Conservation of IL-6 trans-signaling mechanisms controlling L-selectin adhesion by fever-range thermal stress.

Fever is associated with improved survival during infection in endothermic and ectothermic species although the protective mechanisms are largely undefined. Previous studies indicate that fever-range thermal stress increases the binding activity of the L-selectin homing receptor in human or mouse leukocytes, thereby promoting trafficking to lymphoid tissues across high endothelial venules (HEV). Here, we examined the evolutionary conservation of thermal regulation of L-selectin-like adhesion.

Cellular origin and induction of pregnancy-associated alpha 2-glycoprotein synthesis in pregnant rats.

The synthesis of alpha 2-PAG was measured and compared in tissues and cells from normal non-pregnant females, and maternal and fetal rats in vitro to define the target cells hormonally regulated during pregnancy. Synthesis was measured by [L-14C]leucine incorporation into immunochemically isolated alpha 2-PAG and confirmed by radioimmunodiffusion. alpha 2-PAG synthesis was demonstrated in maternal peripheral blood leucocytes, placenta, breast, spleen, liver and fetal peripheral blood leucocytes and liver.

In vitro and in vivo cytotoxic activity of anti-human leukemia monoclonal antibodies SN5c and SN6 daunorubicin conjugates.

Murine monoclonal antibodies SN5c specific for the common acute lymphoblastic leukemia antigen (CALLA) and SN6 specific for a novel GP160 tumor associated antigen expressed on non-T ALL and myelomonocytic leukemia cells were conjugated to daunorubicin via an intermediate dextran carrier. The resulting monoclonal antibody-daunorubicin conjugates retained the immunoreactivity of the unlabeled antibody to antigen positive leukemia target cells. In addition, these conjugates demonstrated selective cytotoxic activity when tested against a panel of human leukemia cell lines and/or human leukemia patient samples of peripheral blood or bone marrow origin.

Specific cytoplasmic alpha-fetoprotein binding protein in MCF-7 human breast cancer cells and primary breast cancer tissue.

Direct evidence was obtained for the existence of a specific high affinity alpha-fetoprotein (AFP)-binding protein in the cytosol of both MCF-7 human breast cancer cultured cells and primary breast cancer tissue from postmenopausal women using a nitrocellulose blotting assay. Scatchard analysis of the binding data for MCF-7 cells at 37 degrees C revealed the presence of a single class of AFP binding sites with an apparent Kd of 4.5 x 10(-8) M, and 75,000 binding sites per cell.

Elevated serum alpha fetoprotein levels in postmenopausal women with primary breast carcinoma.

Elevated serum alpha fetoprotein (AFP) levels were detected and measured by a RIA in postmenopausal women with primary breast carcinoma. This increased AFP consisted of both free and total AFP measured before and after treatment of serum with 0.4 M KCl.

Biosynthesis of alpha fetoprotein by MCF-7 human breast cancer cells.

Direct evidence was obtained for de novo synthesis of AFP by MCF-7 human breast cancer cells per se. Synthesis was demonstrated by L-14C-leucine and L-35S-methionine incorporation into immunochemically isolated AFP, and confirmed by radioimmunodiffusion and radioimmunoelectrophoresis. This information indicates that AFP synthesis is associated with normal and neoplastic cells of several different histotypes, and suggests that AFP detected and measured previously in primary human breast cancer tissue cytosol (Sarcione et al.

Detection and measurement of alpha-fetoprotein in human breast cancer cytosol after treatment with 0.4 M potassium chloride.

The mean concentration of total alpha-fetoprotein (AFP) measured in 51 primary breast cancer cytosols from postmenopausal women by radioimmunoassay after treatment with 0.4 M KCl was 87.2 IU AFP per ml.

Demonstration of pregnancy-associated alpha 2-glycoprotein (alpha 2-PAG) in pregnant, estrogen-treated and breast cancer-bearing rats.

Three pregnancy-associated proteins were demonstrated immunologically in the sera of pregnant rats. Two of these proteins were identified as alpha-fetoprotein and alpha-macrofetoprotein. The third high molecular weight (382,000 daltons) pregnancy-associated alpha 2-glycoprotein (alpha 2-PAG) was detected in the sera of pregnant, estrogen-treated and breast cancer-bearing female rats, and gave immunologic reactions of identity.

Increased ferritin synthesis and release by Hodgkin's disease peripheral blood lymphocytes.

Peripheral blood lymphocytes from patients with all stages of untreated Hodgkin's disease and from normal healthy adults were shown to synthesize and release ferritin in vitro. Ferritin synthesis was confirmed by immunoelectrophoresis, double immunodiffusion and autoradiography. Hodgkin's disease lymphocytes synthesized ferritin 4.

Intracellular synthesis of alpha-fetoprotein and fibrinogen without secretion by Zajdela rat ascites hepatoma cells.

Transplabtable Zajdela rat ascites hepatoma cells, previously considered "nonproducers," synthesize detectable amounts of intracellular alpha-fetoprotein (AFP) and fibrinogen, but fail to secret or release these serum proteins. Evidence for defective secretory mechanisms for serum proteins in these hepatoma cells (a) explains the failure to detect AFP in either the serum or ascitic fluid of rats bearing this hepatoma, (b) indicates that some hepatoma cells should be classified as "nonsecretors," rather than nonproducers of AFP, and (c) suggests that failure to detect AFP in some human and animal hepatomas in vivo and in vitro may also reflect failure of secretion rather than failure of intracellular synthesis.

Ferritin synthesis by splenic tumor tissue of Hodgkin's disease.

Increased ferritin synthesis by Hodgkin's disease splenic tumor tissue was demonstrated by incorporation of 14C-leucine and radioautography. This suggests that elevated tumor and serum ferritin concentrations found in patients with Hodgkin's disease is derived from tumor tissue per se.

Hepatic synthesis of alpha 2 (acute phase)-globulin of rat plasma.

Synthesis of plasma alpha(2) (acute phase)-globulin was demonstrated in isolated perfused rat liver obtained from animals showing acute inflammatory reaction to injury. These findings indicate that the liver is a source of the globulin and that appearance of this protein in the serum results from de novo synthesis by the liver rather than from release of performed and stored globulin.