INSULIN BINDING TO THE HL-60 HUMAN PROMYELOCYTIC CELL LINE
نویسندگان
چکیده
منابع مشابه
DNA repair in human promyelocytic cell line, HL-60.
The human promyelocytic cell line, HL-60, shows large changes in endogenous poly(ADP-ribose) and in nuclear ADP-ribosyl transferase activity (ADPRT) during its induced myelocytic differentiation. DNA strand-breaks are an essential activator for this enzyme; and transient DNA strand breaks occur during the myelocytic differentiation of HL-60 cells. We have tested the hypothesis that these post-m...
متن کاملDecrease in IGF-I binding sites on human promyelocytic leukemia cell line (HL-60) with differentiation.
Specific insulin-like growth factor I (IGF-I) receptors on human promyelocytic leukemia cell line (HL-60) were identified and characterized. [125I]IGF-I specifically bound to the cells, and [125I]IGF-I binding to the cells was displaced by unlabeled IGF-I in a dose dependent manner. [125I]IGF-I binding to the cells were displaced by multiplication stimulating activity (MSA) and porcine insulin,...
متن کاملEosinophilic differentiation of the human promyelocytic leukemia cell line, HL-60
HL-60 promyelocytic leukemia cells differentiated to eosinophils and eosinophilic precursors when cultured under mildly alkaline conditions (pH 7.6-7.8) for 7 d without refeeding. New cytoplasmic granules appeared blue in the least mature cells and red in the most mature cells when stained with Wright-Giemsa. The granules also stained with Luxol-fast-blue, a characteristic of eosinophil granule...
متن کاملProtein kinase C during differentiation of human promyelocytic leukemia cell line, HL-60.
Protein kinase C (PKC) from human promyelocytic leukemia HL-60 cells can be resolved into three fractions (peak, a, b and c) by hydroxyapatite column chromatography. Peak a and c enzymes are indistinguishable from the brain type II PKC having beta (beta I and beta II)-sequence and type III having alpha-sequence, respectively. Peak b enzyme is a previously unidentified PKC subspecies that has en...
متن کاملA membrane-bound lectin responsive to monocytic maturation in the promyelocytic leukemia cell line HL-60.
A novel mammalian lectin activity responsive to monocytic differentiation is described in the human promyelocytic leukemia cell line HL-60. Glycoprotein binding indicates that the lectin recognizes both N-acetylneuraminic acid and galactose-terminating biantennary oligosaccharide structures. Lectin activity is independent of calcium and appears to reside in a Mr 17,000 intracellular membrane pr...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Pediatric Research
سال: 1981
ISSN: 0031-3998,1530-0447
DOI: 10.1203/00006450-198112000-00193