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Cited by 254

The DOI matches its Crossref record.

Insulin-Resistant Diabetes Due to a Point Mutation That Prevents Insulin Proreceptor Processing

Yoshimasa, Yasunao, Seino, Susumu, Whittaker, Jonathan, Kakehi, Takako, Kosaki, Atsushi, Kuzuya, Hideshi, Imura, Hiroo, Bell, Graeme I., Steiner, Donald F.·1988·Science
DOI 10.1126/science.3283938
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Abstract

A point mutation in the human insulin receptor gene in a patient with type A insulin resistance alters the amino acid sequence within the tetrabasic processing site of the proreceptor molecule from Arg-Lys-Arg-Arg to Arg-Lys-Arg-Ser. Epstein-Barr virus-transformed lymphocytes from this patient synthesize an insulin receptor precursor that is normally glycosylated and inserted into the plasma membrane but is not cleaved to mature α and β subunits. Insulin binding to these cells is severely reduced but can be increased about fivefold by gentle treatment with trypsin, accompanied by the appearance of normal α subunits. These results indicate that proteolysis of the proreceptor is necessary for its normal full insulin-binding sensitivity and signal-transducing activity and that a cellular protease that is more stringent in its specificity than trypsin is required to process the receptor precursor.

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Metadata

Authors
Yoshimasa, Y., Seino, S., Whittaker, J., Kakehi, T., Kosaki, A., Kuzuya, H., Imura, H., Bell, G. I., & Steiner, D. F.
Venue
Science
Publisher
American Association for the Advancement of Science (AAAS)
Published
1988-05-06
Volume
240
Issue
4853
Pages
784-787
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
DOI
10.1126/science.3283938
OpenAlex
W2065322825
Cited by
254
References
0
FWCI
11.18
Type
journal article
Language
en
Open access
closed

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