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Cyclic ADP-ribose recently has been suggested to be an important intracellular signal for insulin secretion. CD38, which was originally isolated from human lymphocytes as a surface marker, is active in the synthesis of cyclic ADP-ribose. We report here the cloning of a rat CD38-homologous protein (CD38H) which is expressed in pancreatic islets. The deduced amino acid sequence shows that rat CD38H is a protein of 303 amino acids (M(r), 34.4 kD) and contains one possible membrane-spanning domain, consistent with a type II transmembrane glycoprotein. The overall identity and similarity of the amino acid sequences between the human CD38 and the rat CD38H are 58% and 76%, respectively. RNA blot analysis showed a strong signal of 3.4 kb in rat brain, duodenum, and heart. CD38H also is shown to be expressed in pancreatic islets by the RT-PCR procedure, but its expression is not significantly different in Wistar and GK rats, a genetic model of non-insulin-dependent diabetes mellitus. The presence of rat CD38H in the pancreatic islets suggests that CD38H may be involved in insulin secretion by synthesizing cADP-ribose.

Original publication




Journal article


Biochemical and biophysical research communications

Publication Date





629 - 636


Department of Metabolism and Clinical Nutrition, Kyoto University Faculty of Medicine, Japan.


Islets of Langerhans, Brain, Lymphocytes, Animals, Rats, Inbred Strains, Humans, Mice, Rats, Rats, Wistar, Aplysia, ADP-ribosyl Cyclase, Adenosine Diphosphate Ribose, Cyclic ADP-Ribose, Membrane Glycoproteins, RNA, Messenger, DNA Primers, Antigens, Differentiation, Antigens, CD, Polymerase Chain Reaction, Species Specificity, Gene Expression, Amino Acid Sequence, Base Sequence, Sequence Homology, Amino Acid, Molecular Sequence Data, Male, Antigens, CD38