Processing of pro-islet amyloid polypeptide (proIAPP) by the prohormone convertase PC2

Michael K. Badman; Kathleen I.J. Shennan; Joanne L. Jermany; Kevin Docherty; Anne Clark

doi:10.1016/0014-5793(95)01460-8

Processing of pro-islet amyloid polypeptide (proIAPP) by the prohormone convertase PC2

Michael K. Badman, Kathleen I.J. Shennan, Joanne L. Jermany, Kevin Docherty^*, Anne Clark

^*Corresponding author for this work

Medical Sciences

Research output: Contribution to journal › Article › peer-review

63 Citations (Scopus)

Abstract

Islet amyloid polypeptide (IAPP), 'amylin', is the component peptide of islet amyloid formed in Type 2 diabetes. IAPP is expressed in islet β-cells and is derived from a larger precursor, proIAPP, by proteolysis. An in vitro translation/ translocation system was used to separately examine processing of human proIAPP by the β-cell endopeptidases PC2, PC3 or furin. ProIAPP was converted to mature IAPP by PC2 but there was little conversion by furin or PC3. These data are consistent with processing of proIAPP in β-cell secretory granules. Abnormal cellular proteolysis associated with type 2 diabetes could contribute to IAPP amyloidosis.

Original language	English
Pages (from-to)	227-231
Number of pages	5
Journal	FEBS LETTERS
Volume	378
Issue number	3
DOIs	https://doi.org/10.1016/0014-5793(95)01460-8
Publication status	Published - 15 Jan 1996

Keywords

Furin
Islet amyloid polypeptide
PC2
PC3
Propeptide processing
β-Cell

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1016/0014-5793(95)01460-8

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title = "Processing of pro-islet amyloid polypeptide (proIAPP) by the prohormone convertase PC2",

abstract = "Islet amyloid polypeptide (IAPP), 'amylin', is the component peptide of islet amyloid formed in Type 2 diabetes. IAPP is expressed in islet β-cells and is derived from a larger precursor, proIAPP, by proteolysis. An in vitro translation/ translocation system was used to separately examine processing of human proIAPP by the β-cell endopeptidases PC2, PC3 or furin. ProIAPP was converted to mature IAPP by PC2 but there was little conversion by furin or PC3. These data are consistent with processing of proIAPP in β-cell secretory granules. Abnormal cellular proteolysis associated with type 2 diabetes could contribute to IAPP amyloidosis.",

keywords = "Furin, Islet amyloid polypeptide, PC2, PC3, Propeptide processing, β-Cell",

author = "Badman, {Michael K.} and Shennan, {Kathleen I.J.} and Jermany, {Joanne L.} and Kevin Docherty and Anne Clark",

note = "Funding Information: Acknowledgements.{"} This work was supported by grants from the Medical Research Council, (M.K.B., K.D. and K.I.J.S.), the British Diabetic Association (A.C., K.D. and K.I.J.S.). ",

year = "1996",

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doi = "10.1016/0014-5793(95)01460-8",

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T1 - Processing of pro-islet amyloid polypeptide (proIAPP) by the prohormone convertase PC2

AU - Badman, Michael K.

AU - Shennan, Kathleen I.J.

AU - Jermany, Joanne L.

AU - Docherty, Kevin

AU - Clark, Anne

N1 - Funding Information: Acknowledgements." This work was supported by grants from the Medical Research Council, (M.K.B., K.D. and K.I.J.S.), the British Diabetic Association (A.C., K.D. and K.I.J.S.).

PY - 1996/1/15

Y1 - 1996/1/15

N2 - Islet amyloid polypeptide (IAPP), 'amylin', is the component peptide of islet amyloid formed in Type 2 diabetes. IAPP is expressed in islet β-cells and is derived from a larger precursor, proIAPP, by proteolysis. An in vitro translation/ translocation system was used to separately examine processing of human proIAPP by the β-cell endopeptidases PC2, PC3 or furin. ProIAPP was converted to mature IAPP by PC2 but there was little conversion by furin or PC3. These data are consistent with processing of proIAPP in β-cell secretory granules. Abnormal cellular proteolysis associated with type 2 diabetes could contribute to IAPP amyloidosis.

AB - Islet amyloid polypeptide (IAPP), 'amylin', is the component peptide of islet amyloid formed in Type 2 diabetes. IAPP is expressed in islet β-cells and is derived from a larger precursor, proIAPP, by proteolysis. An in vitro translation/ translocation system was used to separately examine processing of human proIAPP by the β-cell endopeptidases PC2, PC3 or furin. ProIAPP was converted to mature IAPP by PC2 but there was little conversion by furin or PC3. These data are consistent with processing of proIAPP in β-cell secretory granules. Abnormal cellular proteolysis associated with type 2 diabetes could contribute to IAPP amyloidosis.

KW - Furin

KW - Islet amyloid polypeptide

KW - PC2

KW - PC3

KW - Propeptide processing

KW - β-Cell

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DO - 10.1016/0014-5793(95)01460-8

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C2 - 8557106

AN - SCOPUS:0030064237

VL - 378

SP - 227

EP - 231

JO - FEBS Letters

JF - FEBS Letters

SN - 0014-5793

IS - 3

ER -

Processing of pro-islet amyloid polypeptide (proIAPP) by the prohormone convertase PC2

Abstract

Keywords

UN SDGs

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