Transglutaminase-catalyzed incorporation of [2,5-3H]histamine into a Mr 84000 particulate protein in pancreatic islets.
Rat pancreatic islet homogenates catalyze the incorporation of [2,5-3H]histamine into endogenous proteins recovered in both the stacking gel and a Mr 84000 protein separated by polyacrylamide electrophoresis. The labelling of these proteins represents a Ca2+-dependent process inhibited by glycine methylester, but not sarcosine methylester, and enhanced after preincubation of the islets at a high concentration of D-glucose. Although transglutaminase activity is found in both soluble and particulate subcellular fractions, the endogenous transglutaminase substrates were located mainly in particulate, possibly membrane-associated, material.
Gomis
R
R
Endocrinology and Diabetes Unit, Hospital Clinic, Barcelona University, Spain.
Casanovas
A
A
Malaisse
W J
WJ
D000818:Animals; D005947:Glucose / Q000494:pharmacology; D006632:Histamine / Q000378:metabolism*; D066298:In Vitro Techniques; D007515:Islets of Langerhans / Q000187:drug effects / Q000378:metabolism*; D008970:Molecular Weight; D011506:Proteins / Q000378:metabolism; D051381:Rats; D013347:Subcellular Fractions / Q000378:metabolism; D013379:Substrate Specificity; D011503:Transglutaminases / Q000378:metabolism*
D011506:Proteins; D006632:Histamine; D011503:Transglutaminases; D005947:Glucose