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S A Metz
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Articles

Stimulation by prostaglandin E 2 of a high-affinity GTPase in the secretory granules of normal rat and human pancreatic islets

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A Kowluru, S A Metz
Journal: Biochemical Journal
Biochem J (1994) 297 (2): 399–406.
https://doi.org/10.1042/bj2970399
Published: 15 January 1994
View articletitled, Stimulation by prostaglandin E 2 of a high-affinity GTPase in the secretory granules of normal rat and human pancreatic islets
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Articles

Modulation of insulin secretion from normal rat islets by inhibitors of the post-translational modifications of GTP-binding proteins

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S A Metz, M E Rabaglia, J B Stock, A Kowluru
Journal: Biochemical Journal
Biochem J (1993) 295 (1): 31–40.
https://doi.org/10.1042/bj2950031
Published: 01 October 1993
View articletitled, Modulation of insulin secretion from normal rat islets by inhibitors of the post-translational modifications of GTP-binding proteins
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Articles

Stimulation of insulin release by phospholipase D. A potential role for endogenous phosphatidic acid in pancreatic islet function

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S A Metz, M Dunlop
Journal: Biochemical Journal
Biochem J (1990) 270 (2): 427–435.
https://doi.org/10.1042/bj2700427
Published: 01 September 1990
View articletitled, Stimulation of insulin release by phospholipase D. A potential role for endogenous phosphatidic acid in pancreatic islet function
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Articles

Metabolism of lysophospholipids in intact rat islets. The insulin secretagogue p -hydroxymercuribenzoic acid impairs lysophosphatidylcholine catabolism and permits its accumulation

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S A Metz
Journal: Biochemical Journal
Biochem J (1987) 241 (3): 863–869.
https://doi.org/10.1042/bj2410863
Published: 01 February 1987
View articletitled, Metabolism of lysophospholipids in intact rat islets. The insulin secretagogue p -hydroxymercuribenzoic acid impairs lysophosphatidylcholine catabolism and permits its accumulation
Open the PDF for Metabolism of lysophospholipids in intact rat islets. The insulin secretagogue p -hydroxymercuribenzoic acid impairs lysophosphatidylcholine catabolism and permits its accumulation in another window