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  • 1
    ISSN: 1432-0878
    Keywords: Somatotropes, growth hormone cells ; Immunocytochemistry ; Growth hormone (GH) ; Receptors, membrane ; Somatostatin (SRIF) ; Growth hormone-releasing hormone (GRH) ; Rat (Han: WIST)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The synthetic peptides somatostatin (SRIF) and growth hormone-releasing hormone (GRH) were coupled directly to colloidal gold of different particle sizes. Both conjugates were biologically active in displacing the corresponding radiolabeled hormones from high affinity binding sites in pituitary membranes. Release of growth hormone (GH) from cultured anterior pituitary cells was modulated by both conjugates alone or in combination. Ultrastructural studies were performed with cells incubated at 4° C (2 h) and 37° C (2 min-2 h) with one of the labeled peptides or their combination. Somatotropes were identified by immunostaining with anti-rGH followed by protein A-ferritin, thus obtaining a triple labeling. Both hormone conjugates were internalized in different vesicles in the beginning but accumulated during longer incubation times in the same compartment. The secretory vesicles and the nucleus were not labeled by any hormone conjugate. In contrast to SRIF-gold, the uptake of GRH-gold conjugate decreased with longer incubation times. This effect could be neutralized by simulatenous incubation of the somatotropes with both regulating hormones. Hence, whereas the binding and internalization of SRIF by somatotropes do not seem to be influenced by GRH, the corresponding processes for GRH are stimulated by the presence of SRIF.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Cell & tissue research 263 (1991), S. 253-263 
    ISSN: 1432-0878
    Keywords: Astrocytes ; Diencephalon ; Receptors, membrane ; Somatostatin (SRIF) ; Rat (Han: Wist)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Using a somatostatin-gold conjugate of known biological activity, high affinity binding sites for this neuropeptide were visualized at cellular resolution on cultured diencephalic astrocytes and on frozen sections of the rat diencephalon. Binding could be completely suppressed in competition experiments with surplus unlabeled somatostatin. On sections, the ligand was displaced from its binding sites by 10 μM guanosine triphosphate indicating a functional significance of the labeled structures. As with the native peptide, a surplus of the analog SMS 201–995 suppressed nearly all staining. The ligand was bound to distinct populations of astrocytes, namely to those in subependymal and perivascular positions, to astrocytes in somatostatin-innervated hypothalamic nuclei in the mid-sagittal plane and to borderline regions of circumventricular organs. A general mismatch between the distribution of somatostatin-immunoreactive terminals and the pattern of binding of the ligand does not exist. This, together with the competition experiments, suggests a functional relationship between the somatostatin-releasing neurons and associated astrocytes.
    Type of Medium: Electronic Resource
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