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  • Connective tissue sheath  (1)
  • Key words Acyclic retinoid  (1)
  • 1
    ISSN: 1432-0584
    Keywords: Key words Acyclic retinoid ; Acute promyelocytic leukemia (APL) ; Differentiation therapy
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract  Acyclic retinoid (all-trans-3, 7, 11, 15-tetramethyl-2, 4, 6, 10, 14-hexadecapentaenoic acid) binds cellular retinoic acid-binding protein with an affinity similar to that of all-trans retinoic acid and induces differentiation of human hepatoma cell lines and a human acute myelogenous leukemia cell line (HL-60). We investigated the in vitro efficacy of acyclic retinoid to induce the differentiation of acute promyelocytic leukemia (APL) cells using primary cultured cells obtained from 11 APL patients. Five days' incubation with acyclic retinoid effected a dose-dependent induction of differentiation. Cells from eight patients showed maximum differentiation at 10–6 M acyclic retinoid. Cells from one patient required 10–5 M for maximum differentiation, while those from two patients exhibited moderate differentiation at 10–5 M. Five days' incubation with acyclic retinoid (10–7∼10–5 M) did not affect the viability or number of cells from any patient except one, whose cells showed a slight decrease in viability at 10–5 M. Thus, we conclude that acyclic retinoid induced the differentiation of primary cultured APL cells at concentrations of 10–6∼10–5 M, a range at which it is not toxic.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-069X
    Keywords: Hair ; Connective tissue sheath ; Alpha-Smooth muscle actin ; Immunohistochemistry ; Immunoelectron microscopy
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Immunohistochemical and immunoelectron microscopy studies revealed the presence of α-smooth muscle (α-SM) actin in fibroblasts located in the connective tissue sheath (CTS) of human anagen hair follicles. Immunostaining was positive from the base of the bulb to the upper part of the lower portion of the mature anagen hair follicles. The late catagen hair follicles did not stain. Ultrastructurally, α-SM actin was detected only in the fibroblasts located in the innermost layer of the transverse collagenous fibres. Since α-SM actin is located in cells with contractile potential, this newly identified layer may play an important role in the morphological changes of the lower portion of the hair follicle during the hair growth cycle.
    Type of Medium: Electronic Resource
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