The expression of peptide hormones in normal cells and tumour cells
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The expression of peptide hormones in normal cells and tumour cells. / Rehfeld, J. F.; Bardram, L.; Blanke, S.; Cantor, P.; Friis-Hansen, L.; Hilsted, L.; Johnsen, A. H.; Monstein, H. J.; Van Solinge, W. Wouter; Ødum, L.; Ørskov, C.
I: Acta Oncologica, Bind 30, Nr. 4, 1991, s. 429-433.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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TY - JOUR
T1 - The expression of peptide hormones in normal cells and tumour cells
AU - Rehfeld, J. F.
AU - Bardram, L.
AU - Blanke, S.
AU - Cantor, P.
AU - Friis-Hansen, L.
AU - Hilsted, L.
AU - Johnsen, A. H.
AU - Monstein, H. J.
AU - Van Solinge, W. Wouter
AU - Ødum, L.
AU - Ørskov, C.
N1 - Funding Information: This review is based on studies in the laboratory of the authors. The studies were supported by grants from the Danish Medical Research Council, the Danish Cancer Union, the Danish Biotechnology Center for Neuropeptide Research, the Alfred Benzon, Lundbeck, NOVO and Jenny Vissing foundations.
PY - 1991
Y1 - 1991
N2 - Insight in the mechanisms of peptide hormone expression has grown explosively by elucidation of gene, mRNA and. preprohor-mone structures for most hormone systems during the 1980s. in addition, information about the structure and substrate specificity of many prohormone processing enzymes is rapidly accumulating in these years. the preprohormones vary considerably in size and organization from poly- to monoprotein structures. According to the structural organization and sequence homology the hormones are grouped in families. the prohormones are processed to bioactive peptides by multiple enzymatic modifications during the intracellular transport from the rough endoplasmatic reticulum to the mature secretory granules. the modifications comprise different proteolytic cleavages and amino acid derivatizations. the same prohormone may be expressed in several different cell types that process the precursor in entirely different ways. Awareness of such cell-specific processing patterns is important for the understanding of ectopic synthesis in neuroendocrine tumours.
AB - Insight in the mechanisms of peptide hormone expression has grown explosively by elucidation of gene, mRNA and. preprohor-mone structures for most hormone systems during the 1980s. in addition, information about the structure and substrate specificity of many prohormone processing enzymes is rapidly accumulating in these years. the preprohormones vary considerably in size and organization from poly- to monoprotein structures. According to the structural organization and sequence homology the hormones are grouped in families. the prohormones are processed to bioactive peptides by multiple enzymatic modifications during the intracellular transport from the rough endoplasmatic reticulum to the mature secretory granules. the modifications comprise different proteolytic cleavages and amino acid derivatizations. the same prohormone may be expressed in several different cell types that process the precursor in entirely different ways. Awareness of such cell-specific processing patterns is important for the understanding of ectopic synthesis in neuroendocrine tumours.
KW - Bioactive peptides
KW - Biogenesis
KW - Hormone genes
KW - Peptide hormones
KW - Precursors
U2 - 10.3109/02841869109092397
DO - 10.3109/02841869109092397
M3 - Journal article
C2 - 1854500
AN - SCOPUS:0025916255
VL - 30
SP - 429
EP - 433
JO - Acta Oncologica
JF - Acta Oncologica
SN - 1100-1704
IS - 4
ER -
ID: 310765654