By I. Mollerup, T. Kornfelt, P. Oreskov, H. V. Tøttrup (auth.), Professor Pierre J. Lefèbvre M.D., Ph.D., FRCP (eds.)
Glucagon III enhances Glucagon I and II released in 1983 during this sequence as Vols. 66/I and II. those 3 volumes actually signify a "glucagon encyclopedia" and as such haven't any opponents within the clinical literature world wide. during this quantity, the newest information on glucagon molecular biology are reviewed including clinically correct details at the position of glucagon within the pathophysiology of diabetes, where of glucagon in scientific imaging or in emergency drugs. Chapters are dedicated to newly pointed out individuals of the glucagon relations comparable to glucagon-like peptide-1 (GLP-1) and oxyntomodulin. Glucagon III is a entire assessment of all details released in this vital hormone due to the fact that 1983 and is the reference publication at the subject.
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Extra info for Glucagon III
Human GLP-l and GIP-2 share 35% identity and 68% homology and display 48% and 38% identity with glucagon, respectively. The close homologies between glucagon and GLPs SP 20 30 22 30 20 30 20 --- AM INOTP GLUCAGON 30 29 29 29 29 IP GLP 5 34 anglerfish II II chicken IP1 6 6 24 GLP-1 37 IP2 37 13 37 13 GLP-2 ~ rat ~ human 33 33 Fig. 2. Schematic representation of the glucagon precursor, preproglucagon, from anglerfish, chicken, rat and human. Anglerfish possess two nonallelic glucagon genes encoding two glucagon precursors.
The A domain is responsible for both enhancer activity and the mediation of the insulin effects on glucagon gene expression (PHILIPPE et al. 1995; PHILIPPE 1989, 1991a; CHEN et al. 1989a). The A domain binds two complexes that are present in all islet cell phenotypes but not in other cell types. One of the two complexes also interacts with the proximal upstream promoter element Gl. Both G2 and G3 function as islet cell-specific enhancers and, at least as assayed in transformed islet cell lines, are unable to restrict by themselves glucagon gene expression to the A cells relative to the other islet cell phenotypes (PHILIPPE et al.
These observations may be explained by the nature of the nucleotides surrounding the CRE. Several uncharacterized proteins interact with the flanking motif (TCATT) of the glucagon CRE and mutations of this motif enhance the response of the cAMP analogs. These results suggest that the flanking motif-binding proteins negatively modulate the ability of the CRE-binding protein (CREB) to mediate protein kinase A-stimulated transcription. The CRE may be the target for additional sgnals which regulate glucagon gene transcriptional (SCHWANINGER et al.
Glucagon III by I. Mollerup, T. Kornfelt, P. Oreskov, H. V. Tøttrup (auth.), Professor Pierre J. Lefèbvre M.D., Ph.D., FRCP (eds.)