing immunoglobulin genes. Here, we describe a novel approach for generating cDNA expression libraries from MBC tumor samples which are depleted of IgG cDNA clones and, therefore, are suitable for the identification of novel tumor-associated antigens (TAA) by SEREX approach. Modified methodology allowed us to isolate a panel of known and novel TAA which are currently under further investigation.

In this study we describe the identification of sodium-dependent phosphate transporter NaPi2b as MX35 cancer-associated antigen. To achieve this goal we have screened extensively a cDNA expressing library from ovarian cancer cell line OVCAR3 with monoclonal antibody MX35. To further confirm the authenticity of this finding, we showed that bacterially and baculovirally expressed NaPi2b is specifically recognized by MX35 antibody. Moreover, the validity of these results was verified in a parallel study involving affinity purification and mass spectrometry. The epitope for MX35 monoclonal antibody was mapped to the largest extracellular loop of NaPi2b. Taken together, this study uncovers the identity of MX35 antigen and provides molecular tools for studying its function in normal and cancer tissues.