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C‐terminal fragments of parathyroid hormone‐related protein, PTHrP‐(107‐111) and (107‐139), and the N‐terminal PTHrP‐(1‐40) fragment stimulate membrane‐associated protein kinase C activity in rat spleen lymphocytes
Author(s) -
Whitfield James F.,
Isaacs Richard J.,
Chakravarthy Balu R.,
Durkin Jon P.,
Morley Paul,
Neugebauer Witold,
Williams Ross E.,
Willick Gordon,
Rixon Raymond H.
Publication year - 1994
Publication title -
journal of cellular physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.529
H-Index - 174
eISSN - 1097-4652
pISSN - 0021-9541
DOI - 10.1002/jcp.1041580317
Subject(s) - protein kinase c , spleen , parathyroid hormone related protein , chemistry , protein kinase a , parathyroid hormone , immune system , microbiology and biotechnology , phosphorylation , medicine , biology , endocrinology , biochemistry , calcium , immunology , organic chemistry
Membrane‐associated protein kinase C (PKC) activity in lymphocytes freshly isolated from rat spleen was stimulated by the C‐terminal parathyroid hormonerelated protein fragments, PTHrP‐(107–111) and PTHrP‐(107–139), at concentrations from 10 −3 to 10 4 pM. By contrast, the same concentrations of PTHrP‐(120–139), Without the 107–111 TRSAW (‐Thr‐Arg‐Ser‐Ala‐Trp‐) sequence of the other C terminal fragments, did not stimulate spleen lymphocyte PKC. Low concentrations of the N‐terminal PTHrP‐(1–40) fragment also stimulated membrane‐associated PKC activity in the spleen lymphocytes. These results suggest that PTHrP might be an important physiological regulator of the immune response. Published 1994 Wiley‐Liss, Inc.