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Synergy between a collagen IV mimetic peptide and a somatotropin-domain derived peptide as angiogenesis and lymphangiogenesis inhibitors [PDF]
Angiogenesis, 2012 Angiogenesis is central to many physiological and pathological processes. Here we show two potent bioinformatically-identified peptides, one derived from collagen IV and translationally optimized, and one from a somatotropin domain-containing protein ...
Esak Lee +2 more
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Detection of somatotropin receptors on human monocytes
Immunology Letters, 1990The expression of somatotropin receptors on human peripheral blood monocytes was investigated. Binding of [125I]somatotropin to human monocytes was found to be specific and saturable. The binding was rapid and time-dependent, and was abolished by pretreatment of monocytes with trypsin.
P, Jafari, D N, Khansari
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Journal of Animal Science, 1992
Specific binding sites for porcine somatotropin (pST) have been identified in pig liver microsomal membranes. Little information, however, is available about the size and number of ST receptor (ST-R) forms present. Therefore, the present study was conducted to characterize ST-R in pig liver using two approaches.
Louveau, Isabelle, Etherton, T.D.
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Specific binding sites for porcine somatotropin (pST) have been identified in pig liver microsomal membranes. Little information, however, is available about the size and number of ST receptor (ST-R) forms present. Therefore, the present study was conducted to characterize ST-R in pig liver using two approaches.
Louveau, Isabelle, Etherton, T.D.
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International Journal of Peptide and Protein Research, 1981
Two thrombin fragments of reduced carbamidomethylated human somatotropin containing the full primary structure of the native hormone (residues 1–134 and 135–191) were shown to give a recombinant with the same receptor‐binding activity as reduced‐carbamidomethylated somatotropin as tested on rabbit liver and mammary gland membranes.
L, Gràf, C H, Cheng, C H, Li
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Two thrombin fragments of reduced carbamidomethylated human somatotropin containing the full primary structure of the native hormone (residues 1–134 and 135–191) were shown to give a recombinant with the same receptor‐binding activity as reduced‐carbamidomethylated somatotropin as tested on rabbit liver and mammary gland membranes.
L, Gràf, C H, Cheng, C H, Li
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Bulletin of Experimental Biology and Medicine, 1997
Peculiarities of cell and tissue distribution of somatotropin receptors in liver cells of male rats and intact, pregnant, and estrogenized female rats is studied using an indirect immunohistochemical method. Experiments reveal equal and positively regulated by female hormones expression of somatotropin receptors in all hepatocytes.
A. N. Orlova +2 more
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Peculiarities of cell and tissue distribution of somatotropin receptors in liver cells of male rats and intact, pregnant, and estrogenized female rats is studied using an indirect immunohistochemical method. Experiments reveal equal and positively regulated by female hormones expression of somatotropin receptors in all hepatocytes.
A. N. Orlova +2 more
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