Expression of antigenic crossreactivity to RD114 p 30 protein in a human fibrosarcoma cell line.

نویسندگان

  • H S Smith
  • J L Riggs
  • E L Springer
چکیده

An antigen crossreacting with the 30,000-molecular-weight protein (p30) of the feline endogenous oncornavirus (RD114) was detected in a well-characterized human fibrosarcoma cell line, HT1080, by indirect immunofluorescence. Three antisera against RD114 p30 gave similar positive results, while two antisera prepared against simian sarcoma virus p30, one antiserum prepared against murine leukemia virus p30, and one antiserum prepared against feline leukemia virus p30 gave no immunofluorescence. The reactivity observed with the antiserum against RD114 p30 was detected in 10-40% of the cells at early passages and was no longer expressed by the forty-first subculture. The reactivity could be removed by adsorption of the antiserum with RD114-infected dog or human cells, but not by uninfected cells or by cells infected with an antigenically unrelated oncornavirus, feline leukemia virus. Neither complete virus particles nor reverse transcriptase (RNA-dependent DNA nucleotidyltransferase) activity was detected in the culture. These experiments suggest that the fibrosarcoma cell line is expressing an antigen related to the p30 protein of RD114 baboon endogenous virus group of oncornaviruses without producing complete virions.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

In silico design and expression of a novel fusion protein of HBHA and high antigenic region of FAP-P of Mycobacterium avium subsp. paratuberculosis in Pichia pastoris

Mycobacterium avium subsp. paratuberculosis (MAP) is the etiologic agent of Johne's disease in ruminants and there has been a shift in the public health approach to MAP and human diseases like Crohn's disease. The prevention of infection by MAP in ruminants is thought to deter the high impact of economic losses in the level of dairy industry and possible spreading of this pathogen in dairy prod...

متن کامل

Effect of Thermal Stress on MICA/B Induction in a Human Liposarcoma Cell Line

Background: A possible mechanism by which hyperthermia enhances tumor immunogenicity is the induction of NKG2D ligands on tumor cells. Although the expression of MHC class I chain-related protein A and B (MICA/B) has previously been reported in different carcinomas, there is no information about MICA/B expression in liposarcomas. Objective: To investigate MICA/B induction in a human liposarcoma...

متن کامل

Ectopic Expression of Embryo/Cancer Sequence A (ECSA) in KYSE-30 Cell Line Using Retroviral System

Background Human preimplantation embryonic cells share many similarities with cancer cells such as ability to self-renew, unlimited proliferation and maintenance of the undifferentiated state. Embryo-cancer sequence A (ECSA), also known as developmental pluripotency associated-2 (DPPA2), is a cancer testis antigen (CTA) with unclear biological function yet. Objective: CTAs are expressed normal...

متن کامل

تأثیر هورمون استروژن بر میزان پروتئین p53 در رده سلولی T47D سرطان پستان

Background: Breast cancer is one of the most common cancers in women. Nearly 30% of breast cancers are hormone-dependent, and these hormones comprising estrogens influence progression of breast cancers. It is now widely recognized that p53 may be the most frequently mutated protein in breast cancer. High levels of p53 protein are a common feature of many human malignant cancers. Given that, T47...

متن کامل

Expression Analysis of RNA-Binding Motif Gene on Y Chromosome (RBMY) Protein Isoforms in Testis Tissue and a Testicular Germ Cell Cancer-Derived Cell Line (NT2)

a key factor in spermatogenesis and disorders associated with this protein have been recognized to be related to male infertility. Although it was suggested that this protein could have different functions during germ cell development, no studies have been conducted to uncover the mechanism of this potential function yet. Here, we analyzed the expression pattern of RBMY protein isoforms in test...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:
  • Proceedings of the National Academy of Sciences of the United States of America

دوره 74 2  شماره 

صفحات  -

تاریخ انتشار 1977