Deposition of amyloid is the most constantly present alteration in the islets of Langerhans in type 2 diabetes mellitus and is also quite common in insulin-producing tumors of the pancreas and it is very likely that these two amyloids are identical. We have isolated amyloid fibrils from an insulin-secreting human tumour and purified the fibrillar protein. N-terminal amino acid sequence of the protein is unique and does not resemble insulin or its precursors. Instead it has about 50% homology with the neuropeptide CGRP (calcitonin gene related peptide).
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rdfs:comment |
Deposition of amyloid is the most constantly present alteration in the islets of Langerhans in type 2 diabetes mellitus and is also quite common in insulin-producing tumors of the pancreas and it is very likely that these two amyloids are identical. We have isolated amyloid fibrils from an insulin-secreting human tumour and purified the fibrillar protein. N-terminal amino acid sequence of the protein is unique and does not resemble insulin or its precursors. Instead it has about 50% homology with the neuropeptide CGRP (calcitonin gene related peptide).
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skos:exactMatch | |
uniprot:name |
Biochem. Biophys. Res. Commun.
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uniprot:author |
Sletten K.,
Wernstedt C.,
Westermark P.,
Wilander E.
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uniprot:date |
1986
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uniprot:pages |
827-831
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uniprot:title |
A novel peptide in the calcitonin gene related peptide family as an amyloid fibril protein in the endocrine pancreas.
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uniprot:volume |
140
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dc-term:identifier |
doi:10.1016/0006-291X(86)90708-4
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